IndraLab

Statements


USP14 affects DVL
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USP14 deubiquitinates DVL. 10 / 11
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"Deubiquitination of Dishevelled by Usp14 is required for Wnt signaling."

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"These data suggest that deubiquitination of Dvl by Usp14 is necessary for the interaction between Fzd and Dvl."

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"Inhibition of USP14 increases Dvl polyubiquitination and significantly impairs downstream Wnt signaling."

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"A recent report has shown that deubiquitination of disheveled (Dvl) by USP14 is required for Wnt signaling."

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"Therefore, deubiquitination of Dvl by Usp14 may occur via their transient interaction during Wnt signal transduction."

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"To test direct deubiquitination of Dvl by Usp14, we performed a ubiquitin chain trimming assay using immunopurified Dvl-ubiquitin conjugates and recombinant Usp14 in a proteasome-free condition (XREF_FIG and XREF_SUPPLEMENTARY)."

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"As a lack of Dvl deubiquitination by Usp14 appears to attenuate Wnt signaling, we proposed that an elevated forward rate of ubiquitination, which will be counteracted by Usp14 activity, might be induced by Wnt3a CM treatment."

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"Effects of USP14 inhibitor IU1 confirmed that inhibition of USP14 by IU1 increases the K4 linked polyubiquitination of Dvl [XREF_BIBR]."

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"As inhibition of Usp14 activity increased Dvl polyubiquitination, we examined whether knockdown of Usp14 has any effect on Wnt signaling."

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"Contrary to its established mechanistic role, Usp14 mediates deubiquitination of Dvl without a requirement for its UBL domain."
USP14 affects CXCR4
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USP14 deubiquitinates CXCR4. 7 / 7
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"These data suggest that the USP14 gene product indeed serves as a catalyst to deubiquitinate the CXCR4, because when its expression is reduced there is a reciprocal increase in CXCR4 ubiquitination."

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"The physical interaction of CXCR4 and USP14 is paralleled by USP14 catalyzed deubiquitination of the receptor; knockdown of endogenous USP14 by RNA interference (RNAi) blocks CXCR4 deubiquitination, whereas overexpression of USP14 promotes CXCR4 deubiquitination."

"Co-localization of CXCR4 and USP14 also is time-dependent following CXCL12 stimulation."

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"In summary, our findings demonstrate that CXCL12 activation of the CXCR4 leads to a dynamic ubiquitination and deubiquitination cycle and that USP14 preferentially interacts with and deubiquitinates CXCR4."

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"Deubiquitination of CXCR4 by USP14 is critical for both CXCL12 induced CXCR4 degradation and chemotaxis but not ERK ativation."

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"Deubiquitination of CXCR4 by USP14 would thus be expected to reduce the rate of ligand accelerated receptor degradation and result in an increased steady state level of receptors."

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"Deubiquitination of CXCR4 by USP14 Is Critical for Both CXCL12 induced CXCR4 Degradation and Chemotaxis but Not ERK Activation *."
Modified USP14 leads to the deubiquitination of CXCR4. 2 / 2
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"The physical interaction of CXCR4 and USP14 is paralleled by USP14 catalyzed deubiquitination of the receptor; knockdown of endogenous USP14 by RNA interference (RNAi) blocks CXCR4 deubiquitination, whereas overexpression of USP14 promotes CXCR4 deubiquitination."

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"Overexpression of USP14 promotes CXCR4 deubiquitination and allows it to escape degradation [XREF_BIBR, XREF_BIBR]."
USP14 affects AR
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USP14 deubiquitinates AR. 6 / 6
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"USP14 inhibits AR ubiquitination and subsequent degradation in both prostate and breast cancer cells [77, 78]."

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"In addition, reduction of UCHL5 by its siRNA did not affect the expression of AR, suggesting that USP14 but not UCHL5 recruited on the19S proteasome plays a selective role in the deubiquitination of AR."

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"We found that IU1 and USP14 knockdown dramatically increased levels of ubiquitinated and K48 ubiquitinated AR, suggesting that USP14 is an AR DUB, capable of deubiquitinating and thereby stabilizing AR protein."

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"Treatment of control MDA-MB-453 (either scramble shRNA or parental) cells with CHX for up to 12h caused decreased levels of AR, suggesting a contribution of AR protein synthesis to endogenous AR protein levels; however, co-treatment of CHX and USP14 shRNA or IU1 resulted more rapid decrease in levels of endogenous AR protein, strongly suggest that deubiquitination of AR protein by USP14 is essential for its protein stability."

"Additionally, both genetic and pharmacological inhibition of USP14 significantly suppressed cell proliferation in AR-responsive breast cancer cells by blocking G0/G1 to S phase transition and inducing apoptosis."

