IndraLab

Statements


USP38 affects TBK1
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USP38 inhibits TBK1.
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USP38 inhibits TBK1. 10 / 16
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"Furthermore, we found that USP38 expression reduced TBK1 protein, but not TBK1 mRNA, after VSV infection compared with 293T cells transfected with the empty vector (EV) ( Figures 4 H and S3 D)."

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"These results suggest that USP38 specifically degrades the active form (p-TBK1) of TBK1 after viral infection.It has been documented that TBK1 undergoes both K48-linked and K63-linked ubiquitination a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Since the K48-linked ubiquitination of TBK1 is regulated by NLRP4, DTX4, or TRIP proteins ( Cui et al., 2012; Zhang et al., 2012 ), we first tested whether USP38 promotes TBK1 degradation by stabilizi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"The results indicate that USP38 may promote the proteasomal degradation of p-TBK1 instead of the total TBK1."

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"Interestingly, we found that the USP38 (C545A/H857A) mutant failed to degrade TBK1, indicating that the deubiquitinating activity of USP38 is required to degrade TBK1 ( Figure 5 C)."

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"Amlexanox protects USP38 mediated cardiac remodeling, decreasing the protein expression of USP38-mediated TBK1/AKT-GSK3β/mTOR signaling pathway [158]."

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"USP38 deficiency abrogated the degradation of TBK1 and increased the production of type I IFN."

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"Similarly, USP38 negatively regulates IFN-I signaling by targeting the active form of TBK1 for degradation in vitro and in vivo (101)."

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"To determine the specificity of the USP38-mediated TBK1 degradation, we used other USP family members USP3 and USP13 as a control, and we found that USP38, but not USP3 or USP13, induced TBK1 degradat[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"However, the mRNA level of TBK1 remained unchanged ( Figure 4 A), suggesting that USP38 causes TBK1 protein degradation."
USP38 inhibits TBK1-K670R. 1 / 1
| 1

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"We further showed that neither USP38 nor TRIP can degrade TBK1 (K670R) mutants ( Figures 5 J and S4 G), suggesting that Lys670 on TBK1 is critical for controlling TBK1 stability."
USP38 binds TBK1.
| 9 8
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"To examine the interaction between USP38 and TBK1 under physiological conditions, we infected 293T cells, THP-1 cells, or PBMCs with VSV-EGFP, and we found that the interaction between USP38 and TBK1 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"After viral infection, the interaction between USP38 and TBK1 was significantly increased in all three cell types ( Figures 3 D–3F)."

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"To substantiate these findings, we specifically knocked down NLRP4 and found that the interaction between USP38 and TBK1 was markedly attenuated ( Figure 6 F)."

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"Furthermore, we demonstrated that the dynamic interaction between USP38 and TBK1 was totally abrogated in NLRP4 small interfering RNA (siRNA)-treated THP-1 cells after viral infection ( Figure 6 G)."

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"These results suggest that USP38, TRIP, and DTX4 may bind to TBK1 in an NLRP4-dependent manner."

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"Mechanistically, USP38 interacts with TANK-binding kinase 1 (TBK1) and removes K48-linked polyubiquitination of TBK1, stabilizing p-TBK1 and promoting the activation of its downstream mediators."

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"As TBK1 is an upstream component of the Akt signaling pathway, and the TBK1-Akt signaling cascade is known to be significant in pathological cardiac remodeling4, we conducted a comprehensive analysis to explore the association between USP38 and TBK1."

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"Conversely, the K48-linked polyubiquitination level of TBK1 was obviously decreased after AdUSP38 transduced NRCMs (Figure 7B), These findings strongly indicate that USP38 interacts with and deubiquitinates TBK1 in hypertrophied cardiomyocytes."

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"co-immunoprecipitation suggests an interaction between USP38 and TBK1."
USP38 binds TBK1. 8 / 8
| 8

sparser
"Finally, we examined the interaction of USP38 with TBK1 by co-immunoprecipitation (F xref g.  xref I, J)."

sparser
"Consistent with previous findings, this study revealed a significant increase in TBK1, AKT and CaMKII phosphorylation levels after pressure overload-induced HF, and these adverse effects were mitigated in USP38 knockout mice. co-immunoprecipitation suggests an interaction between USP38 and TBK1."

sparser
"We subsequently performed Co-IP and identified that USP38 antibody efficiently precipitated TBK1 in NRCMs, and reverse Co-IP further confirmed that TBK1 interacted with USP38(Figure xref D)."

sparser
"Moreover, the interaction of USP38 with TBK1 was obviously enhanced following Ang II administration(Figure xref E)."

sparser
"Consistent with our in vitro findings, the interaction between USP38 and TBK1 was observed in the heart tissue collected from wild-type mice(Figure xref G)."

sparser
"These results suggest that USP38 interacts with TBK1 in NRCMs and myocardial tissues."

sparser
"In the present study, we validated the interaction of USP38 with TBK1 in heart tissue and NRCMs."

sparser
"USP38 interacts with TBK1 and removes K48-linked polyubiquitination chain."
USP38 ubiquitinates TBK1.
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USP38 ubiquitinates TBK1. 3 / 3
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"The Ub-specific protease 38 (USP38), TRAF-interacting protein (TRIP), Nod-like receptor (NLR) family pyrin domain containing 4 (NLRP4), and DTX4 complex polyubiquitinates TBK1, thereby degrading it to limit the virus-induced IFN-I signaling pathway (Cui et al., 2012)."

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"To determine how USP38 regulates TBK1 ubiquitination, we transfected 293T cells with FLAG-TBK1, Myc-USP38, HA-tagged K48-linked ubiquitin (K48-Ub), or K63-linked ubiquitin (K63-Ub), and we found that [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP38 overexpression promotes polyubiquitination of TBK1, resulting in the stabilization of p-TBK1 and activation of AKT signaling pathway in Ang II-induced myocardial hypertrophy mouse model."
USP38 decreases the amount of TBK1.
| 3
USP38 decreases the amount of TBK1. 3 / 3
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"Conversely, USP38 knockdown in THP-1 cells increased endogenous TBK1 protein levels in cells infected with VSV-EGFP or transfected with IC poly(I:C), but not in uninfected cells ( Figures 4 I and S3 E[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"To understand the molecular mechanisms of USP38 action, we show that USP38 specifically interacts with active TBK1 after viral infection and inhibits type I IFN signaling at the level of TBK1."

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"As shown in Figure 8A and 8B, USP38 deficiency significantly decreased p-TBK1 level after AB surgery, whereas USP38 overexpression dramatically increased the level of p-TBK1."
USP38 activates TBK1.
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USP38 activates TBK1. 3 / 3
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"Meanwhile, we found that knockdown of USP38 accelerated the degradation of p-TBK1 induced by CHX, while USP38 overexpression delayed its degradation (Figure 8I and 8J)."

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"USP38 prevents the proteasomal degradation of p-TBK1."

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"Mechanistically, USP38 prevents the proteasomal degradation of p-TBK1, thus activating the downstream Akt-GSK3β/mTOR signaling pathways."
USP38 increases the amount of TBK1.
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USP38 increases the amount of TBK1. 2 / 2
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"Consistent with in vivo observations, USP38 knockdown mitigated the Ang II-caused increase of p-TBK1 level, whereas overexpression of USP38 further increased the level of p-TBK1 (Figure 8C and 8D)."

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"As shown in Figure 8A and 8B, USP38 deficiency significantly decreased p-TBK1 level after AB surgery, whereas USP38 overexpression dramatically increased the level of p-TBK1."
USP38 deubiquitinates TBK1.
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USP38 deubiquitinates TBK1. 2 / 2
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"Here we report that <span class="match term0">USP38</span> negatively regulates type I IFN signaling by targeting the active form of <span class="match term1">TBK1</span> for degradation in vitro and in vivo"

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"Conversely, the K48-linked polyubiquitination level of TBK1 was obviously decreased after AdUSP38 transduced NRCMs (Figure 7B), These findings strongly indicate that USP38 interacts with and deubiquitinates TBK1 in hypertrophied cardiomyocytes."
ADAR affects USP38
3 | 19 10
ADAR binds USP38.
3 | 6 10
USP38 binds ADAR. 10 / 10
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sparser
"Subsequently, we used the online web tool DMFold () to predict the structure of the USP38 and ADAR complex."

sparser
"DMFold predicted five structures for the USP38ADAR complex."

sparser
"These findings demonstrate that the interaction between USP38 and ADAR is mediated through their C-terminal enzymatic catalytic regions."

sparser
"Structural predictions suggest that ADAR and USP38 interact within their enzymatic activity domains, raising the question of whether ADAR induces conformational changes in USP38 to modulate its enzymatic activity."

sparser
"More importantly, our results provide a rationale for targeting the ADARUSP38 axis for the treatment of ESCC."

sparser
"To further confirm the interaction between USP38 and ADAR, we coexpressed USP38 and ADAR proteins tagged with different tags in HEK293T cells and then analyzed the interaction between USP38 and ADAR through IP."

sparser
"Endogenous coimmunoprecipitation results also showed that stable protein complexes between ADAR and USP38 were readily detected ( xref , B and C )."

sparser
"These results indicate that USP38 and ADAR interact in the cell nucleus."

sparser
"The interaction between USP38 and ADAR depends on its enzymatic active region."

sparser
"To clarify the structural domains involved in the USP38 and ADAR interaction, a series of deletion mutants of USP38 (WT (1-1042AA), N-term (1-400AA), C-term (401-1042AA)) and ADAR (WT (1-931AA), ΔZD (deletion of 1-71AA), ΔRBD (deletion of 207-499AA), and ΔDD (deletion of 591-926AA)) were used for IP analyses."
3 | 6

No evidence text available

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"To further confirm the interaction between USP38 and ADAR, we coexpressed USP38 and ADAR proteins tagged with different tags in HEK293T cells and then analyzed the interaction between USP38 and ADAR through IP."

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"The interaction between USP38 and ADAR depends on its enzymatic active region."

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"To clarify the structural domains involved in the USP38 and ADAR interaction, a series of deletion mutants of USP38 (WT (1-1042AA), N-term (1-400AA), C-term (401-1042AA)) and ADAR (WT (1-931AA), ΔZD (deletion of 1-71AA), ΔRBD (deletion of 207-499AA), and ΔDD (deletion of 591-926AA)) were used for IP analyses."

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"Subsequently, we used the online web tool DMFold (https://zhanggroup.org/DMFold/) to predict the structure of the USP38 and ADAR complex."

reach
"DMFold predicted five structures for the USP38ADAR complex."

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"These findings demonstrate that the interaction between USP38 and ADAR is mediated through their C-terminal enzymatic catalytic regions."

No evidence text available

No evidence text available
ADAR ubiquitinates USP38.
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ADAR ubiquitinates USP38. 6 / 6
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"ADAR promotes USP38 auto-deubiquitylation and stabilization in an RNA editing-independent manner in esophageal squamous cell carcinoma."

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"Mechanistically, ADAR interacts with USP38 to enhance USP38 protein stability and promote USP38 auto-deubiquitylation."

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"We asked whether ADAR also plays a role in the auto-deubiquitylation of USP38."

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"These results indicate that ADAR promotes the auto-deubiquitylation of USP38 and thereby stabilizes USP38 through interaction with USP38."

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"In this study, we demonstrate that ADAR enhances the auto-deubiquitylation and stabilization of USP38."

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"Mechanistically, we demonstrate that ADAR enhances USP38 auto-deubiquitylation to increase USP38 protein stability and upregulate USP38, thereby affecting cell proliferation and growth."
ADAR activates USP38.
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ADAR activates USP38. 6 / 6
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"Structural predictions suggest that ADAR and USP38 interact within their enzymatic activity domains, raising the question of whether ADAR induces conformational changes in USP38 to modulate its enzymatic activity."

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"ADAR can enhance the protein stability of USP38 and upregulate USP38."

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"In conclusion, we show that ADAR enhances USP38 protein stability by interacting with it, and overexpression of USP38 rescues the inhibitory effect of ADAR knockdown on ESCC cell proliferation."

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"ADAR enhances the stability of USP38 protein."

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"The results of nucleo-cytoplasmic separation also indicated that overexpression of ADAR enhanced the accumulation of USP38 in the nucleus (Fig. 3E)."

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"Indeed, protein stability analysis results showed that, compared to control, overexpression of ADAR enhanced USP38 protein stability (Fig. 3H)."
ADAR deubiquitinates USP38.
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ADAR leads to the deubiquitination of USP38-C454A. 1 / 1
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"We analyzed the effect of overexpressing ADAR on the auto-deubiquitylation of USP38 through IP, and the results showed that overexpressing ADAR reduced the ubiquitination of USP38 C454A (Fig. 3I)."
USP38 affects TG
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TG binds USP38. 10 / 24
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sparser
"Next, we observed that left atrial weight/tibia length was heavily increased in USP38-TG group compared with NTG group after AB surgery (see xref , xref )."

sparser
"Additionally, the enlargement of LAD was observed in USP38-TG group compared with NTG group under AB stimulation (Figure xref )."

sparser
"Conversely, LVEF and LVFS showed further reduction in USP38-TG AB group compared with NTG AB group (see xref , xref xref xref )."

sparser
"The USP38-TG group showed a more evident atrial electrical remodelling after AB surgery compared with the NTG group."

sparser
"Specifically, after AB surgery, the levels of calcium-handling proteins, increased p-RYR2 and p-PLB and decreased SERCA2a, were observed in the USP38-TG group compared with the NTG group (Figure xref )."

sparser
"Conversely, inflammation also was exacerbated after AB in USP38-TG group by increased levels of serum inflammatory cytokines and atrial tissue inflammatory marker proteins and transcription (Figure xref )."

sparser
"USP38-TG mice were intraperitoneally injected with Amlexanox (an inhibitor of TBK1) or DMSO 2 weeks after AB surgery(Figure xref A)."

sparser
"To further explore whether USP38 is involved in AB-induced AF through NF-κB, we administered intra-peritoneal injection of PDTC (Sigma, USA) 2 weeks after AB surgery in USP38-TG mice (Figure xref ), which has been shown to inhibit NF-κB activation."

sparser
"Notably, the detrimental effects in USP38-TG mice were significantly prevented by Amlexanox, as evidenced by reduced HW, HW/BW, HW/TL and LW/BW ratio(Figure xref B), improved cardiac function(Figure xref C), alleviated hypertrophic degree(Figure xref D), ameliorated myocardial fibrosis(Figure xref E), and decreased the protein expression of TBK1/Akt-GSK3β/mTOR signaling pathway(Figure xref F)in Amlexanox treated-USP38-TG mice compared with USP38-TG DMSO mice."

sparser
"Previous studies have demonstrated that atrial structural and electrical remodelling plays a fundamental role in the trigger and perpetuation of AF. xref Atrial structural remodelling is usually manifested atrial enlargement and atrial fibrosis, causing delayed conduction and local heterogeneous conduction, which creates the substrate for AF. xref It is worth noting that chronic pressure overload promotes collagen synthesis, causing excessive deposition of extra-cellular matrix proteins in the atrial tissue. xref Moreover, the atrial diameter increases under pressure overload stimulation, xref and the atrial enlargement in patients is associated with the occurrence of AF. xref In this study, we noticed that pressure overload caused the enlargement of LAD was more obvious in USP38-TG mice compared with USP38-NTG mice."
USP38 affects MYC
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USP38 increases the amount of MYC.
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USP38 increases the amount of MYC. 7 / 7
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"These data suggest that USP38 can enhance c-Myc levels, through a DUB-independent mechanism.To further verify the impact of USP38 on c-Myc, endogenous USP38 was knocked down in the A549 cells with two[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Taken together, these data strongly indicate that USP38 is a novel positive regulator of c-Myc.To determine the mechanism by which USP38 increases c-Myc protein levels, USP38 was co-expressed with c-M[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"We found that USP38 no longer increased the levels of c-Myc in the presence of the proteasome inhibitor MG132 ( Fig. 2 A), suggesting that USP38 prevents proteasomal degradation of c-Myc."

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"As expected, knockdown of USP38 failed to reduce the c-Myc levels once the cells were treated with MG132 ( Fig. 2 B)."

