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Rpn13-Rpn2 complex structural analysis shows that RA190 targets hRpn13 and Uch37 through parallel mechanisms and at proteasomes, RA190-inactivated Uch37 cannot disassemble hRpn13-bound ubiquitin chains
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Our study provides a new mechanism for chromatin occupancy of Tcf7 and uncovers the physiological significance of Uch37 during early vertebrate development by regulating the Wnt/beta-catenin pathway.
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Our studies provide a molecular mechanism by which UCHL5 mitigates TGFbeta-1 signaling by stabilizing Smad2/Smad3. These data indicate that UCHL5 may contribute to the pathogenesis of idiopathic pulmonary fibrosis and may be a potential therapeutic target.
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Positive cytoplasmic UCHL5 tumor immunoexpression is linked to increased survival of patients with small (<5 cm) tumors (p = 0.001), disease stages I-II (p = 0.025), and age 66 years or older (p = 0.037). UCHL5 is thus a potential marker in gastric cancer with new prognostic relevance.
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our report demonstrates significant value in targeting USP14/UCHL5 with VLX1570 in drug-resistant Waldenstrom macroglobulinemia (WM) and carries a high potential for clinical translation
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UCHL5 is a promising novel prognostic marker in lymph-node-positive rectal cancer. Our results also advance the currently limited knowledge of biomarkers in colorectal cancer treatment.
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UCHL5 expression could function as a prognostic marker in pancreatic ductal adenocarcinoma, particularly at disease stages IIB to III. As UCHL5 is one of the few markers predicting increased survival, our results may be of clinical relevance.
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this work implicates hRpn13 and Uch37 in cell cycle progression, providing a rationale for their function in cellular proliferation and for the apoptotic effect of the hRpn13-targeting molecule RA190.
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These results uncover a novel mechanism for E2F1 transcriptional activation through removal of its Lys-63-linked ubiquitination by UCH37.
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Uch37 consists of two domains, a globular UCH-domain and a fibrous C-terminal tail. The C-terminal residues of Uch37 are implicated in Rpn13 binding.
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Data show that DEUBAD domain in RPN13 (ADRM1) activates ubiquitin thioesterase L5 (UCH-L5), and the related DEUBAD domain in INO80G (NFRKB) inhibits UCH-L5.
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Data indicate that ubiquitin thioesterase L5 UCH37 (UCHL5) comprises a catalytic UCH domain followed by the four-helix (alpha8-alpha11) C-terminal domain.
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High expression of UCH37 is significantly associated with epithelial ovarian cancer.
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b-AP15 is an inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance.
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UCH37 over-expression is associated with hepatocellular carcinoma recurrence.
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UCH37 is associated with outcome and recurrence of ESCC and can be a novel predictor for poor prognosis of esophageal squamous cell carcinoma patients after curative resection.
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a functional proteomic analysis was performed to screen UCH37-interacting proteins in hepatocellular carcinoma (HCC), and glucose-regulated protein 78 was identified as one interacting with UCH37
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our structures reveal conformationally dynamic parts of the enzyme that may play a role in the structural transition to the more active form.
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Silencing of UCH37 in A549 cells induced apoptosis.
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UCH37 interacts with Smads and regulates TGF-beta signalling.