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"Moreover, AR overexpression inhibited USP14 inhibition induced events, suggesting that AR deubiquitination by USP14 is critical for breast cancer growth and USP14 inhibition is a possible strategy to treat AR positive breast cancer."
USP14 affects Proteasome
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USP14 deubiquitinates Proteasome. 2 / 2
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"Given that proteasome deubiquitination mediated by USP14 has fundamental roles in regulating proteasomal degradation of ubiquitinylated substrates XREF_BIBR XREF_BIBR, it is rational to speculate that perturbation of ubiquitin chain trimming functions of PfUSP14 may impact intraerythrocytic parasite development and cause difficulties for parasite egress from the host cell."

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"USP14 deubiquitinates proteasome bound substrates that are ubiquitinated at multiple sites."
USP14 deubiquitinates Proteasome on S26. 2 / 2
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"Thus Uch37 and Usp14 may both deubiquitinate the 26S proteasome."

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"Thus the DUB activities of Uch37 and/or Usp14 appear to antagonize ubiquitination of the 26S proteasome."
USP14 leads to the deubiquitination of Proteasome on K48. 1 / 1
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"We found that inhibition of USP14 accelerated the K48 ubiquitination and proteasome mediated degradation of AR protein."
USP14 affects NLRC5
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USP14 deubiquitinates NLRC5. 5 / 5
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"The ubiquitination of NLRC5 could be reversely regulated by USP14."

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"In an effort to elucidate the mechanisms underlying this regulation, the Cui group showed that TLR4 stimulation activates the TRAF2/6 complex, which ubiquitinates NLRC5 on Lys1178 residue, presumably leading to its degradation and release of IKKalpha and IKKbeta to complex with IKKgamma [XREF_BIBR, XREF_BIBR] (XREF_FIG) This study also showed that the ubiquitin specific protease 14 (USP14) deubiquitinates NLRC5 to sustain the NLRC5 mediated inhibition of NF-kappaB activation."

"The researchers propose that, after the ubiquitination of NLRC5 at lysine 1178 is catalyzed by TRAF2/6, USP14 specifically removes the polyubiquitin chains from NLRC5 to enhance NLRC5-mediated inhibition of IKK–NF-κB signaling, thus forming a coherent feedforward loop to regulate IKK–NF-κB activation"

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"These results suggest that USP14 inhibits NLRC5 ubiquitination through its DUB activity."

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"Next, we determined whether USP14 inhibited NLRC5 ubiquitination through its DUB activity."
USP14 affects TAB2
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USP14 leads to the deubiquitination of TAB2. 4 / 4
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"Taken together, our data demonstrate that USP14 can negatively regulate autophagy induction by inhibiting Beclin 1 ubiquitination, interrupting association between TRAF6 and Beclin 1, and affecting TLR4-induced activation of NF-魏B through deubiquitination of TAB 2 protein"

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"Since USP14 induced the deubiquitination of TAB 2, we then examined the functional regulation of TLR4 mediated signaling in Ctrl and USP14 KD THP-1 cells."

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"These results suggest that USP14 induces the deubiquitination of TAB 2."

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"USP14 Induces Deubiquitination of TAB 2 and Inhibits TLR4 Mediated Signaling."
USP14 affects CREBBP
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USP14 deubiquitinates CREBBP. 2 / 2
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"To investigate whether USP14 deubiquitylated CBP, we transfected MLE12 cells to overexpress USP14 or treated them with IU1, and then we examined the ubiquitylation of CBP."

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"Furthermore, we revealed that USP14 deubiquitylated CBP and promoted its stability."
Modified USP14 leads to the deubiquitination of CREBBP. 1 / 1
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"We found that overexpression of USP14 reduced CBP ubiquitylation, whereas IU1 had the opposite effect (XREF_FIG)."
USP14 affects BECN1
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USP14 deubiquitinates BECN1. 3 / 3
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"Based on these previous findings, we hypothesized that the suppression of Beclin 1 ubiquitination by USP14 might be critically associated with TRAF6 mediated ubiquitination in both autophagy and TLR4 mediated signaling."