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"Together, these data imply that USP38 enhances c-Myc levels by inhibiting polyubiquitination and degradation of c-Myc.Given that USP38 can inhibit the degradation of c-Myc, we next determined the effe[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"As was expected, ectopic expression of USP38 indeed promoted the expression of c-Myc target genes, such as HK2, PKM2, and LDHA ( Fig. 1 E and F)."

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"Besides, When USP38 was co-transfected with c-Myc in HEK293 T cells, the levels of c-Myc were increased by USP38 in a dose-dependent manner ( Fig. 1 B, lanes 1–3)."
Mutated USP38 increases the amount of MYC. 2 / 2
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"Both wild-type and DUB-inactive mutant of USP38 dramatically increased endogenous protein levels of c-Myc ( Fig. 1 D)."

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"Since the enzyme-inactive mutant of USP38 can still increase c-Myc levels ( Fig. 1 B and D), it is not surprising that USP38 mutant can also abolish FBW7α-mediated degradation of c-Myc ( Fig. 5 B)."
USP38-C454A increases the amount of MYC. 1 / 1
| 1

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"Meanwhile, the DUB-inactive mutant of USP38 (C454A/H857A) was still able to increase c-Myc levels ( Fig. 1 B, lanes 4–6)."
USP38-H857A increases the amount of MYC. 1 / 1
| 1

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"Meanwhile, the DUB-inactive mutant of USP38 (C454A/H857A) was still able to increase c-Myc levels ( Fig. 1 B, lanes 4–6)."
USP38 activates MYC.
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USP38 activates MYC. 6 / 6
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"Functionally, USP38 promotes cell proliferation in a c-Myc dependent manner."

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"Surprisingly, we found that knockdown of USP38 also notably decreased the c-Myc protein levels ( Fig. 1 A)."

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"We found that USP38 no longer increased the levels of c-Myc in the presence of the proteasome inhibitor MG132 ( Fig. 2 A), suggesting that USP38 prevents proteasomal degradation of c-Myc."

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"In addition, USP38 has been shown to promote cell proliferation by stabilizing LSD1 or c-Myc proteins27, 28."

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"USP38 is able to enhance the stability of c-Myc by antagonizing the function of FBW7α."

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"In addition, USP38 promotes lung cancer cell proliferation by stabilizing c-Myc (14)."
Mutated USP38 activates MYC. 1 / 1
| 1

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"Since the enzyme-inactive mutant of USP38 can still increase c-Myc levels ( Fig. 1 B and D), it is not surprising that USP38 mutant can also abolish FBW7α-mediated degradation of c-Myc ( Fig. 5 B)."
USP38 deubiquitinates MYC.
1 | 1
USP38 leads to the deubiquitination of MYC on D2. 1 / 1
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"The results showed that USP38 greatly decreased the polyubiquitination of c-Myc ( Fig. 2 D)."
USP38 deubiquitinates MYC. 1 / 1
1 |

"<span class="match term0">USP38</span> can inhibit the polyubiquitination of c-<span class="match term1">Myc</span>, thereby increasing c-<span class="match term1">Myc</span> stability"
USP38 inhibits MYC.
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USP38 inhibits MYC. 1 / 1
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"However, ectopic expression of USP38 abrogated FBW7α-mediated degradation of c-Myc ( Fig. 5 A)."
USP38 decreases the amount of MYC.
| 1
USP38 decreases the amount of MYC. 1 / 1
| 1

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"Moreover, reduction of c-Myc levels caused by FBW7α overexpression could be restored by the simultaneous overexpression of USP38 in both A549 and Hela cells ( Fig. 5 C), indicating that USP38 can elim[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 affects ADAR
3 | 8 10
USP38 binds ADAR.
3 | 6 10
USP38 binds ADAR. 10 / 10
| 10

sparser
"Subsequently, we used the online web tool DMFold () to predict the structure of the USP38 and ADAR complex."

sparser
"DMFold predicted five structures for the USP38ADAR complex."

sparser
"These findings demonstrate that the interaction between USP38 and ADAR is mediated through their C-terminal enzymatic catalytic regions."

sparser
"Structural predictions suggest that ADAR and USP38 interact within their enzymatic activity domains, raising the question of whether ADAR induces conformational changes in USP38 to modulate its enzymatic activity."

sparser
"More importantly, our results provide a rationale for targeting the ADARUSP38 axis for the treatment of ESCC."

sparser
"To further confirm the interaction between USP38 and ADAR, we coexpressed USP38 and ADAR proteins tagged with different tags in HEK293T cells and then analyzed the interaction between USP38 and ADAR through IP."

sparser
"Endogenous coimmunoprecipitation results also showed that stable protein complexes between ADAR and USP38 were readily detected ( xref , B and C )."

sparser
"These results indicate that USP38 and ADAR interact in the cell nucleus."

sparser
"The interaction between USP38 and ADAR depends on its enzymatic active region."

sparser
"To clarify the structural domains involved in the USP38 and ADAR interaction, a series of deletion mutants of USP38 (WT (1-1042AA), N-term (1-400AA), C-term (401-1042AA)) and ADAR (WT (1-931AA), ΔZD (deletion of 1-71AA), ΔRBD (deletion of 207-499AA), and ΔDD (deletion of 591-926AA)) were used for IP analyses."
3 | 6

No evidence text available

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"To further confirm the interaction between USP38 and ADAR, we coexpressed USP38 and ADAR proteins tagged with different tags in HEK293T cells and then analyzed the interaction between USP38 and ADAR through IP."

reach
"The interaction between USP38 and ADAR depends on its enzymatic active region."

reach
"To clarify the structural domains involved in the USP38 and ADAR interaction, a series of deletion mutants of USP38 (WT (1-1042AA), N-term (1-400AA), C-term (401-1042AA)) and ADAR (WT (1-931AA), ΔZD (deletion of 1-71AA), ΔRBD (deletion of 207-499AA), and ΔDD (deletion of 591-926AA)) were used for IP analyses."

reach
"Subsequently, we used the online web tool DMFold (https://zhanggroup.org/DMFold/) to predict the structure of the USP38 and ADAR complex."

reach
"DMFold predicted five structures for the USP38ADAR complex."

reach
"These findings demonstrate that the interaction between USP38 and ADAR is mediated through their C-terminal enzymatic catalytic regions."

No evidence text available

No evidence text available
USP38 activates ADAR.
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USP38 activates ADAR. 2 / 2
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"We then detected whether USP38 could rescue the inhibitory effect of ADAR knockdown on esophageal squamous carcinoma cells proliferation through CCK-8 and colony formation assays."

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"In conclusion, we show that ADAR enhances USP38 protein stability by interacting with it, and overexpression of USP38 rescues the inhibitory effect of ADAR knockdown on ESCC cell proliferation."
USP38 affects BIRC5
1 | 17
USP38 binds BIRC5.
1 | 6
1 | 6

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"The interaction between USP38 and BIRC5 was explored by using co-immunoprecipitation (Co-IP) and the ubiquitination level and stability of BIRC5 were examined by using Western blot."

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"At the molecular level, USP38 interacts with and stabilizes BIRC5 by decreasing its ubiquitination."

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"USP38 interacted with and deubiquitinated BIRC5 in IEC-6 cells."

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"These results suggest that USP38 interacts with and deubiquitinates BIRC5 to stabilize it in IEC-6 cells."

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"USP35/USP38 interacted with and deubiquitinated survivin."

No evidence text available

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"Our work revealed that USP35 and its orthologous gene USP38 interacted with and deubiquitinated survivin, which in turn stabilized the survivin protein."
USP38 deubiquitinates BIRC5.
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USP38 deubiquitinates BIRC5. 5 / 5
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"USP38 interacted with and deubiquitinated BIRC5 in IEC-6 cells."

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"These results suggest that USP38 interacts with and deubiquitinates BIRC5 to stabilize it in IEC-6 cells."

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"In addition, USP38 interacted with survivin and promoted the deubiquitination of survivin ( Fig. S1D and Fig. S1E )."

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"USP35/USP38 interacted with and deubiquitinated survivin."

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"Our work revealed that USP35 and its orthologous gene USP38 interacted with and deubiquitinated survivin, which in turn stabilized the survivin protein."
USP38 increases the amount of BIRC5.
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USP38 increases the amount of BIRC5. 3 / 3
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"Overexpression of USP38 also upregulated the endogenous survivin protein level ( Fig. S1B )."

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"qPCR data confirmed that incubation of BIRC5-deficient USP38-overexpressing BM-MSC-EVs could efficiently increase USP38 and reduce BIRC5 expression in OGD/R-treated IEC-6 cells (Figure 4B)."

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"Indeed, we found that USP38 are able to increase the protein level of survivin during our screen ( Fig. S1A )."
USP38 activates BIRC5.
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USP38 activates BIRC5. 2 / 2
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"USP38 protected IEC-6 cells from OGD/R-induced injury by stabilizing BIRC5."

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"Western blot data revealed that USP38 significantly enhanced the stability of BIRC5 (Figure 3C and D)."
USP38 decreases the amount of BIRC5.
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USP38 decreases the amount of BIRC5. 1 / 1
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"Co-IP assay data showed that USP38 can interact with BIRC5 (Figure 3A) and the overexpression of USP38 in IEC-6 cells significantly decreased the ubiquitination level of BIRC5 (Figure 3B)."
TBK1 affects USP38
| 10 8
TBK1 binds USP38.
| 9 8
| 9

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"To examine the interaction between USP38 and TBK1 under physiological conditions, we infected 293T cells, THP-1 cells, or PBMCs with VSV-EGFP, and we found that the interaction between USP38 and TBK1 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"After viral infection, the interaction between USP38 and TBK1 was significantly increased in all three cell types ( Figures 3 D–3F)."

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"To substantiate these findings, we specifically knocked down NLRP4 and found that the interaction between USP38 and TBK1 was markedly attenuated ( Figure 6 F)."

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"Furthermore, we demonstrated that the dynamic interaction between USP38 and TBK1 was totally abrogated in NLRP4 small interfering RNA (siRNA)-treated THP-1 cells after viral infection ( Figure 6 G)."

reach
"These results suggest that USP38, TRIP, and DTX4 may bind to TBK1 in an NLRP4-dependent manner."

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"Mechanistically, USP38 interacts with TANK-binding kinase 1 (TBK1) and removes K48-linked polyubiquitination of TBK1, stabilizing p-TBK1 and promoting the activation of its downstream mediators."

reach
"As TBK1 is an upstream component of the Akt signaling pathway, and the TBK1-Akt signaling cascade is known to be significant in pathological cardiac remodeling4, we conducted a comprehensive analysis to explore the association between USP38 and TBK1."

reach
"Conversely, the K48-linked polyubiquitination level of TBK1 was obviously decreased after AdUSP38 transduced NRCMs (Figure 7B), These findings strongly indicate that USP38 interacts with and deubiquitinates TBK1 in hypertrophied cardiomyocytes."

reach
"co-immunoprecipitation suggests an interaction between USP38 and TBK1."
USP38 binds TBK1. 8 / 8
| 8

sparser
"Finally, we examined the interaction of USP38 with TBK1 by co-immunoprecipitation (F xref g.  xref I, J)."

sparser
"Consistent with previous findings, this study revealed a significant increase in TBK1, AKT and CaMKII phosphorylation levels after pressure overload-induced HF, and these adverse effects were mitigated in USP38 knockout mice. co-immunoprecipitation suggests an interaction between USP38 and TBK1."

sparser
"We subsequently performed Co-IP and identified that USP38 antibody efficiently precipitated TBK1 in NRCMs, and reverse Co-IP further confirmed that TBK1 interacted with USP38(Figure xref D)."

sparser
"Moreover, the interaction of USP38 with TBK1 was obviously enhanced following Ang II administration(Figure xref E)."

sparser
"Consistent with our in vitro findings, the interaction between USP38 and TBK1 was observed in the heart tissue collected from wild-type mice(Figure xref G)."

sparser
"These results suggest that USP38 interacts with TBK1 in NRCMs and myocardial tissues."

sparser
"In the present study, we validated the interaction of USP38 with TBK1 in heart tissue and NRCMs."

sparser
"USP38 interacts with TBK1 and removes K48-linked polyubiquitination chain."
TBK1 activates USP38.
| 1
TBK1 activates USP38. 1 / 1
| 1

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"TBK1 mediated USP38-regulated pathological cardiac remodeling."
USP38 affects JUNB
| 12
USP38 binds JUNB.
| 6
| 6

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"USP38 directly associates with JunB and removes TCR-induced JunB poly-ubiquitination."

reach
"We demonstrated that USP38 directly associated with JunB and removed its poly-ubiquitination to block JunB degradation in TCR signaling, thus initiating Th2 differentiation and driving allergic asthma."

reach
"USP38 associated with JunB directly as well as in a TCR signal–dependent manner."

reach
"We then checked into the endogenous system and found that USP38 bound to JunB, but not c-Jun, in a TCR stimulation–dependent manner (Fig. 9 B)."

reach
"USP38 did not associate with Itch, nor its activator Ndfip1, in either 293T overexpression system or TCR-induced endogenous system (Fig. 9, A and B), indicating that USP38 may directly associate with JunB for its deubiquitination."

reach
"All these data suggest that USP38 directly associates with JunB, and its enzyme activity removes JunB ubiquitination in TCR signaling."
USP38 activates JUNB.
| 4
USP38 activates JUNB. 4 / 4
| 4

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"USP38 critically promotes asthmatic pathogenesis by stabilizing JunB protein."

reach
"USP38 is induced by TCR signaling and in turn promotes JunB stabilization to specifically regulate Th2 cell differentiation."

reach
"Altogether, our data suggest that TCR-induced USP38 specifically blocks JunB protein turnover, thus promoting Th2 cytokines production."

reach
"The restoration study also confirmed the specificity of USP38 in TCR-induced JunB instead of c-Jun stability (Fig. 10 A)."
USP38 ubiquitinates JUNB.
| 1
USP38 leads to the ubiquitination of JUNB. 1 / 1
| 1

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"USP38 de-ubiquitinated TCR-induced Lys-48–linked poly-ubiquitination of JunB and thus consequently blocked proteasome-mediated JunB degradation."
USP38 deubiquitinates JUNB.
| 1
USP38 deubiquitinates JUNB. 1 / 1
| 1

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"For example, USP38 deubiquitinates JunB protein, which contributes to the development of allergic asthma."

reach
"Conversely, knockdown of USP38 effectively inhibited the proliferation of A549 and Hela cells ( Fig. 3 C and D)."

reach
"The effect of USP38 on promoting cell proliferation only occurred in control A549 cells, but not in c-Myc knockdown A549 cells ( Fig. 3 E)."

reach
"Conversely, in gastric cancer (GC), USP38 is overexpressed and promotes the proliferation and migration of GC cells, facilitating GC progression by stabilizing FASN [35]."

reach
"Functionally, USP38 promotes cell proliferation in a c-Myc dependent manner."

eidos
"Functionally , USP38 is able to promote cell proliferation via a c-Myc dependent manner ."

reach
"In this research, we found that USP38 was overexpressed in GC tissues, and USP38 contributed to GC cell proliferation, migration and tumorigenesis."

reach
"USP38 silencing suppresses the proliferation of LUAD cells in vitro and impedes the tumorigenic activity of cells in xenograft mouse models in vivo."

reach
"In addition, USP38 has been shown to promote cell proliferation by stabilizing LSD1 or c-Myc proteins27, 28."

reach
"On the other hand, USP38 is able to promote cell proliferation and asthmatic pathogenesis, seeming to be an oncogenic factor ( Chen et al., 2018 ; Liu et al., 2018 )."

reach
"In addition, USP38 promotes lung cancer cell proliferation by stabilizing c-Myc (14)."
USP38 affects SLC16A1
| 11
USP38 binds SLC16A1.
| 4
| 4

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"Co-immunoprecipitation and ubiquitination assays were conducted to analyze the interaction between USP38 and MCT1, as well as the regulation of MCT1 deubiquitination."

reach
"To further validate this interaction, we performed a Co‐IP assay, which confirmed the binding between USP38 and MCT1 (Figure 4B,C)."

reach
"This study demonstrated that USP38 interacts with the monocarboxylate transporter MCT1 (SLC16A1), deubiquitinates MCT1 to enhance its expression, and thereby promotes lactate efflux under PM2.5 exposure."

