IndraLab

Statements


UCHL5 affects SMAD2
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UCHL5 deubiquitinates SMAD2. 6 / 6
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"UCH5/UCH37 deubiquitinates both smad2 and smad3 to promote TGFβ-1 induced lung fibrosis [70]."

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"In the present study, we demonstrate that UCHL5 de-ubiquitinates and stabilizes Smad2 and Smad3, thereby promoting TGFbeta-1 signaling."

"Here, we report a novel interaction between smads and ubiquitin c-terminal hydrolase uch37, a deubiquitinating enzyme that could potentially reverse smurf-mediated ubiquitination. In gst pull down experiments, uch37 bound weakly to smad2 and smad3, and bound very strongly to smad7 in a region that is distinct from the -py- motif in smad7 that interacts with smurf ubiquitin ligases"

"Here, we report a novel interaction between smads and ubiquitin c-terminal hydrolase uch37, a deubiquitinating enzyme that could potentially reverse smurf-mediated ubiquitination. In gst pull down experiments, uch37 bound weakly to smad2 and smad3, and bound very strongly to smad7 in a region that is distinct from the -py- motif in smad7 that interacts with smurf ubiquitin ligases"

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"Here, we demonstrate that UCHL5 de-ubiquitinates and stabilizes Smad2 and Smad3, thereby promoting TGFbeta-1 signaling and contributes to the pathogenesis of pulmonary fibrosis."

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"Also, OTUB1 regulates only phosphorylated Smad2 and Smad3 under TGFbeta-1 treatment XREF_BIBR, while UCHL5 de-ubiquitinates Smad2 and Smad3 regardless of TGFbeta-1 treatment."
Modified UCHL5 leads to the deubiquitination of SMAD2. 1 / 1
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"We demonstrate that Smad2 and Smad3 ubiquitination was diminished by over-expression of UCHL5, while it was enhanced by inhibition or down-regulation of UCHL5."
UCHL5 affects SMAD3
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UCHL5 deubiquitinates SMAD3. 5 / 5
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"UCH5/UCH37 deubiquitinates both smad2 and smad3 to promote TGFβ-1 induced lung fibrosis [70]."

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"Here, we demonstrate that UCHL5 de-ubiquitinates and stabilizes Smad2 and Smad3, thereby promoting TGFbeta-1 signaling and contributes to the pathogenesis of pulmonary fibrosis."

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"In the present study, we demonstrate that UCHL5 de-ubiquitinates and stabilizes Smad2 and Smad3, thereby promoting TGFbeta-1 signaling."

"Here, we report a novel interaction between smads and ubiquitin c-terminal hydrolase uch37, a deubiquitinating enzyme that could potentially reverse smurf-mediated ubiquitination. In gst pull down experiments, uch37 bound weakly to smad2 and smad3, and bound very strongly to smad7 in a region that is distinct from the -py- motif in smad7 that interacts with smurf ubiquitin ligases"

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"Also, OTUB1 regulates only phosphorylated Smad2 and Smad3 under TGFbeta-1 treatment XREF_BIBR, while UCHL5 de-ubiquitinates Smad2 and Smad3 regardless of TGFbeta-1 treatment."
Modified UCHL5 leads to the deubiquitination of SMAD3. 1 / 1
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"We demonstrate that Smad2 and Smad3 ubiquitination was diminished by over-expression of UCHL5, while it was enhanced by inhibition or down-regulation of UCHL5."
UCHL5 affects NLRP3
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UCHL5 deubiquitinates NLRP3. 5 / 5
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"Moreover, UCHL5 overexpression enhanced protein stability by deubiquitinating NLRP3."

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"At last, UCHL5 inhibition enhanced osteoblast differentiation by promoting NLRP3 ubiquitination and degradation."

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"Deubiquitination of NLRP3 by UCHL5 is required for inflammasome activation."

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"Rv1579c, secreted from MTB H37Rv RD3, interacts with the receptor for activated C kinase 1 (RACK1) via its amino acid Y80 at the C-terminus, then recruits ubiquitin C-terminal hydrolase L5 (UCHL5) to deubiquitinate NLRP3, and finally activate the NLRP3 inflammasome [XREF_BIBR]."

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"Deubiquitination and Activation of the NLRP3 Inflammasome by UCHL5 in HCV-Infected Cells."
UCHL5 leads to the deubiquitination of NLRP3 on K48. 1 / 1
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"S3E), suggesting that UCHL5 mediates K48 deubiquitination of NLRP3 after EST12 stimulation."
UCHL5 affects TGFBR1
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UCHL5 deubiquitinates TGFBR1. 5 / 5
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"XREF_BIBR reported that UCHL5 de-ubiquitinates and stabilizes TbetaRI in human cancer cells."

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"One such DUB is UCH37, which was shown to bind to Smad7 and deubiquitinate TbetaRI."