"USP14 regulates autophagy by suppressing K63 ubiquitination of Beclin 1"

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"The deubiquitination of BECLIN 1 by USP14 inhibits the PtdIns3P production of VPS34."
USP14 affects VIM
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USP14 deubiquitinates VIM. 2 / 2
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"Furthermore, USP14 can also deubiquitinate and stabilize vimentin, a vital protein which involves in epithelial-to-mesenchymal transition(EMT) and significantly promotes cell growth, migration and invasion in human gastric cancer"

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"According to the above results, USP14 de-ubiquitinates vimentin and increases its expression levels, which may influence the aggressiveness of GC cells."
USP14 affects FASN
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USP14 deubiquitinates FASN. 2 / 2
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"As shown in Figure 4b,c, USP14 slightly reduced FASN ubiquitination."
| PMC

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"Since USP14 reduced FASN protein levels in cancer cells, it was necessary to confirm the deubiquitination of FASN by USP14."
| PMC
USP14 affects CGAS
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USP14 deubiquitinates CGAS. 2 / 2
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"TRIM14 has been reported to interact with cGAS via its PRYSPRY domain and upon DNA virus infection recruit the proteasome-associated deubiquitinase (DUB) USP14 to deubiquitinate cGAS, preventing recruitment of p62 and autophagy-dependent degradation of cGAS (Jia et al., 2017) ."

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"TRIM14 has been reported to interact with cGAS via its PRYSPRY domain and upon DNA virus infection recruit the proteasome associated deubiquitinase (DUB) USP14 to deubiquitinate cGAS, preventing recruitment of p62 and autophagy dependent degradation of cGAS."

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"Consequently, USP14 deficiency may cause ataxia in the ax J mice in part by perturbing the turnover and/or cell surface distribution of GABA A R. Still, since it is not clear that USP14 directly deubiquitinates GABA A R, it is also worth considering that this DUB may regulate the receptor indirectly."
USP14 affects ZUP1
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USP14 deubiquitinates ZUP1. 1 / 1
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"Proteasomes function under tonic inhibitory conditions, possibly via the ubiquitin chain-trimming function of USP14, a proteasome-associated deubiquitinating enzyme (DUB)."
USP14 affects Wnt
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USP14 leads to the deubiquitination of Wnt. 1 / 1
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"Genetic and chemical suppression of USP14 activity caused an increase in Dishevelled (Dvl) polyubiquitination and significantly impaired downstream Wnt signaling, suggesting an oncogenic role for USP14 through Wnt and beta-catenin signaling enhancement [XREF_BIBR]."
USP14 affects WT NCB1
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USP14 deubiquitinates WT NCB1. 1 / 1
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"When we quenched substrate degradation by replacing ATP with ADP (XREF_FIG), USP14 dependent deubiquitination of WT NCB1 conjugates was preserved (XREF_FIG)."
USP14 affects IKBKB
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USP14 deubiquitinates IKBKB. 1 / 1
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"This study suggests that USP14 removes the ubiquitin chain of I-κB, therefore inducing I-κB degradation and increasing cytokine release in lung epithelial cells."
USP14 affects GABBR1
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USP14 deubiquitinates GABBR1. 1 / 1
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"Post-endocytotic Deubiquitination and Degradation of the Metabotropic γ-Aminobutyric Acid Receptor by the Ubiquitin-specific Protease 14"
USP14 affects ELOVL6
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USP14 deubiquitinates ELOVL6. 1 / 1
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"Among the potential substrates identified, we show that fatty acid synthase (FASN), a key enzyme involved in hepatic lipogenesis, is a bona fide substrate of USP14."
USP14 affects DVL2
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USP14 deubiquitinates DVL2. 1 / 1
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"Usp14 deubiquitinates K63-linked polyubiquitin chains of Dvl"
USP14 affects DDX58
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USP14 deubiquitinates DDX58. 1 / 1
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"n this study, we demonstrated USP14, a deubiquitinating enzyme, as a negative regulator in antiviral responses by directly deubiquitinating K63-linked RIG-I."
USP14 affects CyclinB1
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USP14 deubiquitinates CyclinB1. 1 / 1
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"CyclinB1 deubiquitination by USP14 regulates cell cycle progression in breast cancer."
USP14 affects CTNNB1
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USP14 deubiquitinates CTNNB1. 1 / 1
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"Additionally, DUBs USP14, USP15, USP47, and Fam/USP9X have been reported to prevent β-catenin turnover by inhibiting its Ub-proteasomal degradation"
USP14 affects BUR6
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USP14 deubiquitinates BUR6. 1 / 1
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"USP14 deubiquitinated this form of NCB1 at a rate comparable to that of wild-type conjugates, indicating that USP14 does not act obligatorily on ubiquitin-ubiquitin linkages (XREF_FIG)."
USP14 affects AURKB
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USP14 deubiquitinates AURKB. 1 / 1
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"The Deubiquitinating Enzyme USP14 Regulates Leukemic Chemotherapy Drugs-Induced Cell Apoptosis by Suppressing Ubiquitination of Aurora Kinase B"