reach
"However, direct evidence supporting an interaction between USP38 and MCT1 remains to be established."
USP38 increases the amount of SLC16A1.
| 2
USP38 increases the amount of SLC16A1. 2 / 2
| 2

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"Future studies will focus on investigating this potential interaction in greater depth.In summary, our findings demonstrate that USP38 modulates MCT1 expression through deubiquitination, promoting the export of lactate accumulated in lung epithelial cells due to PM2.5 exposure."

reach
"Additionally, the knockdown of USP38 increased the ubiquitination level of MCT1 (Figure 4J), while overexpression of USP38 reduced the ubiquitination level of MCT1 (Figure 4K)."
USP38 deubiquitinates SLC16A1.
| 2
USP38 deubiquitinates SLC16A1. 2 / 2
| 2

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"TUNEL staining provided further evidence that USP38 knockout exacerbated apoptosis in the lung tissue of mice (Figure 3F,G).3.4 USP38 Deubiquitinated the Lactate Transporter Protein MCT1."

reach
"This study demonstrated that USP38 interacts with the monocarboxylate transporter MCT1 (SLC16A1), deubiquitinates MCT1 to enhance its expression, and thereby promotes lactate efflux under PM2.5 exposure."
USP38 decreases the amount of SLC16A1.
| 2
USP38 decreases the amount of SLC16A1. 2 / 2
| 2

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"Proteomic analysis further revealed a significant decrease in MCT1 expression following USP38 knockdown (Table S3)."

reach
"Additionally, the knockdown of USP38 increased the ubiquitination level of MCT1 (Figure 4J), while overexpression of USP38 reduced the ubiquitination level of MCT1 (Figure 4K)."
USP38 inhibits SLC16A1.
| 1
| 1

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"In contrast, the knockdown of USP38 enhanced the degradation rate of MCT1 (Figure 4H,I)."
USP38 affects Hypoxia
| 11
| 11

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"Furthermore, overexpression of USP38 enhanced the expression of hypoxia-inducible genes under hypoxia (Fig. 1C)."

reach
"To determine whether the screened USP38 specifically enhanced hypoxia signaling, we selected two additional USPs, USP53 and USP25, for validation."

reach
"In wild-type H1299 cells, overexpression of USP38 significantly enhanced hypoxia-stimulated expression of BNIP3 and VEGFA, but not in HIF1β-deficient H1299 cells (Fig. 1K)."

reach
"Taken together, these data suggest that USP38 enhances hypoxia signaling."

reach
"These data suggest that USP38 may enhance hypoxia signaling to influence cellular ROS and subsequent cell apoptosis dependent on HIF1α."

reach
"Although we provide evidence to support that USP38 can enhance hypoxia signaling by stabilizing HIF1α, the physiological relevance of this modulation is still largely unknown due to the lack of animal models."

reach
"Further investigation of the role of USP38 in modulating hypoxia signaling in vivo will provide insight into the physiological function of USP38 and the underlying molecular mechanisms."

reach
"USP38 promoted hypoxia-responsive gene expression under hypoxia."

reach
"We found that overexpression of USP38 increased hypoxia-responsive gene expression, but knockout of USP38 suppressed hypoxia-responsive gene expression under hypoxia."

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"USP38 enhances hypoxia signaling."
| 9
| 7

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"In addition, USP38 attenuated cellular ROS and suppressed cell apoptosis under hypoxia."

reach
"Knockout of USP38 hindered cancer cell proliferation, migration, and invasion, and enhanced apoptosis."

reach
"For instance, USP38 stabilizes HIF1α through deubiquitination under hypoxic conditions, thereby reducing cellular ROS and inhibiting apoptosis [20]."

reach
"By stabilizing MCT1, USP38 facilitates lactate export, thereby preventing intracellular lactate accumulation and reducing apoptosis.3.7 USP38 Activated the AKT/mTOR Pathway to Inhibit PM2.5-Induced Apoptosis."

reach
"Loss of USP38 leads to accumulation of cellular ROS and increased cell apoptosis."

reach
"Knockdown of USP38 enhanced PM2.5‐induced cell apoptosis (Figure 2D and Figure S1D) and led to increased lactate accumulation (Figure 2F)."

reach
"However, the underlying mechanisms are still poorly understood and need to be further explored.In this study, we found that knockout of USP38 resulted in the accumulation of ROS and increased cell apoptosis."
| 2

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"After administering the AKT inhibitor MK2206, the USP38‐mediated suppression of PM2.5‐induced cellular apoptosis and the subsequent activation of the AKT/mTOR signaling pathway were reduced (Figure 7D,E)."

reach
"In addition, we show that USP38 attenuates cellular ROS and suppresses cell apoptosis under hypoxia."
BIRC5 affects USP38
1 | 8
BIRC5 binds USP38.
1 | 6
1 | 6

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"The interaction between USP38 and BIRC5 was explored by using co-immunoprecipitation (Co-IP) and the ubiquitination level and stability of BIRC5 were examined by using Western blot."

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"At the molecular level, USP38 interacts with and stabilizes BIRC5 by decreasing its ubiquitination."

reach
"USP38 interacted with and deubiquitinated BIRC5 in IEC-6 cells."

reach
"These results suggest that USP38 interacts with and deubiquitinates BIRC5 to stabilize it in IEC-6 cells."

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"USP35/USP38 interacted with and deubiquitinated survivin."

No evidence text available

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"Our work revealed that USP35 and its orthologous gene USP38 interacted with and deubiquitinated survivin, which in turn stabilized the survivin protein."
BIRC5 inhibits USP38.
| 1
BIRC5 inhibits USP38. 1 / 1
| 1

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"Knock-down of BIRC5 abolished the protective effect of excessive USP38 on OGD/R-treated IEC-6 cells."
BIRC5 activates USP38.
| 1
BIRC5 activates USP38. 1 / 1
| 1

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"Moreover, BIRC5 deficiency also nullified the effect of excessive USP38 in decreasing the ROS level of OGD/R-treated IEC-6 cells, as evidenced by the DCFDA staining results (Figure 4H and I)."
| 4 4

eidos
"USP38 Binds to E Protein through Its C-Terminal Domain Next , the mechanism by which USP38 represses ZIKV infection was explored ."
| PMC

eidos
"USP38 Inhibits Zika Virus Infection by Removing Envelope Protein Ubiquitination ."

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"Table 3 summarizes these peptides and other, active agents against cancer and virus targets.Recently, it was reported that ubiquitin-specific peptidase 38 (USP38) represses ZIKV infection by binding t[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

eidos
"USP38 Inhibits Zika Virus Infection by Removing Envelope Protein Ubiquitination Zika virus ( ZIKV ) is a mosquito-borne flavivirus , and its infection may cause severe neurodegenerative diseases ."
| PMC

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"USP38 Inhibits Zika Virus Infection by Removing Envelope Protein Ubiquitination."

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"Overexpression of USP38 (ubiquitin-specific peptidase 38) in HeLa cells, which is also known to regulate inflammation and histone modification and can inhibit IFN-I signaling during viral infection (142, 143), reduced ZIKV infection."

reach
"In addition, we found that the deubiquitinase activity of USP38 was essential to inhibit ZIKV infection, and the mutant that lacked the deubiquitinase activity of USP38 lost the ability to inhibit infection."

eidos
"These results demonstrate that ZIKV infection was repressed by USP38 ."
| PMC
USP38 affects Interferon
| 8
USP38 inhibits Interferon.
| 5
| 5

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"Taken together, these data suggest that USP38 inhibits type I IFN signaling by removing K33-linked and promoting K48-linked poly-ubiquitination chains of TBK1 at Lys670.Since both NLRP4 and USP38 degr[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP38 is an almost uncharacterized DUB with only one functional report showing that USP38 inhibits TBK1-mediated type 1 interferon signaling in macrophages (Lin et al., 2016)."

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"Thus, it is critical to elucidate its molecular mechanisms for a better understanding of how dynamic ubiquitin editing shapes TBK1 function as well as antiviral responses.Our findings show that USP38 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Ubiquitin-specific peptidase 38 (USP38), a member of the ubiquitin specific processing enzyme family, has been reported to inhibit type I interferon signaling during viral infection (Lin et al., 2016)."

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"These results suggest that USP38 inhibits type I IFN signaling by interacting with TBK1 after viral infection.Next we sought to determine the molecular mechanisms of how USP38 inhibits type I IFN sign[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 decreases the amount of Interferon.
| 2
USP38 decreases the amount of Interferon. 2 / 2
| 2

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"Further qPCR analysis revealed that the mRNA levels of IFNα4 , IFNβ , IFIT1 , IFIT2 , and ISG15 in USP38 ectopic expression cells were markedly reduced during VSV infection ( Figure S1 B), suggesting [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"To substantiate these findings, we knocked down USP38 in THP-1 cells, 293T cells, A549 cells, or PBMCs, and we found that USP38 knockdown significantly increased the IFN - α4 and IFN - β expression, a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 activates Interferon.
| 1
| 1

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"USP38 deficiency abrogated the degradation of TBK1 and increased the production of type I IFN."
USP38 affects HDAC1
4 | 4
USP38 binds HDAC1.
4 | 1
4 |

No evidence text available

No evidence text available

No evidence text available

No evidence text available
USP38 binds HDAC1 and K63. 1 / 1
| 1

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"In response to DNA damage, USP38 interacted with HDAC1 and specifically removed the K63 linked ubiquitin chain promoting the deacetylase activity of HDAC1."
USP38 inhibits HDAC1.
| 1
Modified USP38 inhibits HDAC1. 1 / 1
| 1

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"Importantly, we found that USP38 overexpression significantly decreased the ubiquitination level of HDAC3 but not HDAC1 and had no effect on the overall protein level of HDAC3 and HDAC1."
USP38 deubiquitinates HDAC1.
| 1
USP38 deubiquitinates HDAC1. 1 / 1
| 1

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"24 USP38 deubiquitinated HDAC1 to regulate cancer cell resistance to genotoxic insults."
USP38 activates HDAC1.
| 1
USP38 bound to K63 and HDAC1 activates HDAC1. 1 / 1
| 1

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"In response to DNA damage, USP38 interacted with HDAC1 and specifically removed the K63 linked ubiquitin chain promoting the deacetylase activity of HDAC1."
TCR affects USP38
| 8
TCR activates USP38.
| 4
TCR activates USP38. 4 / 4
| 4

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"USP38 is induced by TCR signaling and in turn promotes JunB stabilization to specifically regulate Th2 cell differentiation."

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"Considering that USP38 was induced by TCR signaling in T cells, but not induced in macrophages by the innate sensor triggers, we hypothesize that the observed USP38 expression in the infiltrated immune cells is likely due to its induction in T cells after OVA challenge.Apart from its essential role in TCR-induced JunB stability, we found that USP38 was dispensable for the cytokine (IL-4, IL-2, and IL-6)-induced signaling in T cells (Fig. S4, A–C)."

reach
"To explore this point, we pretreated cells with MG132 to block proteasome-mediated protein degradation and indeed found that MG132 restored the TCR-induced accumulation defect of JunB protein in USP38-deficient T cells (Fig. 8 D)."

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"Chen et al. reported that TCR stimulation (anti-CD3/CD28) promoted USP38 in allergic asthma."
TCR increases the amount of USP38.
| 3
TCR increases the amount of USP38. 3 / 3
| 3

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"Here we found that TCR activation induced expression of ubiquitin-specific peptidase 38 (USP38), whose gene has been recently reported to be in a chromosome locus associated with human asthma in a genome-wide association study (GWAS; Hirota et al., 2011)."

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"We further found that the mRNA level of usp38 did not show statistic difference in different CD4 T cell subsets (Fig. S3 A) and was not induced by the subset-specific cytokines, including IL-2, IL-4, IL-6, IFN, and TGF-β in primary CD4 T cells (Fig. S3 B), suggesting that usp38 expression is directly regulated by TCR signal rather than by cytokines downstream of TCR signaling."

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"178 In the pathogenesis of allergic asthma, TCR signaling can upregulate the levels of the deubiquitinase USP38, which, in turn, stabilizes the TH2 development factor JunB, ultimately promoting asthma."
TCR inhibits USP38.
| 1
TCR inhibits USP38. 1 / 1
| 1

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"Altogether, our data suggest that TCR-induced USP38 specifically blocks JunB protein turnover, thus promoting Th2 cytokines production."
SLC16A1 affects USP38
| 8
SLC16A1 binds USP38.
| 4
| 4

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"Co-immunoprecipitation and ubiquitination assays were conducted to analyze the interaction between USP38 and MCT1, as well as the regulation of MCT1 deubiquitination."

reach
"To further validate this interaction, we performed a Co‐IP assay, which confirmed the binding between USP38 and MCT1 (Figure 4B,C)."

reach
"This study demonstrated that USP38 interacts with the monocarboxylate transporter MCT1 (SLC16A1), deubiquitinates MCT1 to enhance its expression, and thereby promotes lactate efflux under PM2.5 exposure."

reach
"However, direct evidence supporting an interaction between USP38 and MCT1 remains to be established."
SLC16A1 activates USP38.
| 3
SLC16A1 activates USP38. 3 / 3
| 3

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"MCT1 knockdown impaired the ability of USP38 to reduce PM2.5‐induced lactate accumulation (Figure 6A) and abolished the protective effect of USP38 on cell viability (Figure 6B)."

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"Western blot analysis confirmed that MCT1 knockdown completely eliminated the ability of USP38 to inhibit PM2.5‐induced apoptosis (Figure 6C)."

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"TUNEL staining provides additional evidence that the suppression of MCT1 markedly diminishes the protective role of USP38 in counteracting PM2.5‐induced apoptotic cell death (Figure 6D,E)."
SLC16A1 inhibits USP38.
| 1
| 1

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"Subsequent research indicated that the downregulation of MCT1 inhibited the ability of USP38 to activate the AKT/mTOR pathway (Figure 7F)."
JUNB affects USP38
| 8
JUNB binds USP38.
| 6
| 6

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"USP38 directly associates with JunB and removes TCR-induced JunB poly-ubiquitination."

reach
"We demonstrated that USP38 directly associated with JunB and removed its poly-ubiquitination to block JunB degradation in TCR signaling, thus initiating Th2 differentiation and driving allergic asthma."

reach
"USP38 associated with JunB directly as well as in a TCR signal–dependent manner."

reach
"We then checked into the endogenous system and found that USP38 bound to JunB, but not c-Jun, in a TCR stimulation–dependent manner (Fig. 9 B)."

reach
"USP38 did not associate with Itch, nor its activator Ndfip1, in either 293T overexpression system or TCR-induced endogenous system (Fig. 9, A and B), indicating that USP38 may directly associate with JunB for its deubiquitination."

reach
"All these data suggest that USP38 directly associates with JunB, and its enzyme activity removes JunB ubiquitination in TCR signaling."
JUNB activates USP38.
| 2
JUNB activates USP38. 2 / 2
| 2

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"The block of JunB protein induction in the USP38-deficient T cells was restored by the proteasome inhibitor MG132, and likewise, the degradation rate of JunB is more rapid in usp38 CD4 T cells in the presence of CHX after TCR stimulation, suggesting that USP38 stabilizes JunB protein in TCR signaling."

reach
"Analogous to the quantitative change of JunB level in the condition of the transgenic mice (Li et al., 1999), our data showed that USP38 only regulated JunB protein stability and was not required for Junb mRNA induction, and thus, there was still JunB induction in USP38-deficient CD4 T cells upon TCR stimulation."
USP38 affects KDM1A
1 1 | 3 2
USP38 binds KDM1A.
1 | 2
USP38 binds KDM1A. 2 / 2
| 2

sparser
"Therefore, we could not perform pull-down test to prove the direct interaction between USP38 and LSD1."

sparser
"Thus, USP38 promotes the colony formation ability of HCT116 cells through the interaction between USP38 and LSD1."
1 |

No evidence text available
USP38 deubiquitinates KDM1A.
1 | 1
USP38 deubiquitinates KDM1A. 2 / 2
1 | 1

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"USP38 promotes the ability of cellular drug tolerance and colony formation in colon cancer cells by deubiquitinating LSD1.46 Methylation of LSD1."