"Via SMAD7, UCH37 can further be recruited to TβRI, where it removes polyubiquitin chains synthesized by SMURF"

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"It has been revealed that the DUBs, UCH37, USP11, and USP15, de-ubiquitinate and stabilize TbetaRI."

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"Similarly to USP15, another deubiquitylating enzyme, UCH37, forms a complex with Smad7 by binding to a sequence that is distinct from the PY motif with which Smurf1 or Smurf2 interact, and also deubiquitylates and stabilizes TbetaRI."
UCHL5 affects NFRKB
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UCHL5 deubiquitinates NFRKB. 5 / 5
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"LncRNA DRAIC inhibits proliferation and metastasis of gastric cancer cells through interfering with NFRKB deubiquitination mediated by UCHL5."

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"Combining the above results, it can be concluded that DRAIC mediates the ubiquitylation degradation of NFRKB by interfering with deubiquitination of NFRKB induced by UCHL5, and then exerts an anti-cancer effect in GC."

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"On the other hand, Zhang et al. found that lncRNA DRAIC could suppress GC metastasis of GC cells via through influencing NFRKB de-ubiquitination induced by UCHL5 27.EMT is considered to be a core factor of tumor metastasis, and it is clear that a variety of lncRNAs participated in GC development by regulating this cell program."

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"So we further tested the ubiquitination level of NFRKB, and found that the NFRKB ubiquitination level increased significantly after oeDRAIC, which could demonstrate that DRAIC weakens the deubiquitination of NFRKB mediated by UCHL5, and maintains the ubiquitination level of NFRKB and boost the degradation of NFRKB via the ubiquitination-proteasome pathway."

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"UCHL5 is also required for BLM/EXO1 dependent end resection through de-ubiquitinating the INO80 subunit NFRKB, although the function of this subunit in regulating end resection is not currently understood [37]."
UCHL5 affects TGFB
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UCHL5 deubiquitinates TGFB. 3 / 3
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"In addition, we show that UCH37 can deubiquitinate and stabilize the type I TGF-beta receptor."

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"The study hypothesized that Smad7 could act as an adaptor to recruit UCH37 to the type I TGF-beta receptor and showed that UCH37 dramatically up-regulates TGF-beta-dependent gene expression by deubiquitinating and stabilizing the type I TGF-beta receptor [XREF_BIBR]."

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"Wicks et al. reported that UCH37 can deubiquitinate and stabilize type I TGFbeta receptor and augment TGFbeta signaling [XREF_BIBR] (XREF_FIG)."
UCHL5 deubiquitinates TGFB on R1. 1 / 1
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"UCHL5 can deubiquitinate and stabilize Smads as well as TGF-beta receptor 1 (TGF-beta R1) and therefore activate TGF-beta signaling [XREF_BIBR]."
UCHL5 affects TCF7
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UCHL5 deubiquitinates TCF7. 4 / 4
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"Because Uch37 mediates deubiquitination of Tcf7 protein without affecting its stability, we next sought to elucidate the non proteolytic role of Uch37 mediated deubiquitination of Tcf7 and subsequent activation of Wnt signalling."

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"Here, we report that Uch37 mediates the deubiquitination of Tcf7 without affecting protein stability."

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"To further examine if Uch37 directly deubiquitinates Tcf7, we conducted in vitro deubiquitination assays using immunopurified Tcf7-ubiquitin conjugates."

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"However, deubiquitination of TCF7 by UCH37 is involved in TCF7 binding to the promoters of c-Myc, and Cyclin D1 [XREF_BIBR, XREF_BIBR]."
UCHL5 affects E2F1
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UCHL5 deubiquitinates E2F1. 4 / 4
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"Here we identify UCH37 as the first, to our knowledge, deubiquitinating enzyme for E2F1."

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"In addition, Uch37 deubiquitinates E2 promoter binding factor 1 (E2F1), promoting transcription of pro apoptotic and cell cycle related genes XREF_BIBR."

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"Instead, UCH37, but not a catalytically dead mutant, decreases the Lys-63-linked ubiquitination of E2F1 and activates its transcriptional activity."

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"UCHL5 activates the E2F1 transcriptional activity by decreasing Lys-63-linked ubiquitination of E2F1."
UCHL5 affects TGFBR
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UCHL5 deubiquitinates TGFBR. 2 / 2
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"In addition, we show that UCH37 can deubiquitinate and stabilize the type I TGF-beta receptor."