"RESULTS: The deubiquitinase <span class="match term0">USP38</span> stabilizes protein <span class="match term1">LSD1</span> in cells by binding <span class="match term1">LSD1</span> and cleaving its ubiquitin chain to prevent the degradation of <span class="match term1">LSD1</span> by the intracellular proteasome"
USP38 activates KDM1A.
| 2
USP38 activates KDM1A. 2 / 2
| 2

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"In addition, USP38 has been shown to promote cell proliferation by stabilizing LSD1 or c-Myc proteins27, 28."

reach
"USP38 enhances the stability of LSD1, thereby activating signaling pathways and promoting cell proliferation and colony formation (6, 7), which suggests a role of LSD1 in COPD pathogenesis.LSD1 is a member of the flavin adenine dinucleotide-dependent amine oxidase family (8)."

reach
"In conclusion, USP38 promotes inflammatory AF induced by pressure overload."

reach
"Conversely, USP38 overexpression further increased susceptibility to AF by exacerbating atrial structural and electrical remodelling."

reach
"Overall, our study indicates that USP38 promotes pressure overload-induced AF through targeting NF-kappaB/NLRP3-mediated inflammatory responses."

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"Ubiquitin-specific protease 38 (USP38) was upregulated in the left atrium after aortic banding surgery.Cardiac-specific knockout of USP38 attenuated the atrial dilation and fibrosis and reduced the vulnerability of atrial fibrillation (AF) induced by pressure overload.Cardiac-specific overexpression of USP38 aggravated the atrial structural and electrical remodelling induced by pressure overload.Ubiquitin-specific protease 38 promoted atrial inflammation by interacting with and deubiquitinating nuclear factor-kappa B.Targeting USP38 may be an effective treatment for AF induced by pressure overload."

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"Ubiquitin-specific protease 38 (USP38) was upregulated in the left atrium after aortic banding surgery.Cardiac-specific knockout of USP38 attenuated the atrial dilation and fibrosis and reduced the vulnerability of atrial fibrillation (AF) induced by pressure overload.Cardiac-specific overexpression of USP38 aggravated the atrial structural and electrical remodelling induced by pressure overload.Ubiquitin-specific protease 38 promoted atrial inflammation by interacting with and deubiquitinating nuclear factor-kappa B.Targeting USP38 may be an effective treatment for AF induced by pressure overload."

reach
"It was found that overexpression of USP38 increased vulnerability to AF in diabetic mice."

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"USP38 overexpression increased susceptibility to AF, accompanied by aberrant expression of calcium-handling protein, heightened iron load and oxidation stress in diabetic mice."
USP38 affects Mice
| 6
USP38 activates Mice.
| 4
USP38 activates Mice. 4 / 4
| 4

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"USP38 deficiency improves cardiac function and reduces the susceptibility of VAs in mice with HF induced by pressure overload.."

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"Conversely, cardiac-specific overexpression of USP38 exacerbated cardiac diastolic dysfunction and increased susceptibility to VAs in HFpEF mice."

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"It was found that overexpression of USP38 increased vulnerability to AF in diabetic mice."

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"Together, these results demonstrate that USP38 promotes the activation of the TBK1/AKT/CaMKII signaling pathway in mice with HF."
USP38 inhibits Mice.
| 2
USP38 inhibits Mice. 2 / 2
| 2

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"These findings were further confirmed in our study, indicating that USP38 decreases the expression of ion channels in mice after HF, thereby prolonging action potential duration and increasing susceptibility to VAs.Cx43 exists in the ventricular gap junction structure, regulating electrical conduction between cardiomyocytes and coordinating heart rhythm."

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"USP38 reduces the expression of ion channels in mice with HF induced by pressure overload.."
USP38 affects MTOR
| 6
USP38 activates MTOR.
| 4
USP38 activates MTOR. 4 / 4
| 4

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"Interestingly, we observed that USP38 activated the AKT/mTOR pathway and counteracted the inhibitory effects of PM2.5 (Figure 7C)."

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"In conclusion, these findings demonstrated that USP38 mitigates PM2.5‐induced lung epithelial cell damage by activating the AKT/mTOR pathway via MCT1, reducing lactate accumulation and apoptosis.4 Discussion."

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"USP38 facilitates lactate export through MCT1, activates the AKT/mTOR pathway, and mitigates PM2.5‐induced lung injury."

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"By stabilizing MCT1, USP38 facilitates lactate export, thereby preventing intracellular lactate accumulation and reducing apoptosis.3.7 USP38 Activated the AKT/mTOR Pathway to Inhibit PM2.5-Induced Apoptosis."
USP38 phosphorylates MTOR.
| 1
USP38 leads to the phosphorylation of MTOR. 1 / 1
| 1

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"Consistently, knockdown of USP38 in NRCMs remarkedly decreased Akt, GSK3β and mTOR phosphorylation levels after Ang II stimulation (Figure 5C), whereas the activation of Akt signaling was obviously enhanced through USP38 overexpression (Figure 5D)."
USP38 increases the amount of MTOR.
| 1
USP38 increases the amount of MTOR. 1 / 1
| 1

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"Consistently, knockdown of USP38 in NRCMs remarkedly decreased Akt, GSK3β and mTOR phosphorylation levels after Ang II stimulation (Figure 5C), whereas the activation of Akt signaling was obviously enhanced through USP38 overexpression (Figure 5D)."
USP38 affects FBXW7
2 | 4
USP38 binds FBXW7.
2 | 1
2 | 1

No evidence text available

No evidence text available

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"An interaction between endogenous FBW7 and USP38 was also detected ( Fig. 4 D)."
USP38 activates FBXW7.
| 3
USP38 activates FBXW7. 2 / 2
| 2

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"However, ectopic expression of USP38 abrogated FBW7α-mediated degradation of c-Myc ( Fig. 5 A)."

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"USP38 interacts with FBW7α and abolishes FBW7α-mediated degradation, thereafter increasing c-Myc protein stability."
Mutated USP38 activates FBXW7. 1 / 1
| 1

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"Since the enzyme-inactive mutant of USP38 can still increase c-Myc levels ( Fig. 1 B and D), it is not surprising that USP38 mutant can also abolish FBW7α-mediated degradation of c-Myc ( Fig. 5 B)."

reach
"For instance, USP38 stabilizes HIF1α through deubiquitination under hypoxic conditions, thereby reducing cellular ROS and inhibiting apoptosis [20]."

reach
"In addition, we show that USP38 attenuates cellular ROS and suppresses cell apoptosis under hypoxia."

reach
"In addition, USP38 attenuated cellular ROS and suppressed cell apoptosis under hypoxia."
USP38 decreases the amount of Reactive Oxygen Species.
| 2
USP38 decreases the amount of Reactive Oxygen Species. 2 / 2
| 2

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"Incubation of these cells with BM-MSC-EVs substantially elevated the USP38 expression, resulting in improved viability, reduced apoptosis, enhanced migration, and decreased ROS levels."

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"Furthermore, research indicates that USP38 reduces cellular ROS levels and suppresses apoptosis under hypoxic conditions [20]."
USP38 affects Histone
| 5
USP38 acetylates Histone.
| 3
USP38 leads to the acetylation of Histone. 3 / 3
| 3

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"USP38 modulates histone acetylation."

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"Taken together, our data indicated that USP38 modulates histone acetylation via regulating histone deacetylases."

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"Hence, our data indicated that USP38 functions as a deubiquitinase of HDAC3 to modulate the acetylation of histones and regulate gene expression."
USP38 activates Histone.
| 2
USP38 activates Histone. 2 / 2
| 2

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"Next, we analyzed the expression level of HDACs in control, USP38 knockdown, and overexpressing HCT116 cells to determine which HDAC is responsible for USP38 mediated histone modification."

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"Taken together, our data demonstrated that HDAC3 is functional responsible for USP38 mediated histone modifications, which further controls the expression of cancer stem cell related genes."
USP38 affects HIF1
| 5
USP38 activates HIF1.
| 4
USP38 activates HIF1. 4 / 4
| 4

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"Ectopic expression of USP38 caused HIF1α stabilization in a dose-dependent manner (Fig. 3A)."

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"We further found that ectopic expression of USP38 also stabilized the HIF1α hydroxylation-deficient mutants, HIF1α (in which Pro 402 and 564, and Asp 803 were mutated to alanine) and HIF1α (in which Pro402 and 564 were mutated to alanine) (Fig. S5), indicating that USP38-mediated HIF1α stabilization is independent of PHD/VHL-mediated oxygen-dependent degradation of HIF1α."

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"Treatment with cycloheximide (CHX) indicated that USP38 significantly suppressed HIF1α degradation (Fig. 3D)."

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"To determine whether USP38-mediated HIF1α stabilization is dependent on the deubiquitinase activity of USP38, we used the enzymatically inactive mutants for subsequent assays (37, 38, 39)."
USP38 deubiquitinates HIF1.
| 1
USP38 leads to the deubiquitination of HIF1. 1 / 1
| 1

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"Ubiquitination assays showed that overexpression of USP38 significantly reduced polyubiquitination of HIF1α (Fig. 4A)."
USP38 affects FASN
2 | 3
USP38 binds FASN.
2 | 1
2 | 1

No evidence text available

No evidence text available

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"Another study demonstrated that interaction between USP38 and FASN enhances the stability of FASN protein and increases triglyceride production in gastric cancer cells, which contributes to cell proliferation, migration, and tumorigenesis (Zheng et al. 2022)."
USP38 activates FASN.
| 2
USP38 activates FASN. 1 / 1
| 1

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"It has been reported that USP38 promotes gastric cancer progression by upregulating fatty acid synthase (13)."
USP38 bound to FASN activates FASN. 1 / 1
| 1

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"Another study demonstrated that interaction between USP38 and FASN enhances the stability of FASN protein and increases triglyceride production in gastric cancer cells, which contributes to cell proliferation, migration, and tumorigenesis (Zheng et al. 2022)."
METTL14 affects USP38
| 5
METTL14 inhibits USP38.
| 2
| 2

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"METTL14 represses BCa cell migration, invasion and EMT via USP38."

reach
"Huang et al. [101] further demonstrated that METTL14 inhibits BCa cell migration, invasion, and EMT by modifying the stability of USP38 mRNA through m6A modification.In RCC, METTL3 plays a dual role."
METTL14 activates USP38.
| 2
METTL14 activates USP38. 2 / 2
| 2

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"METTL14 stabilizes USP38 mRNA by inducing N6-methyladenosine (m6A) modification and enhances USP38 mRNA stability in YTHDF2-dependent manner."

reach
"METTL14 stabilized USP38 mRNA by inducing m6A modification and enhanced USP38 mRNA stability in a YTHDF2-dependent manner [97]."
METTL14 decreases the amount of USP38.
| 1
METTL14 decreases the amount of USP38. 1 / 1
| 1

reach
"METTL14 represses bladder cancer cell migration, invasion, and EMT by increasing the expression of USP38 [97]."
HDAC1 affects USP38
4 | 1
4 |

No evidence text available

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No evidence text available
USP38 binds HDAC1 and K63. 1 / 1
| 1

reach
"In response to DNA damage, USP38 interacted with HDAC1 and specifically removed the K63 linked ubiquitin chain promoting the deacetylase activity of HDAC1."
USP38 affects lactate
| 4
USP38 inhibits lactate.
| 3
| 3

reach
"Conversely, overexpression of USP38 inhibited PM2.5‐induced cell apoptosis (Figure 2D and Figure S1E) and reduced PM2.5‐induced lactate production (Figure 2F)."

reach
"In conclusion, these findings demonstrated that USP38 mitigates PM2.5‐induced lung epithelial cell damage by activating the AKT/mTOR pathway via MCT1, reducing lactate accumulation and apoptosis.4 Discussion."

reach
"We have demonstrated that both USP38 and MCT1 reduce PM2.5‐induced lactate accumulation."
USP38 activates lactate.
| 1
USP38 bound to SLC16A1 activates lactate. 1 / 1
| 1

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"This study demonstrated that USP38 interacts with the monocarboxylate transporter MCT1 (SLC16A1), deubiquitinates MCT1 to enhance its expression, and thereby promotes lactate efflux under PM2.5 exposure."
USP38 affects KDM5B
2 | 2
USP38 binds KDM5B.
2 | 1
2 | 1

No evidence text available

No evidence text available

reach
"Furthermore, USP38 can bind to KDM5B and prevent it from proteasomal degradation, which further enhances the function of KDM5B in the regulation of inflammation related genes."
USP38 inhibits KDM5B.
| 1
USP38 inhibits KDM5B. 1 / 1
| 1

reach
"We also showed that USP38 specifically inhibited proteasomal degradation of KDM5B to resolve inflammation, further indicating the importance of histone methylases and demethylases in immune regulation (11)."
USP38 affects Flag
| 4
USP38 binds Flag. 4 / 4
| 4

sparser
"In addition, A549 cells were transfected with HA-UB, Flag-vector, or Flag-USP38 for 24 h and then infected with ZIKV (1 MOI)."
| PMC

sparser
"Furthermore, we analyzed the colocalization of USP38 and ADAR by immunofluorescence and found that both heterologously coexpressed ADAR-HA and Flag-USP38, as well as endogenous ADAR and USP38, were localized in the nucleus, with a strong colocalization fluorescence intensity observed ( xref D )."

sparser
"Therefore, we analyzed the ubiquitination levels of Flag-USP38 WT and Flag-USP38 C454A/H857A by coexpressing them with His-tagged ubiquitin (His-Ub) respectively and immunoprecipitating ubiquitylated proteins with a His antibody."

sparser
"To further clarify that USP38 can indeed regulate its own ubiquitination level, we coexpressed WT USP38 (Flag-USP38 WT) and two inactive mutants (Flag-USP38 C454A or C454A/H857A) with His-Ub, respectively, followed by IP analysis using Flag antibody."
USP38 affects Cytokinin dehydrogenase
| 4

sparser
"The USP38-CKO group showed an improvement in the expression level of the above channel proteins (Fig.  xref A–F)."

sparser
"To better elucidate the role of USP38 in regulation of HF-related VAs, we utilized the Cre-LoxP system to generate USP38-CKO mice, with their wild-type littermates referred to as the Flox-Sham group."

sparser
"The absence of USP38 expression in the USP38-CKO mice were confirmed by Western blotting (Fig. S3A)."

sparser
"After AB surgery, the Flox group exhibited a significant increase in QRS duration and QTc, However, these changes were attenuated in the USP38-CKO group following AB surgery (Fig.  xref A, B)."
USP38 affects AKT
| 4
USP38 activates AKT. 4 / 4
| 4

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"USP38 facilitates lactate export through MCT1, activates the AKT/mTOR pathway, and mitigates PM2.5‐induced lung injury."

reach
"In conclusion, these findings demonstrated that USP38 mitigates PM2.5‐induced lung epithelial cell damage by activating the AKT/mTOR pathway via MCT1, reducing lactate accumulation and apoptosis.4 Discussion."

reach
"Interestingly, we observed that USP38 activated the AKT/mTOR pathway and counteracted the inhibitory effects of PM2.5 (Figure 7C)."

reach
"By stabilizing MCT1, USP38 facilitates lactate export, thereby preventing intracellular lactate accumulation and reducing apoptosis.3.7 USP38 Activated the AKT/mTOR Pathway to Inhibit PM2.5-Induced Apoptosis."
Mice affects USP38
| 4
Mice activates USP38. 4 / 4
| 4

reach
"Conversely, Akt, GSK3β and mTOR phosphorylation levels were markedly increased in USP38 overexpression mice (Figure 5B)."

reach
"Next, we also established cardiac-specific USP38 overexpression mice to further verify the role of USP38 in HF induced by pressure overload (Fig. S3B)."

reach
"However, mice overexpressed USP38 had a higher incidence of VAs, with VT accounting for 75% and VF accounting for 20% (Fig. 3H, I)."

reach
"We constructed and generated cardiac specific USP38 knockout mice and cardiac specific USP38 overexpression mice to assess the role of USP38 in pathological cardiac remodeling."
Flag affects USP38
| 4
USP38 binds Flag. 4 / 4
| 4

sparser
"In addition, A549 cells were transfected with HA-UB, Flag-vector, or Flag-USP38 for 24 h and then infected with ZIKV (1 MOI)."
| PMC

sparser
"Furthermore, we analyzed the colocalization of USP38 and ADAR by immunofluorescence and found that both heterologously coexpressed ADAR-HA and Flag-USP38, as well as endogenous ADAR and USP38, were localized in the nucleus, with a strong colocalization fluorescence intensity observed ( xref D )."

sparser
"Therefore, we analyzed the ubiquitination levels of Flag-USP38 WT and Flag-USP38 C454A/H857A by coexpressing them with His-tagged ubiquitin (His-Ub) respectively and immunoprecipitating ubiquitylated proteins with a His antibody."

sparser
"To further clarify that USP38 can indeed regulate its own ubiquitination level, we coexpressed WT USP38 (Flag-USP38 WT) and two inactive mutants (Flag-USP38 C454A or C454A/H857A) with His-Ub, respectively, followed by IP analysis using Flag antibody."
Cytokinin dehydrogenase affects USP38
| 4

sparser
"The USP38-CKO group showed an improvement in the expression level of the above channel proteins (Fig.  xref A–F)."

sparser
"To better elucidate the role of USP38 in regulation of HF-related VAs, we utilized the Cre-LoxP system to generate USP38-CKO mice, with their wild-type littermates referred to as the Flox-Sham group."

sparser
"The absence of USP38 expression in the USP38-CKO mice were confirmed by Western blotting (Fig. S3A)."

sparser
"After AB surgery, the Flox group exhibited a significant increase in QRS duration and QTc, However, these changes were attenuated in the USP38-CKO group following AB surgery (Fig.  xref A, B)."
3 |
Sodium arsenite increases the amount of USP38. 3 / 3
3 |

No evidence text available

No evidence text available

No evidence text available
| 2

reach
"Together, these results demonstrate that USP38 promotes the activation of the TBK1/AKT/CaMKII signaling pathway in mice with HF."

reach
"Mechanistically, USP38 knockout inhibited activation of the TAK1/NF-κB signaling pathway after MI, whereas USP38 overexpression enhanced activation of the TAK1/NF-κB signaling pathway after MI."
| 1

reach
"Amlexanox protects USP38 mediated cardiac remodeling, decreasing the protein expression of USP38-mediated TBK1/AKT-GSK3β/mTOR signaling pathway [158]."
| 3
| 3

reach
"On the other hand, USP38 is able to promote cell proliferation and asthmatic pathogenesis, seeming to be an oncogenic factor ( Chen et al., 2018 ; Liu et al., 2018 )."

reach
"These results support the T cell intrinsic role of USP38 in OVA-induced asthmatic pathogenesis."

reach
"USP38 critically promotes asthmatic pathogenesis by stabilizing JunB protein."
USP38 affects ferroptosis
| 3
USP38 activates ferroptosis.
| 2
USP38 bound to IREB2 activates ferroptosis. 1 / 1
| 1

reach
"USP38 could bind to iron regulatory protein 2 (IRP2), stabilizing it and removing K48-linked polyubiquitination chains, leading to increasing intracellular iron overload, lipid peroxidation, and ultimately contribute to ferroptosis."
| 1

reach
"Conversely, USP38 deficiency reduced vulnerability to AF by hampering ferroptosis."
USP38 inhibits ferroptosis.
| 1
| 1

reach
"Moreover, USP38 deficiency increased sensitivity to chemotherapy drugs and promoted ferroptosis in gastric and breast cancer cell lines."

reach
"Notably, USP38 promotes NHEJ and allows cancer cells to develop resistance to genotoxic damage."

reach
"Deletion of USP38 impairs the dissociation of NHEJ factors from DSB sites."

reach
"The absence of USP38 diminishes NHEJ efficiency and heightens cell vulnerability to IR [237]."
USP38 affects USP38
| 3
USP38 inhibits USP38.
| 1
USP38 inhibits USP38. 1 / 1
| 1

reach
"Moreover, we found that PIAS1-mediated SUMOylation of USP38 was promoted, whereas SENP2-mediated de-SUMOylation of USP38 suppressed the deubiquitination effects of USP38 on KLF5."
USP38 decreases the amount of USP38.
| 1
USP38 decreases the amount of USP38. 1 / 1
| 1

reach
"Amlexanox protects USP38 mediated cardiac remodeling, decreasing the protein expression of USP38-mediated TBK1/AKT-GSK3β/mTOR signaling pathway [158]."
USP38 activates USP38.
| 1
USP38 activates USP38. 1 / 1
| 1

reach
"Mechanistically, we demonstrate that ADAR enhances USP38 auto-deubiquitylation to increase USP38 protein stability and upregulate USP38, thereby affecting cell proliferation and growth."
| 1 2

reach
"Furthermore, FASN was critical for GC cell growth, migration and tumor development triggered by USP38 overexpression because its inhibitor orilistat reversed phenotypes in USP38 overexpressed GC cells."

reach
"Conversely, in gastric cancer (GC), USP38 is overexpressed and promotes the proliferation and migration of GC cells, facilitating GC progression by stabilizing FASN [35]."

eidos
"Ubiquitin specific peptidase 38 promotes the progression of gastric cancer through upregulation of fatty acid synthase ."
USP38 affects Neoplasms
| 3
USP38 activates Neoplasms.
| 2
| 2

reach
"The results showed that knockdown of USP38 inhibited tumor growth in the Eca-109 xenograft mouse model (Fig. 1, G–I)."

reach
"Furthermore, FASN was critical for GC cell growth, migration and tumor development triggered by USP38 overexpression because its inhibitor orilistat reversed phenotypes in USP38 overexpressed GC cells."
USP38 inhibits Neoplasms.
| 1
| 1

reach
"The stabilization of USP38 mRNA by METTL14 inhibits tumor migration, invasion, and EMT."
USP38 affects NFkappaB
| 1 2
USP38 binds NFkappaB.
| 2
NFkappaB binds USP38. 2 / 2
| 2

sparser
"Finally, we detected the interaction of USP38 with NF-κB after Ang II administration by co-immunoprecipitation (Figure xref )."

sparser
"Mechanistically, USP38 interacts with NF-κB and mitigates the ubiquitination level of NF-κB, which promotes the activation of NLRP3."
USP38 deubiquitinates NFkappaB.
| 1
USP38 deubiquitinates NFkappaB. 1 / 1
| 1

reach
"Mechanistically, USP38 interacted with and deubiquitinated nuclear factor-kappa B (NF-kappaB), and USP38 overexpression increased the level of p-NF-kappaB in vivo and in vitro, accompanied by the upregulation of NOD-like receptor protein 3 (NLRP3) and inflammatory cytokines, suggesting that USP38 contributes to adverse effects by driving NF-kappaB/NLRP3-mediated inflammatory responses."
USP38 affects LDHA
1 | 2
USP38 increases the amount of LDHA.
| 2
USP38 increases the amount of LDHA. 2 / 2
| 2

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"We next confirmed that overexpression of USP38 together with HIF1α apparently enhanced the expression of BNIP3, LDHA, PDK1 and VEGFA (Fig. 1A)."

reach
"Overexpression of USP38 significantly increased LDHA expression (Fig. S1)."
USP38 binds LDHA.
1 |
1 |

No evidence text available
USP38 affects Hypertrophy
| 3
USP38 activates Hypertrophy.
| 2
| 2

reach
"Conversely, overexpression of USP38 accelerates the progression of cardiac hypertrophy and myocardial fibrosis."

reach
"Herein, we found that USP38 positively regulates pathological cardiac hypertrophy and remodeling by preventing the proteasomal degradation of p-TBK1, leading to the activation of Akt-GSK3β/mTOR signaling pathway and the acceleration of heart failure progression."
USP38 inhibits Hypertrophy.
| 1
| 1

reach
"Deletion of USP38 markedly ameliorated HFpEF-induced left ventricular (LV) hypertrophy and cardiac diastolic dysfunction."
| 3
| 3

reach
"Overall, USP38 overexpression aggravates pressure overload-induced pathological cardiac remodeling and promotes the development of heart failure."

reach
"In this study, we examined the impact of USP38 on VAs in pressure overload-induced HF."

reach
"These results suggest that USP38 deficiency alleviates cardiac hypertrophy and myocardial fibrosis, and prevents the progression of heart failure."
USP38 affects HMX3
2 | 1
USP38 binds HMX3.
2 |
2 |

No evidence text available

No evidence text available
USP38 deubiquitinates HMX3.
| 1
USP38 leads to the deubiquitination of HMX3. 1 / 1
| 1

reach
"Conversely, some studies also suggest USP38 as a tumor suppressor, such as USP38 promotes nonhomologous end joining repair in kidney clear cell carcinoma cancer by deubiquitinating HDAC1 to modulate its activity, maintaining genome stability and regulating cancer cells' response to genotoxic insults (15); USP38 inhibits tumor stemness in colorectal cancer by mediating K63 deubiquitination of HDAC3 (16); USP38 suppresses cell proliferation and migration by downregulating HMX3 ubiquitination in colorectal cancer (17); METTL14 inhibits bladder cancer cell migration and invasion by stabilizing USP38 (18)."
USP38 affects HIF1A
| 3
USP38 binds HIF1A. 3 / 3
| 3

sparser
"USP38 interacts with HIF1α."

sparser
"Further co-immunoprecipitation assays for endogenous protein interaction showed that USP38 could only interact with HIF1α under hypoxia, but not with VHL ( xref , B – D and xref )."

sparser
"Domain mapping revealed that all domains of HIF1α interacted with the N-terminus and the C-terminus of USP38 ( xref , E – G )."
USP38 affects H1-3
3 |
3 |

No evidence text available

No evidence text available

No evidence text available
USP38 affects GJA1
| 3
USP38 decreases the amount of GJA1.
| 2
USP38 decreases the amount of GJA1. 2 / 2
| 2

reach
"In addition, USP38 knockout increased ion channel and Cx43 expression in ventricle."

reach
"USP38 decreases the expression of Cx43 in HF induced by pressure overload.."
USP38 activates GJA1.
| 1
USP38 activates GJA1. 1 / 1
| 1

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"Our study revealed that the expression level and distribution area of Cx43 in the ventricle were further decreased after USP38 overexpression in mice with HF, while USP38 knockout inhibited the degradation of Cx43."
USP38 affects AHSG
3 |
3 |

No evidence text available

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USP38 is modified
| 3
USP38 is ubiquitinated. 3 / 3
| 3

sparser
"We analyzed the effect of overexpressing ADAR on the auto-deubiquitylation of USP38 through IP, and the results showed that overexpressing ADAR reduced the ubiquitination of USP38 C454A ( xref I )."

sparser
"Based on this, we analyzed whether the ubiquitylation of USP38 is sensitive to β-ME treatment."

sparser
"These results indicate that the ubiquitinated USP38 C454A and C454A/H857A are sensitive to the reducing agents, which also indicates that the protein is subject to cysteine ubiquitination modification."
KDM5B affects USP38
2 | 1
2 | 1

No evidence text available

No evidence text available

reach
"Furthermore, USP38 can bind to KDM5B and prevent it from proteasomal degradation, which further enhances the function of KDM5B in the regulation of inflammation related genes."
KDM1A affects USP38
1 | 2
USP38 binds KDM1A. 2 / 2
| 2

sparser
"Therefore, we could not perform pull-down test to prove the direct interaction between USP38 and LSD1."

sparser
"Thus, USP38 promotes the colony formation ability of HCT116 cells through the interaction between USP38 and LSD1."
1 |

No evidence text available
HIF1A affects USP38
| 3
USP38 binds HIF1A. 3 / 3
| 3

sparser
"USP38 interacts with HIF1α."

sparser
"Further co-immunoprecipitation assays for endogenous protein interaction showed that USP38 could only interact with HIF1α under hypoxia, but not with VHL ( xref , B – D and xref )."

sparser
"Domain mapping revealed that all domains of HIF1α interacted with the N-terminus and the C-terminus of USP38 ( xref , E – G )."
H1-3 affects USP38
3 |
3 |

No evidence text available

No evidence text available

No evidence text available
FBXW7 affects USP38
2 | 1
2 | 1

No evidence text available

No evidence text available

reach
"An interaction between endogenous FBW7 and USP38 was also detected ( Fig. 4 D)."
FASN affects USP38
2 | 1
2 | 1

No evidence text available

No evidence text available

reach
"Another study demonstrated that interaction between USP38 and FASN enhances the stability of FASN protein and increases triglyceride production in gastric cancer cells, which contributes to cell proliferation, migration, and tumorigenesis (Zheng et al. 2022)."
AHSG affects USP38
3 |
3 |

No evidence text available

No evidence text available

No evidence text available
2 |
Valproic acid increases the amount of USP38.
1 |
Valproic acid increases the amount of USP38. 1 / 1
1 |

No evidence text available
Valproic acid demethylates USP38.
1 |
1 |

No evidence text available
2 |
Pirinixic acid increases the amount of USP38. 2 / 2
2 |

No evidence text available

No evidence text available
Methylmercury chloride increases the amount of USP38.
1 |
Methylmercury chloride increases the amount of USP38. 1 / 1
1 |

No evidence text available
Methylmercury chloride decreases the amount of USP38.
1 |
Methylmercury chloride decreases the amount of USP38. 1 / 1
1 |

No evidence text available
Folic acid affects USP38
2 |
Folic acid demethylates USP38.
1 |
Folic acid demethylates USP38. 1 / 1
1 |

No evidence text available
Folic acid decreases the amount of USP38.
1 |
Folic acid decreases the amount of USP38. 1 / 1
1 |

No evidence text available
Bisphenol A affects USP38
2 |
Bisphenol A increases the amount of USP38. 2 / 2
2 |

No evidence text available

No evidence text available
Anti-CD3 affects USP38
| 2
Anti-CD3 activates USP38. 2 / 2
| 2

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"We observed that either anti-CD3/CD28 or anti-CD3 alone induced usp38 mRNA (Fig. 8, G and H)."

reach
"Similarly, USP38 protein was induced by anti-CD3/CD28 or anti-CD3 (Fig. 8, I and J), indicating that TCR signaling instead of CD28 signaling is responsible for USP38 induction."

reach
"USP38 knockout reduced atrial inflammation after MI by downregulating the activation of the TAK1-NF-κB pathway, whereas USP38 overexpression showed the opposite effect."

reach
"USP38 cardiac-conditional knockout attenuates LA inflammation at 3 days post-MI."
| 2

reach
"We found that overexpression of USP38 increased hypoxia-responsive gene expression, but knockout of USP38 suppressed hypoxia-responsive gene expression under hypoxia."

reach
"USP38 promoted hypoxia-responsive gene expression under hypoxia."
USP38 affects cell growth
| 2
USP38 inhibits cell growth.
| 1
| 1

reach
"USP38 inhibits colorectal cancer cell growth in vivo and in vitro."
USP38 activates cell growth.
| 1
| 1

reach
"Furthermore, FASN was critical for GC cell growth, migration and tumor development triggered by USP38 overexpression because its inhibitor orilistat reversed phenotypes in USP38 overexpressed GC cells."
USP38 affects c-Myc.Given
| 2
USP38 ubiquitinates c-Myc.Given.
| 1
USP38 leads to the ubiquitination of c-Myc.Given. 1 / 1
| 1

reach
"Together, these data imply that USP38 enhances c-Myc levels by inhibiting polyubiquitination and degradation of c-Myc.Given that USP38 can inhibit the degradation of c-Myc, we next determined the effe[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 deubiquitinates c-Myc.Given.
| 1
USP38 leads to the deubiquitination of c-Myc.Given. 1 / 1
| 1

reach
"Together, these data imply that USP38 enhances c-Myc levels by inhibiting polyubiquitination and degradation of c-Myc.Given that USP38 can inhibit the degradation of c-Myc, we next determined the effe[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 affects VEGFA
| 2
USP38 increases the amount of VEGFA. 2 / 2
| 2

reach
"We next confirmed that overexpression of USP38 together with HIF1α apparently enhanced the expression of BNIP3, LDHA, PDK1 and VEGFA (Fig. 1A)."