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"The study hypothesized that Smad7 could act as an adaptor to recruit UCH37 to the type I TGF-beta receptor and showed that UCH37 dramatically up-regulates TGF-beta-dependent gene expression by deubiquitinating and stabilizing the type I TGF-beta receptor [XREF_BIBR]."
UCHL5 deubiquitinates TGFBR on R1. 1 / 1
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"UCHL5 can deubiquitinate and stabilize Smads as well as TGF-beta receptor 1 (TGF-beta R1) and therefore activate TGF-beta signaling [XREF_BIBR]."
UCHL5 affects SMO
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UCHL5 deubiquitinates SMO. 3 / 3
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"UCHL5 could inhibit SMO ubiquitination and suppress PC-12 cell apoptosis during OGD/R."

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"We provide both genetic and biochemical evidence that UCHL5 interacts with and deubiquitinates Smo, increasing stability and promoting accumulation at the cell membrane."

"The deubiquitinase UCHL5/UCH37 positively regulates Hedgehog signaling by deubiquitinating Smoothened"
UCHL5 affects SMAD7
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UCHL5 deubiquitinates SMAD7. 2 / 2
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"Type 1 TGF-beta receptor (TGF-betaR1) is degraded by Smad7 dependent ubiquitination-proteasomal pathway, which is deubiquitinated by ubiquitin C-terminal hydrolase-L5 (UCHL5)."

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"Type I TGF-beta receptor (TGF-betaR I) is degraded by Smad7 dependent ubiquitination-proteasomal pathway, which is deubiquitinated by ubiquitin C-terminal hydrolase-L5 (UCHL5)."
UCHL5 affects Proteasome
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UCHL5 deubiquitinates Proteasome on S26. 1 / 1
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"Thus Uch37 and Usp14 may both deubiquitinate the 26S proteasome."
UCHL5 deubiquitinates Proteasome. 1 / 1
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"Another proposal is that UCH37 deubiquitylates proteasome subunits that can undergo regulatory ubiquitylation."

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"In addition, we show that UCH37 can deubiquitinate and stabilize the type I TGF-beta receptor."
UCHL5 affects epoxomicin
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UCHL5 deubiquitinates epoxomicin. 1 / 1
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"Neither ubiquitin-aldehyde, which inhibits deubiquitylation by Uch37, nor epoxomicin, which inhibits substrate proteolysis, changed the dwell time."
UCHL5 affects UbK48 chains
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UCHL5 deubiquitinates UbK48 chains. 1 / 1
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"UCH37 does not deubiquitinate UbK48 chains or affect E2F1 protein stability."
UCHL5 affects TGFbeta receptor
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UCHL5 deubiquitinates TGFbeta receptor. 1 / 1
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"Wicks et al. reported that UCH37 can deubiquitinate and stabilize type I TGFbeta receptor and augment TGFbeta signaling [XREF_BIBR] (XREF_FIG)."
UCHL5 affects TCF3
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UCHL5 deubiquitinates TCF3. 1 / 1
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"It was reported that UCHL5 deubiquitinates Tcf3, which helps it to fully activate the Wnt/β–catenin pathway [143]."
UCHL5 affects SMURF
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UCHL5 leads to the deubiquitination of SMURF. 1 / 1
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"Likely, UCH37 is found to connect to Smad7 and reverse Smurf-mediated ubiquitination [114]."
UCHL5 affects SMAD2_3
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UCHL5 deubiquitinates SMAD2_3. 1 / 1
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"We have shown that USP11 stabilizes TGF-β receptor II and UCHL5 deubiquitinates and stabilizes Smad2/3."
UCHL5 affects RI
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UCHL5 deubiquitinates RI. 1 / 1
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"UCH37, a member of DUBs, can deubiquitinate and stabilize the TβRI which is targeted for ubiquitylation-mediated degradation."
UCHL5 affects PRPF19
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UCHL5 deubiquitinates PRPF19. 1 / 1
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"Ubiquitin C-terminal Hydrolase 37, a novel predictor for hepatocellular carcinoma recurrence, promotes cell migration and invasion via interacting and deubiquitinating PRP19."
UCHL5 affects NOS2
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UCHL5 deubiquitinates NOS2. 1 / 1
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"In this study, we show that Rpn13 is involved in iNOS degradation and is required for iNOS interaction with the deubiquitination protein UCH37."
UCHL5 affects NFKBIA
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UCHL5 deubiquitinates NFKBIA. 1 / 1
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"Furthermore, we discovered that IkappaB-alpha, a protein whose proteasomal degradation activates the transcription factor NF-kappaB, is also a substrate for the Rpn13/UCH37 complex."
UCHL5 affects INO80
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UCHL5 deubiquitinates INO80. 1 / 1
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"UCHL5 is also required for BLM/EXO1 dependent end resection through de-ubiquitinating the INO80 subunit NFRKB, although the function of this subunit in regulating end resection is not currently understood [37]."
UCHL5 affects ELK3
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UCHL5 deubiquitinates ELK3. 1 / 1
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"Mechanistically, UCHL5 could directly deubiquitinate and stabilize ELK3 proteins."