reach
"In the USP38-deficient H1299 cell, reconstitution of wild-type USP38 dramatically upregulated VEGFA expression, but reconstitution of the mutant, USP38-C454S/D918N, did not do so (Fig. 3, G and H)."
USP38 affects Th2 cytokines
| 2
USP38 increases the amount of Th2 cytokines.
| 1
USP38 increases the amount of Th2 cytokines. 1 / 1
| 1

reach
"USP38 deficiency in T cells resulted in dramatically reduced numbers of total BALF cells (Fig. 5 A), eosinophils and lymphocytes (Fig. 5 B), decreased Th2 cells (Fig. 5 C), and reduced secretion of Th2 cytokines (Fig. 5 D)."
USP38 activates Th2 cytokines.
| 1
USP38 activates Th2 cytokines. 1 / 1
| 1

reach
"Functionally, USP38 was necessary for production of Th2 cytokines (IL-4, IL-5 and IL-13) induced by TCR, and mice with USP38 knockout were refractory to asthma induced by OVA or HDM (Chen et al., 2018)."
USP38 affects PM2.5
| 2
USP38 inhibits PM2.5. 2 / 2
| 2

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"Conversely, overexpression of USP38 inhibited PM2.5‐induced cell apoptosis (Figure 2D and Figure S1E) and reduced PM2.5‐induced lactate production (Figure 2F)."

reach
"After administering the AKT inhibitor MK2206, the USP38‐mediated suppression of PM2.5‐induced cellular apoptosis and the subsequent activation of the AKT/mTOR signaling pathway were reduced (Figure 7D,E)."
USP38 affects NLRP4
| 2
| 2

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"To demonstrate the interaction between USP38 and NLRP4 in physiological conditions, we infected THP-1 cells or PBMCs with VSV-EGFP for the indicated time points, and we observed the enhanced interacti[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"Interaction between NLRP4 and USP38 was further increased after viral infection."
USP38 affects KLF5
| 2
USP38 deubiquitinates KLF5.
| 1
Sumoylated USP38 leads to the deubiquitination of KLF5. 1 / 1
| 1

reach
"SUMOylation of USP38 enhances the deubiquitination and stability of KLF5, thereby augmenting the malignant progression of LUAD."
USP38 decreases the amount of KLF5.
| 1
USP38 decreases the amount of KLF5. 1 / 1
| 1

reach
"Additionally, our results demonstrated that KLF5 overexpression restored the suppression of the malignant properties of LUAD cells by USP38 knockdown."
USP38 affects ISRE-luc
| 2
USP38 inhibits ISRE-luc.
| 1
USP38 inhibits ISRE-luc. 1 / 1
| 1

reach
"As IFN-β activation requires cooperative activation of IRF3 and NF-κB, we used an IFN-stimulated response element (ISRE) luciferase reporter to test whether USP38 directly affects IRF3 signaling, and [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 activates ISRE-luc.
| 1
USP38 activates ISRE-luc. 1 / 1
| 1

reach
"Moreover, USP38 knockdown blocked the USP38-mediated degradation of TBK1 and restored ISRE-luc activity ( Figures 4 D and 4E)."
USP38 affects IRF3
| 2
USP38 inhibits IRF3.
| 1
USP38 inhibits IRF3. 1 / 1
| 1

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"We next assessed phosphorylation of IRF3 in 293T cells, expressing USP38 together with RIG-I(N), MDA5, MAVS, STING-cGAS, or TRIF, and we found that USP38 inhibited the activation of IRF3 induced by al[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 dephosphorylates IRF3.
| 1
USP38 leads to the dephosphorylation of IRF3. 1 / 1
| 1

reach
"Consistent with this result, we found that USP38 knockdown markedly enhanced the phosphorylation of IRF3 upon these treatments ( Figure 1 D)."
USP38 affects IREB2
| 2
| 2

reach
"USP38 could bind to iron regulatory protein 2 (IRP2), stabilizing it and removing K48-linked polyubiquitination chains, leading to increasing intracellular iron overload, lipid peroxidation, and ultimately contribute to ferroptosis."

reach
"Mechanistically, USP38 bound to iron regulatory protein 2 (IRP2), stabilizing it and remove K48-linked polyubiquitination chains, thereby increasing intracellular iron overload, lipid peroxidation, and ultimately contributing to ferroptosis."
USP38 affects IFNB1
| 2
USP38 inhibits IFNB1.
| 1
USP38 inhibits IFNB1. 1 / 1
| 1

reach
"We found that USP38 potently inhibited the activation of IFN-β by treatments of intracellular (IC) low-molecular-weight (LMW) poly(I:C) (a ligand for RIG-I), IC high-molecular-weight (HMW) poly(I:C) ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 activates IFNB1.
| 1
USP38 activates IFNB1. 1 / 1
| 1

reach
"Usp38 −/− BMMs produced 2- to 4-fold more IFN-β in response to VSV or HSV-1 than WT BMMs ( Figures 2 A and 2B )."
USP38 affects HIPK2
| 2
USP38 inhibits HIPK2.
| 1
USP38 inhibits HIPK2. 1 / 1
| 1

reach
"Knockout of USP38 reduced the susceptibility of HFpEF hearts to VAs by inhibiting HIPK2 activation."
USP38 activates HIPK2.
| 1
USP38 activates HIPK2. 1 / 1
| 1

reach
"Mechanistically, USP38 deletion suppresses the activation of HIPK2 and its downstream mediators."
USP38 affects H2BC3
2 |
2 |

No evidence text available

No evidence text available
| 1 1

reach
"USP38 is expressed at low levels in ccRCC, and USP38-deficient mice have increased genomic instability, indicating that USP38 is a regulator of the DNA damage response [19]."

eidos
"It has been shown that USP38 affects DNA damage repair by regulating the activity of HDAC1 , meanwhile , a low expression of USP38 causes genome instability , which may lead to tumorigenesis [ 18 ] ."
| PMC
USP38 affects GST
| 2
USP38 binds GST. 2 / 2
| 2

sparser
"The molecular weight of USP38 is 116 kDa, making the molecular weight of the fusion protein GST-USP38 larger, approximately 137 kDa, and thus it is very difficult for bacteria to express GST-USP38 ectopically."

sparser
"However, we do not know whether this interaction is direct or indirect, because we could not induce the prokaryote Escherichia coli to express the fusion protein GST-USP38."
USP38 affects Fibrosis
| 2
| 2

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"Conversely, overexpression of USP38 accelerates the progression of cardiac hypertrophy and myocardial fibrosis."

reach
"Ubiquitin-specific protease 38 (USP38) was upregulated in the left atrium after aortic banding surgery.Cardiac-specific knockout of USP38 attenuated the atrial dilation and fibrosis and reduced the vulnerability of atrial fibrillation (AF) induced by pressure overload.Cardiac-specific overexpression of USP38 aggravated the atrial structural and electrical remodelling induced by pressure overload.Ubiquitin-specific protease 38 promoted atrial inflammation by interacting with and deubiquitinating nuclear factor-kappa B.Targeting USP38 may be an effective treatment for AF induced by pressure overload."
USP38 affects ESCC
| 2
USP38 activates ESCC. 2 / 2
| 2

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"Knockdown of USP38 inhibits ESCC growth."

reach
"Knockdown of USP38 inhibited ESCC growth."
USP38 affects E
| 2
USP38 binds E. 2 / 2
| 2

sparser
"Collectively, our results suggested that USP38 binds to the 132–193aa of E protein through its C-terminal domain."
| PMC

sparser
"More detailed truncation results showed that USP38 binds to 132–193aa of E protein ( xref I)."
| PMC
USP38 affects E protein polyubiquitination
| 2
USP38 inhibits E protein polyubiquitination. 2 / 2
| 2

eidos
"Meanwhile , USP38 decreased E protein polyubiquitination ."
| PMC

eidos
"Notably , ZIKV E protein polyubiquitination was catalyzed significantly by Myc-UB , catalyzed slightly by K48R or K63R , and the levels of E protein polyubiquitination were repressed by USP38 ( Figure 3D ) ."
| PMC
| 1 1
| 1 1

eidos
"In this research , we found that USP38 was overexpressed in GC tissues , and USP38 contributed to GC cell proliferation , migration and tumorigenesis ."

reach
"In this research, we found that USP38 was overexpressed in GC tissues, and USP38 contributed to GC cell proliferation, migration and tumorigenesis."
USP38 affects CD133
| 2
USP38 inhibits CD133.
| 1
USP38 inhibits CD133. 1 / 1
| 1

reach
"In both HCT116 and SW620 cells, simultaneous knockdown of USP38 and HDAC3 attenuated the decreased H3K27ac level and increased CD44 and CD133."
USP38 activates CD133.
| 1
USP38 activates CD133. 1 / 1
| 1

reach
"Surprisingly, our results showed that Aza treatment had no effect on USP38 mediated regulation of genes, while TSA treatment abolished USP38 mediated CD133, SOX2, and NANOG inhibition, suggesting that USP38 regulates CD133 via histone acetylation."
USP38 affects Akt-GSK3β/mTOR
| 2
USP38 activates Akt-GSK3β/mTOR. 2 / 2
| 2

reach
"Thus, these data suggest that USP38 promotes the Akt-GSK3β/mTOR pathway in pathological cardiac remodeling."

reach
"During our investigation into the USP38 mediated-signaling pathways, we demonstrated that Akt-GSK3β/mTOR signaling is dramatically activated by USP38 under hypertrophic stimulation."
Particulate Matter increases the amount of USP38.
1 |
Particulate Matter increases the amount of USP38. 1 / 1
1 |

No evidence text available
Particulate Matter decreases the amount of USP38.
1 |
Particulate Matter decreases the amount of USP38. 1 / 1
1 |

No evidence text available
NLRP4 affects USP38
| 2
| 2

reach
"To demonstrate the interaction between USP38 and NLRP4 in physiological conditions, we infected THP-1 cells or PBMCs with VSV-EGFP for the indicated time points, and we observed the enhanced interacti[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"Interaction between NLRP4 and USP38 was further increased after viral infection."
NFkappaB affects USP38
| 2
NFkappaB binds USP38. 2 / 2
| 2

sparser
"Finally, we detected the interaction of USP38 with NF-κB after Ang II administration by co-immunoprecipitation (Figure xref )."

sparser
"Mechanistically, USP38 interacts with NF-κB and mitigates the ubiquitination level of NF-κB, which promotes the activation of NLRP3."
IREB2 affects USP38
| 2
| 2

reach
"USP38 could bind to iron regulatory protein 2 (IRP2), stabilizing it and removing K48-linked polyubiquitination chains, leading to increasing intracellular iron overload, lipid peroxidation, and ultimately contribute to ferroptosis."

reach
"Mechanistically, USP38 bound to iron regulatory protein 2 (IRP2), stabilizing it and remove K48-linked polyubiquitination chains, thereby increasing intracellular iron overload, lipid peroxidation, and ultimately contributing to ferroptosis."
HMX3 affects USP38
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2 |

No evidence text available

No evidence text available
H2BC3 affects USP38
2 |
2 |

No evidence text available

No evidence text available
GST affects USP38
| 2
USP38 binds GST. 2 / 2
| 2

sparser
"The molecular weight of USP38 is 116 kDa, making the molecular weight of the fusion protein GST-USP38 larger, approximately 137 kDa, and thus it is very difficult for bacteria to express GST-USP38 ectopically."

sparser
"However, we do not know whether this interaction is direct or indirect, because we could not induce the prokaryote Escherichia coli to express the fusion protein GST-USP38."
E affects USP38
| 2
USP38 binds E. 2 / 2
| 2

sparser
"Collectively, our results suggested that USP38 binds to the 132–193aa of E protein through its C-terminal domain."
| PMC

sparser
"More detailed truncation results showed that USP38 binds to 132–193aa of E protein ( xref I)."
| PMC
CD28 affects USP38
| 2
CD28 activates USP38. 2 / 2
| 2

reach
"We observed that either anti-CD3/CD28 or anti-CD3 alone induced usp38 mRNA (Fig. 8, G and H)."

reach
"Similarly, USP38 protein was induced by anti-CD3/CD28 or anti-CD3 (Fig. 8, I and J), indicating that TCR signaling instead of CD28 signaling is responsible for USP38 induction."
2 |
Air Pollutants increases the amount of USP38.
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Air Pollutants increases the amount of USP38. 1 / 1
1 |

No evidence text available
Air Pollutants decreases the amount of USP38.
1 |
Air Pollutants decreases the amount of USP38. 1 / 1
1 |

No evidence text available
2 |
17beta-estradiol increases the amount of USP38.
1 |
17beta-estradiol increases the amount of USP38. 1 / 1
1 |

No evidence text available
17beta-estradiol decreases the amount of USP38.
1 |
17beta-estradiol decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1,2-dichloroethane decreases the amount of USP38. 2 / 2
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No evidence text available

No evidence text available
1 |
Zinc chromate increases the amount of USP38. 1 / 1
1 |

No evidence text available
Urethane affects USP38
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Urethane increases the amount of USP38. 1 / 1
1 |

No evidence text available
Trimellitic anhydride increases the amount of USP38. 1 / 1
1 |

No evidence text available
Topotecan affects USP38
1 |
Topotecan decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
1 |

No evidence text available
Tetrachloromethane decreases the amount of USP38. 1 / 1
1 |

No evidence text available
Sunitinib affects USP38
1 |
Sunitinib increases the amount of USP38. 1 / 1
1 |

No evidence text available
Silver(0) affects USP38
1 |
Silver(0) decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Pirimiphos-methyl decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |

No evidence text available
Paracetamol affects USP38
1 |
Paracetamol increases the amount of USP38. 1 / 1
1 |

No evidence text available
Oxaliplatin affects USP38
1 |
Oxaliplatin decreases the amount of USP38. 1 / 1
1 |

No evidence text available
Methylisothiazolinone increases the amount of USP38. 1 / 1
1 |

No evidence text available
Manganese(II) chloride increases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Manganese atom increases the amount of USP38. 1 / 1
1 |

No evidence text available
Leflunomide affects USP38
1 |
Leflunomide increases the amount of USP38. 1 / 1
1 |

No evidence text available
Lactate affects USP38
| 1
Lactate activates USP38. 1 / 1
| 1

reach
"Similarly, the addition of exogenous lactate also dose‐dependently upregulated USP38 (Figure 2A)."
Jinfukang affects USP38
1 |
Jinfukang decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-mir-4500 decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-mir-4458 decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-mir-3658 decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-98-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-7856-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-6831-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-590-3p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-5581-3p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-548e-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-4694-3p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-3927-3p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-376a-2-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-17-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-148a-3p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-124-3p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-let-7i-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-let-7g-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-let-7f-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-let-7e-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-let-7d-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-let-7c-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-let-7b-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Hsa-let-7a-5p decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Formaldehyde decreases the amount of USP38. 1 / 1
1 |

No evidence text available
Fenofibrate affects USP38
1 |
Fenofibrate increases the amount of USP38. 1 / 1
1 |

No evidence text available
Copper(II) sulfate increases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Cobalt dichloride increases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Chromium(6+) increases the amount of USP38. 1 / 1
1 |

No evidence text available
Choline affects USP38
1 |
Choline demethylates USP38. 1 / 1
1 |

No evidence text available
Cadmium dichloride increases the amount of USP38. 1 / 1
1 |

No evidence text available
Bis(2-ethylhexyl) phthalate increases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
1 |

No evidence text available
1 |

No evidence text available
Atrazine affects USP38
1 |
Atrazine decreases the amount of USP38. 1 / 1
1 |

No evidence text available
1 |
Arsenic atom increases the amount of USP38. 1 / 1
1 |

No evidence text available
| 1
| 1

reach
"153 In USP38-deficient allergic asthma models induced by OVA and aluminum, the total number of cells, eosinophils, and lymphocytes in BALF were significantly decreased, as well as the percentage and absolute count of Th2 cells in mediastinal lymph nodes detected by flow cytometry."
All-trans-retinoic acid increases the amount of USP38. 1 / 1
1 |

No evidence text available
ZHX2 affects USP38
1 |
1 |

No evidence text available
VIRMA affects USP38
1 |
1 |

No evidence text available
VAV2 affects USP38
1 |
1 |

No evidence text available
1 |
1 |

No evidence text available
USP38 affects uspC
| 1
USP38 inhibits uspC. 1 / 1
| 1

reach
"The results indicated that USP38, USP21, and USP30 are the most significantly downregulated USPs upon OGD/R treatment (Figure 1A)."
USP38 affects ubiquitination over-expressed E protein
| 1
USP38 inhibits ubiquitination over-expressed E protein. 1 / 1
| 1

eidos
"The results indicated that USP38 could strongly reduce the ubiquitination level of over-expressed E protein ( Figure 3A ) ."
| PMC
USP38 affects ubiquitination ZIKV E protein infected cells
| 1
USP38 inhibits ubiquitination ZIKV E protein infected cells. 1 / 1
| 1

eidos
"Similarly , the results showed that USP38 also significantly attenuated the ubiquitination level of ZIKV E protein in infected cells ( Figure 3B ) ."
| PMC
USP38 affects ubiquitination K33-linkage poly-ubiquitin chains
| 1
USP38 inhibits ubiquitination K33-linkage poly-ubiquitin chains. 1 / 1
| 1

eidos
"USP38 knockdown has enhanced the ubiquitination of K33-linkage poly-ubiquitin chains , but the formation of the k48-linked ubiquitin chain and the degradation of TBK1 are disrupted , indicating that the effects of DTX4 and TRIP on TBK1 depend on the presence of USP38 ."
USP38 affects ubiquitination E protein
| 1
USP38 inhibits ubiquitination E protein. 1 / 1
| 1

eidos
"We overexpressed USP38 in HEK293T cells and found that USP38 notably reduced the ubiquitination of E protein ."
| PMC
USP38 affects ubiquitin-proteasome
| 1
USP38 inhibits ubiquitin-proteasome. 1 / 1
| 1

reach
"Several regulators, including DTX4, NLRP4, TRIM27, USP38, TRIP, and TRAF3IP3, can degrade TBK1 via the ubiquitin-proteasome pathway [37–41]."
| 1
USP38 bound to FASN activates triglyceride. 1 / 1
| 1

reach
"Another study demonstrated that interaction between USP38 and FASN enhances the stability of FASN protein and increases triglyceride production in gastric cancer cells, which contributes to cell proliferation, migration, and tumorigenesis (Zheng et al. 2022)."
USP38 affects synthesis IFN
| 1
USP38 inhibits synthesis IFN. 1 / 1
| 1

eidos
"USP38 Inhibits ZIKV Infection Previous studies determined that , during viral infection , USP38 inhibits type I interferon pathway by degrading TBK1 , thereby inhibiting the synthesis of type I IFN [ 15 ] ."
| PMC
USP38 affects proteolysis
| 1
| 1

reach
"However, the mRNA level of TBK1 remained unchanged ( Figure 4 A), suggesting that USP38 causes TBK1 protein degradation."

reach
"USP38 Inhibits Zika Virus Infection by Removing Envelope Protein Ubiquitination."
USP38 affects polyubiquitination
| 1
USP38 inhibits polyubiquitination. 1 / 1
| 1

eidos
"USP38 can inhibit the polyubiquitination of c-Myc , thereby increasing c-Myc stability ."
USP38 affects migration
| 1
USP38 activates migration. 1 / 1
| 1

eidos
"In this research , we found that USP38 was overexpressed in GC tissues , and USP38 contributed to GC cell proliferation , migration and tumorigenesis ."

reach
"Activating USP38 can reduce LPS‐induced apoptosis in alveolar type II epithelial cells [33]."
USP38 affects ligand
| 1
USP38 inhibits ligand. 1 / 1
| 1

reach
"We found that USP38 potently inhibited the activation of IFN-β by treatments of intracellular (IC) low-molecular-weight (LMW) poly(I:C) (a ligand for RIG-I), IC high-molecular-weight (HMW) poly(I:C) ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 affects ion channel
| 1
USP38 decreases the amount of ion channel. 1 / 1
| 1

reach
"The above results demonstrated that USP38 overexpression could down-regulate the expression of cardiac ion channel protein after AB surgery."
USP38 affects interferon pathway
| 1
USP38 inhibits interferon pathway. 1 / 1
| 1

eidos
"USP38 Inhibits ZIKV Infection Previous studies determined that , during viral infection , USP38 inhibits type I interferon pathway by degrading TBK1 , thereby inhibiting the synthesis of type I IFN [ 15 ] ."
| PMC
USP38 affects inhibitory FBW7alpha
| 1
USP38 activates inhibitory FBW7alpha. 1 / 1
| 1

eidos
"Furthermore , USP38 can restore the inhibitory effect of FBW7alpha on proliferation ."

reach
"The stabilization of USP38 mRNA by METTL14 inhibits tumor migration, invasion, and EMT."
USP38 affects deacetylase
| 1
USP38 bound to K63 and HDAC1 activates deacetylase. 1 / 1
| 1

reach
"In response to DNA damage, USP38 interacted with HDAC1 and specifically removed the K63 linked ubiquitin chain promoting the deacetylase activity of HDAC1."

reach
"USP38 is induced by TCR signaling and in turn promotes JunB stabilization to specifically regulate Th2 cell differentiation."
| 1

reach
"We further noticed that elevated expression of USP38 reduced the expression and secretion of cell adhesion-related molecules with the elevation in expression of pro-apoptotic proteins, and these effects might be mediated by inhibition of JAK2/STAT3 signalling pathway as USP38 is the upstream regulator of STAT3 and inhibition of cellular adhesion process."
USP38 affects c-Myc stability
| 1
USP38 activates c-Myc stability. 1 / 1
| 1

eidos
"USP38 can inhibit the polyubiquitination of c-Myc , thereby increasing c-Myc stability ."
USP38 affects bleomycin-induced pulmonary fibrosis
| 1
USP38 inhibits bleomycin-induced pulmonary fibrosis. 1 / 1
| 1

eidos
"USP38 deficiency aggravates IL-33-induced lung inflammatory response and bleomycin-induced pulmonary fibrosis ."
USP38 affects activation IFN signaling pathways
| 1
USP38 inhibits activation IFN signaling pathways. 1 / 1
| 1

eidos
"For example , USP3 , USP38 , and USP19 target RIG-I , TBK1 , and TRAF3 for deubiquitination , respectively , thereby blocking the activation of type I IFN signaling pathways ( Cui et al ., 2014 ; Gu et al ., 2017 ; Lin et al ., 2016 ) ."
| 1

reach
"USP38 knockout decreased the susceptibility of VAs by shortening action potential duration (APD) and prolonging effective refractory period (ERP)."
USP38 affects ZIKV structural protein E non-structural protein
| 1
USP38 inhibits ZIKV structural protein E non-structural protein. 1 / 1
| 1

eidos
"The results indicated that , in Hela cells transfected with HA-USP38 and infected with ZIKV , the production of ZIKV structural protein E and non-structural protein 5 ( NS5 ) ( Figure 1A ) , the expression of E mRNA and NS5 mRNA ( Figure 1B ) , and the level of ZIKV mRNA ( Figure 1C ) were significantly attenuated by USP38 ."
| PMC
USP38 affects ZIKV mRNA
| 1
USP38 inhibits ZIKV mRNA. 1 / 1
| 1

eidos
"The results indicated that , in Hela cells transfected with HA-USP38 and infected with ZIKV , the production of ZIKV structural protein E and non-structural protein 5 ( NS5 ) ( Figure 1A ) , the expression of E mRNA and NS5 mRNA ( Figure 1B ) , and the level of ZIKV mRNA ( Figure 1C ) were significantly attenuated by USP38 ."
| PMC
USP38 affects ZIKV invasion
| 1
USP38 activates ZIKV invasion. 1 / 1
| 1

eidos
"Here , we demonstrate that , overexpression of USP38 in Hela cells markedly inhibited ZIKV infection , while deficient of USP38 increased ZIKV invasion ."
| PMC
USP38 affects ZIKV dsRNA
| 1
USP38 activates ZIKV dsRNA. 1 / 1
| 1

eidos
"Furthermore , immunofluorescence analyses indicated that the levels of ZIKV dsRNA were repressed by USP38 , but not by the mutant protein ( Figure 4E ) , suggesting that unlike USP38 , the mutant protein USP38-MUT failed to repress ZIKV infection ."
| PMC
USP38 affects ZIKV RNA
| 1
USP38 inhibits ZIKV RNA. 1 / 1
| 1

eidos
"Immunoblot analyses indicated that the levels of ZIKV E protein and NS5 protein were significantly attenuated by USP38 , but not by USP38-MUT ( Figure 4B ) , and similarly , qPCR results revealed that the levels of ZIKV N mRNA and NS5 mRNA ( Figure 4C ) as well as ZIKV RNA ( Figure 4D ) were significantly reduced by USP38 , but relatively unaffected by USP38-MUT ."
| PMC
USP38 affects ZIKV N mRNA NS5 mRNA
| 1
USP38 inhibits ZIKV N mRNA NS5 mRNA. 1 / 1
| 1

eidos
"Immunoblot analyses indicated that the levels of ZIKV E protein and NS5 protein were significantly attenuated by USP38 , but not by USP38-MUT ( Figure 4B ) , and similarly , qPCR results revealed that the levels of ZIKV N mRNA and NS5 mRNA ( Figure 4C ) as well as ZIKV RNA ( Figure 4D ) were significantly reduced by USP38 , but relatively unaffected by USP38-MUT ."
| PMC
USP38 affects ZIKV Infection Previous determined
| 1
USP38 inhibits ZIKV Infection Previous determined. 1 / 1
| 1

eidos
"USP38 Inhibits ZIKV Infection Previous studies determined that , during viral infection , USP38 inhibits type I interferon pathway by degrading TBK1 , thereby inhibiting the synthesis of type I IFN [ 15 ] ."
| PMC
USP38 affects ZHX2
1 |
1 |

No evidence text available

reach
"We found that USP38 potently inhibited the activation of IFN-β by treatments of intracellular (IC) low-molecular-weight (LMW) poly(I:C) (a ligand for RIG-I), IC high-molecular-weight (HMW) poly(I:C) ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 affects VIRMA
1 |
1 |

No evidence text available
USP38 affects VAV2
1 |
1 |

No evidence text available
USP38 affects Ubiquitin
| 1
| 1

reach
"Lin et al. found that knockout of USP38 increased K33-linked ubiquitylation and decreased K48 Ub-mediated degradation of TBK1 kinase, thus enhancing type I IFN signaling."
USP38 affects UBC
1 |
1 |

No evidence text available
USP38 affects Th2 genes
| 1
USP38 activates Th2 genes. 1 / 1
| 1

reach
"Accordingly, USP38 deficiency dramatically reduced the production of the Th2 genes under Th2 differentiation condition (Fig. 7 C)."
USP38 affects TWIST1
| 1
USP38 inhibits TWIST1. 1 / 1
| 1

reach
"USP38 negatively regulates cancer SCs in CRC via HDAC3 (histone deacetylase 3) deubiquitination and is downregulated in clinical CRC samples and cell lines."
USP38 affects TRIM16
1 |
1 |

No evidence text available
USP38 affects TRAF
| 1
USP38 inhibits TRAF. 1 / 1
| 1

reach
"On the other hand, USP38 can inhibit TRAF, inducing ST2L degradation via the autophagolysosomal pathway [102,103]."
USP38 affects TP53
| 1
USP38 bound to MDM2 decreases the amount of TP53. 1 / 1
| 1

reach
"Mechanistically, USP38 directly binds to MDM2, functioning as a deubiquitinating enzyme (DUB) to stabilize MDM2 and suppress p53 expression."
USP38 affects TLR
| 1
USP38 inhibits TLR. 1 / 1
| 1

reach
"We found that USP38 could also negatively regulate TLR and RIG-I signaling through different mechanisms (213, 214) ."
USP38 affects TBK1/AKT/CaMKII
| 1
USP38 activates TBK1/AKT/CaMKII. 1 / 1
| 1

reach
"Together, these results demonstrate that USP38 promotes the activation of the TBK1/AKT/CaMKII signaling pathway in mice with HF."
USP38 affects TBK1/AKT/CAMKII
| 1
USP38 activates TBK1/AKT/CAMKII. 1 / 1
| 1

reach
"In both in vivo and in vitro experiments, USP38 knockout inhibited TBK1/AKT/CAMKII signaling, whereas USP38 overexpression activated this pathway."
USP38 affects TBK1 proteasome
| 1
USP38 inhibits TBK1 proteasome. 1 / 1
| 1

eidos
"Collectively , USP38 could promotes TBK1 proteasome degradation and maintains the homeostasis of the antiviral response ( Lin et al ., 2016a ) ."
USP38 affects SOX2
| 1
USP38 activates SOX2. 1 / 1
| 1

reach
"Furthermore, we examined the protein levels of cancer stem cell related genes and found that downregulation of USP38 caused significant upregulation of cancer stem cell marker genes SOX2, NANOG, OCT4, BIM1, SNAIL, CD133, ABCG2, and CD44, suggesting that USP38 restrains cancer stem cell population of colorectal cancer cells."
USP38 affects SEM1
1 |
1 |

No evidence text available
USP38 affects RPS27A
1 |
1 |

No evidence text available
USP38 affects RPS12
1 |
1 |

No evidence text available
USP38 affects RPL7
1 |
1 |

No evidence text available
USP38 affects RIGI
| 1
USP38 inhibits RIGI. 1 / 1
| 1

reach
"We found that USP38 could also negatively regulate TLR and RIG-I signaling through different mechanisms (213, 214) ."
USP38 affects QARS1
1 |
1 |

No evidence text available
USP38 affects PDPK1
| 1
USP38 increases the amount of PDPK1. 1 / 1
| 1

reach
"We next confirmed that overexpression of USP38 together with HIF1α apparently enhanced the expression of BNIP3, LDHA, PDK1 and VEGFA (Fig. 1A)."
USP38 affects OGD/R
| 1
USP38 activates OGD/R. 1 / 1
| 1

reach
"USP38-overexpressing BM-MSC-EVs were produced to treat OGD/R-treated IEC-6 cells."

reach
"The stabilization of USP38 mRNA by METTL14 inhibits tumor migration, invasion, and EMT."
USP38 affects NOS2
| 1
USP38 increases the amount of NOS2. 1 / 1
| 1

reach
"Overexpression of USP38 significantly increased iNOS expression but had no significant effect on expression with CD163."
USP38 affects NLRP3
| 1
USP38 increases the amount of NLRP3. 1 / 1
| 1

reach
"Furthermore, our findings demonstrated that, after AB surgery, the elevated levels of NLRP3 were reduced in USP38 mice (Figure 7A), whereas USP38 overexpression led to further increase in the expression of NLRP3 (Figure 7B)."
USP38 affects NHEJ repair
| 1
USP38 activates NHEJ repair. 1 / 1
| 1

reach
"The deubiquitinase USP38 promotes NHEJ repair through regulation of HDAC1 activity and regulates cancer cell response to genotoxic insults."
USP38 affects NFKB1
| 1
USP38 increases the amount of NFKB1. 1 / 1
| 1

reach
"Mechanistically, USP38 interacted with and deubiquitinated nuclear factor-kappa B (NF-kappaB), and USP38 overexpression increased the level of p-NF-kappaB in vivo and in vitro, accompanied by the upregulation of NOD-like receptor protein 3 (NLRP3) and inflammatory cytokines, suggesting that USP38 contributes to adverse effects by driving NF-kappaB/NLRP3-mediated inflammatory responses."
USP38 affects NF-κB/NLRP3
| 1
USP38 activates NF-κB/NLRP3. 1 / 1
| 1

reach
"This indicates that USP38 promotes NF-κB/NLRP3 signalling-mediated inflammatory cytokines expression, exacerbating pressure overload-induced atrial remodelling."
USP38 affects MK-2206
| 1
| 1

reach
"After administering the AKT inhibitor MK2206, the USP38‐mediated suppression of PM2.5‐induced cellular apoptosis and the subsequent activation of the AKT/mTOR signaling pathway were reduced (Figure 7D,E)."
USP38 affects MDM2
| 1
| 1

reach
"Mechanistically, USP38 directly binds to MDM2, functioning as a deubiquitinating enzyme (DUB) to stabilize MDM2 and suppress p53 expression."
USP38 affects MCM6
1 |
1 |

No evidence text available
USP38 affects MAP3K7
| 1
USP38 activates MAP3K7. 1 / 1
| 1

reach
"However, USP38-mediated TAK1 regulation does not involve the DUB activity of USP38."
USP38 affects LUAD
| 1
Sumoylated USP38 activates LUAD. 1 / 1
| 1

reach
"SUMOylation of USP38 enhances the deubiquitination and stability of KLF5, thereby augmenting the malignant progression of LUAD."
USP38 affects LSD1.46
| 1
USP38 deubiquitinates LSD1.46. 1 / 1
| 1

reach
"USP38 promotes the ability of cellular drug tolerance and colony formation in colon cancer cells by deubiquitinating LSD1.46 Methylation of LSD1."
USP38 affects LGALS7B
1 |
1 |

No evidence text available
USP38 affects KRT6B
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No evidence text available
USP38 affects K63-linked ubiquitination E protein
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USP38 inhibits K63-linked ubiquitination E protein. 1 / 1
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eidos
"USP38 was capable to attenuate both K48 - and K63-linked ubiquitination of E protein to prevent ZIKV infection ."
| PMC
USP38 affects K63-linked polyubiquitination ZIKV E protein
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USP38 inhibits K63-linked polyubiquitination ZIKV E protein. 1 / 1
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"In summary , USP38 impairs both K48-linked polyubiquitination and K63-linked polyubiquitination of ZIKV E protein ."
| PMC
USP38 affects K63
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USP38 binds HDAC1 and K63. 1 / 1
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"In response to DNA damage, USP38 interacted with HDAC1 and specifically removed the K63 linked ubiquitin chain promoting the deacetylase activity of HDAC1."
USP38 affects K48-linked polyubiquitination
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USP38 inhibits K48-linked polyubiquitination. 1 / 1
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eidos
"In summary , USP38 impairs both K48-linked polyubiquitination and K63-linked polyubiquitination of ZIKV E protein ."
| PMC
USP38 affects JUN
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USP38 activates JUN. 1 / 1
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"The restoration study also confirmed the specificity of USP38 in TCR-induced JunB instead of c-Jun stability (Fig. 10 A)."
USP38 affects ISG
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USP38 decreases the amount of ISG. 1 / 1
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"Conversely, USP38 deficiency enhances type I IFN signaling, ISG expression, and antiviral immunity against both DNA and RNA viral infection."
USP38 affects IL1RL1
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USP38 activates IL1RL1. 1 / 1
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"On the other hand, USP38 can inhibit TRAF, inducing ST2L degradation via the autophagolysosomal pathway [102,103]."
USP38 affects IL-33-induced lung inflammatory response
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USP38 inhibits IL-33-induced lung inflammatory response. 1 / 1
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eidos
"USP38 deficiency aggravates IL-33-induced lung inflammatory response and bleomycin-induced pulmonary fibrosis ."
USP38 affects IFN-I
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USP38 inhibits IFN-I. 1 / 1
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"Similarly, USP38 negatively regulates IFN-I signaling by targeting the active form of TBK1 for degradation in vitro and in vivo (101)."
USP38 affects IFIH1
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USP38 inhibits IFIH1. 1 / 1
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"We found that USP38 potently inhibited the activation of IFN-β by treatments of intracellular (IC) low-molecular-weight (LMW) poly(I:C) (a ligand for RIG-I), IC high-molecular-weight (HMW) poly(I:C) ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 affects IC high-molecular-weight
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USP38 inhibits IC high-molecular-weight. 1 / 1
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"We found that USP38 potently inhibited the activation of IFN-β by treatments of intracellular (IC) low-molecular-weight (LMW) poly(I:C) (a ligand for RIG-I), IC high-molecular-weight (HMW) poly(I:C) ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 affects HSPB1
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No evidence text available
USP38 affects HFpEF hearts
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USP38 activates HFpEF hearts. 1 / 1
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"Knockout of USP38 reduced the susceptibility of HFpEF hearts to VAs by inhibiting HIPK2 activation."
USP38 affects HDAC3
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Modified USP38 decreases the amount of HDAC3. 1 / 1
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"Importantly, we found that USP38 overexpression significantly decreased the ubiquitination level of HDAC3 but not HDAC1 and had no effect on the overall protein level of HDAC3 and HDAC1."
USP38 affects HDAC
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USP38 activates HDAC. 1 / 1
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"Hence, we detected the global histone deacetylase (HDAC) activity in HCT116 cells with downregulated, normal, and upregulated levels of USP38, respectively and found that the global HDAC activities were significantly induced by downregulation of USP38 in HCT116 cells and SW620 cells while the global HDAC activities were inhibited in USP38 overexpressing HCT116 cells."
USP38 affects HCVgp1
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HCVgp1 binds USP38. 1 / 1
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No evidence text available
USP38 affects H3K56
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USP38 leads to the deacetylation of H3K56 on K63. 1 / 1
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"USP38 enhances the deacetylase activity of Histone deacetylase 1 (HDAC1) and promotes the deacetylation of H3K56 by eliminating the K63-linked polyubiquitin chains of HDAC1."
USP38 affects H3C12
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No evidence text available
USP38 affects Glioma
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USP38 inhibits Glioma. 1 / 1
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"In this study, we firstly constructed a USP38 overexpression and inhibition model in 2 cell lines and found that overexpression of USP38 inhibits the viability rate and migration ability of glioma cells."
USP38 affects GNB5
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No evidence text available
USP38 affects GC cell
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USP38 activates GC cell. 1 / 1
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"In this research , we found that USP38 was overexpressed in GC tissues , and USP38 contributed to GC cell proliferation , migration and tumorigenesis ."
USP38 affects ELK3
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USP38 activates ELK3. 1 / 1
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"USP38 knockout decreased the susceptibility of VAs by shortening action potential duration (APD) and prolonging effective refractory period (ERP)."
USP38 affects E mRNA NS5 mRNA
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USP38 inhibits E mRNA NS5 mRNA. 1 / 1
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"The results indicated that , in Hela cells transfected with HA-USP38 and infected with ZIKV , the production of ZIKV structural protein E and non-structural protein 5 ( NS5 ) ( Figure 1A ) , the expression of E mRNA and NS5 mRNA ( Figure 1B ) , and the level of ZIKV mRNA ( Figure 1C ) were significantly attenuated by USP38 ."
| PMC
USP38 affects DNA repair
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"Additionally, USP38 and USP28 both interact with DNA damage response proteins (GO response to ionizing radiation, FDR =7.0 × 10 and 3.0 × 10 for USP38 and USP28 respectively), supporting the hypothesis that these DUBs are involved in DNA repair (Figure 3b)."

reach
"USP38 is expressed at low levels in ccRCC, and USP38-deficient mice have increased genomic instability, indicating that USP38 is a regulator of the DNA damage response [19]."
USP38 affects DDX39A
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No evidence text available
USP38 affects DCT
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USP38 inhibits DCT. 1 / 1
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"We found that USP38 potently inhibited the activation of IFN-β by treatments of intracellular (IC) low-molecular-weight (LMW) poly(I:C) (a ligand for RIG-I), IC high-molecular-weight (HMW) poly(I:C) ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP38 affects CKB
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No evidence text available
USP38 affects CD68
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USP38 increases the amount of CD68. 1 / 1
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"Cardiac Conditional USP38 knockout (USP38-CKO) reduces the expression of the inflammatory marker CD68 as well as the inflammatory factors TNF-α and IL-1β after MI, thereby alleviating advanced cardiac fibrosis, electrical remodeling, ion channel remodeling, and susceptibility to VAs."
USP38 affects CD44
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USP38 inhibits CD44. 1 / 1
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"In both HCT116 and SW620 cells, simultaneous knockdown of USP38 and HDAC3 attenuated the decreased H3K27ac level and increased CD44 and CD133."
USP38 affects CACNA1C
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USP38 decreases the amount of CACNA1C. 1 / 1
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"This experiment observed that USP38 overexpression downregulated the expression level of Cav1.2, and the prolongation of APD may be attributed to the reduction of outward potassium current, exerting a stronger impact on APD."
USP38 affects BNIP3
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USP38 increases the amount of BNIP3. 1 / 1
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"We next confirmed that overexpression of USP38 together with HIF1α apparently enhanced the expression of BNIP3, LDHA, PDK1 and VEGFA (Fig. 1A)."
USP38 affects BMAL1
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No evidence text available
USP38 affects BAX
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USP38 increases the amount of BAX. 1 / 1
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"Conversely, the downregulated expression of another pro-apoptotic regulator BAX and the elevated expression of the anti-apoptotic marker BCL2, which was caused by excessive USP38, were reversed by BIRC5 knock-down (Figure 4J and K)."
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"USP38 exacerbates pressure overload-induced left ventricular electrical remodeling."
USP38 affects Asthma
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USP38 activates Asthma. 1 / 1
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"178 In the pathogenesis of allergic asthma, TCR signaling can upregulate the levels of the deubiquitinase USP38, which, in turn, stabilizes the TH2 development factor JunB, ultimately promoting asthma."

reach
"Ubiquitin specific peptidase 38 epigenetically regulates KLF transcription factor 5 to augment malignant progression of lung adenocarcinoma."
USP38 affects AKT-GSK3β/mTOR
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USP38 inhibits AKT-GSK3β/mTOR. 1 / 1
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"Amlexanox protects USP38 mediated cardiac remodeling, decreasing the protein expression of USP38-mediated TBK1/AKT-GSK3β/mTOR signaling pathway [158]."
USP38 affects AKT inhibitor
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USP38 inhibits AKT inhibitor. 1 / 1
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"After administering the AKT inhibitor MK2206, the USP38‐mediated suppression of PM2.5‐induced cellular apoptosis and the subsequent activation of the AKT/mTOR signaling pathway were reduced (Figure 7D,E)."
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"USP38 cardiac-conditional knockout attenuates LA inflammation at 3 days post-MI."
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"We found that USP38 potently inhibited the activation of IFN-β by treatments of intracellular (IC) low-molecular-weight (LMW) poly(I:C) (a ligand for RIG-I), IC high-molecular-weight (HMW) poly(I:C) ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
UBC affects USP38
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No evidence text available
Tobacco Smoke Pollution increases the amount of USP38. 1 / 1
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No evidence text available
TRIM16 affects USP38
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No evidence text available
TMT1B affects USP38
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TMT1B decreases the amount of USP38. 1 / 1
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"Impressively, METTL7B suppressed the expression of USP38 via m6A dependent mRNA degradation, resulting in increasing ubiquitylation of HDAC3, which is a proven histone lysine delactylases."
Soman affects USP38
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Soman increases the amount of USP38. 1 / 1
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No evidence text available
Smoke affects USP38
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Smoke decreases the amount of USP38. 1 / 1
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No evidence text available
SEM1 affects USP38
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No evidence text available
RPS27A affects USP38
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No evidence text available
RPS12 affects USP38
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No evidence text available
RPL7 affects USP38
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No evidence text available
QARS1 affects USP38
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No evidence text available
Protease affects USP38
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Protease leads to the deubiquitination of USP38. 1 / 1
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"Ubiquitin-specific protease 38 (USP38) was upregulated in the left atrium after aortic banding surgery.Cardiac-specific knockout of USP38 attenuated the atrial dilation and fibrosis and reduced the vulnerability of atrial fibrillation (AF) induced by pressure overload.Cardiac-specific overexpression of USP38 aggravated the atrial structural and electrical remodelling induced by pressure overload.Ubiquitin-specific protease 38 promoted atrial inflammation by interacting with and deubiquitinating nuclear factor-kappa B.Targeting USP38 may be an effective treatment for AF induced by pressure overload."
MIR587 affects USP38
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MIR587 decreases the amount of USP38. 1 / 1
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No evidence text available
MDM2 affects USP38
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"Mechanistically, USP38 directly binds to MDM2, functioning as a deubiquitinating enzyme (DUB) to stabilize MDM2 and suppress p53 expression."
MCM6 affects USP38
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No evidence text available
LGALS7B affects USP38
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No evidence text available
LDHA affects USP38
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No evidence text available
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L-methionine demethylates USP38. 1 / 1
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No evidence text available
KRT6B affects USP38
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No evidence text available
K63 affects USP38
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USP38 binds HDAC1 and K63. 1 / 1
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"In response to DNA damage, USP38 interacted with HDAC1 and specifically removed the K63 linked ubiquitin chain promoting the deacetylase activity of HDAC1."
IL1RL1 affects USP38
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IL1RL1 inhibits USP38. 1 / 1
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"In this study, we identified USP38, which negatively regulates IL-33-triggered signaling by mediating K27-linked deubiquitination of IL-33R at K511 and its autophagic degradation."
HSPB1 affects USP38
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No evidence text available
HIPK2 affects USP38
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HIPK2 activates USP38. 1 / 1
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"Overexpression of HIPK2 in the hearts of cardiac-specific USP38 knockout mice partially negated the beneficial effects of USP38 deletion on diastolic dysfunction and arrhythmogenesis."
HDAC1 affects K63, and USP38
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USP38 binds HDAC1 and K63. 1 / 1
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"In response to DNA damage, USP38 interacted with HDAC1 and specifically removed the K63 linked ubiquitin chain promoting the deacetylase activity of HDAC1."
HCVgp1 affects USP38
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HCVgp1 binds USP38. 1 / 1
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No evidence text available
H3C12 affects USP38
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No evidence text available
Gentamicins affects USP38
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Gentamicins increases the amount of USP38. 1 / 1
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No evidence text available
GNB5 affects USP38
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No evidence text available
DDX39A affects USP38
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No evidence text available
Cd4-Cre affects USP38
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Cd4-Cre inhibits USP38. 1 / 1
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"Through Cd4-Cre–mediated USP38 deficiency in T cells, we demonstrate the T cell intrinsic role of USP38 in asthma pathology."
CKB affects USP38
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No evidence text available
CD44 affects USP38
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CD44 inhibits USP38. 1 / 1
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"Importantly, flow cytometry analysis of cell surface markers revealed that the number of CD133 and CD44 double positive cells was significantly elevated in colorectal cancer cells transfected with shRNA targeting USP38 and the number of CD133 and CD44 double positive cells was significantly reduced in colorectal cancer cells overexpressing USP38."
BMAL1 affects USP38
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No evidence text available
BALF affects USP38
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BALF activates USP38. 1 / 1
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"153 In USP38-deficient allergic asthma models induced by OVA and aluminum, the total number of cells, eosinophils, and lymphocytes in BALF were significantly decreased, as well as the percentage and absolute count of Th2 cells in mediastinal lymph nodes detected by flow cytometry."
Asthma affects USP38
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Asthma inhibits USP38. 1 / 1
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"153 In USP38-deficient allergic asthma models induced by OVA and aluminum, the total number of cells, eosinophils, and lymphocytes in BALF were significantly decreased, as well as the percentage and absolute count of Th2 cells in mediastinal lymph nodes detected by flow cytometry."
AdshUSP38 affects USP38
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AdshUSP38 inhibits USP38. 1 / 1
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"In in vitro experiments, H9c2 cells were infected with AdshUSP38 to knockdown USP38 or with AdUSP38 to overexpress USP38, followed by treatment with 1uM Ang II. H9c2 cells infected with AdshRNA and AdGFP were used as the control group."

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"In addition, we demonstrate that adenosine deaminase acting on RNA (ADAR) could enhance the stability of USP38 protein and facilitate USP38 auto-deubiquitylation by interacting with USP38 in an RNA editing-independent manner."
Acrylamide affects USP38
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Acrylamide increases the amount of USP38. 1 / 1
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No evidence text available
| 1

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"Firstly, we analyzed the number of apoptotic cells in USP38 knock down and USP38 overexpressing HCT116 cells treated with 5-fluorouracil (5-FU), oxaliplatin (Oxal) or 5-FU plus Oxal (5-FU/Oxal)."

No evidence text available
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No evidence text available
2-palmitoylglycerol increases the amount of USP38. 1 / 1
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No evidence text available
2-hydroxypropanoic acid decreases the amount of USP38. 1 / 1
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No evidence text available
4,4'-sulfonyldiphenol decreases the amount of USP38. 1 / 1
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No evidence text available