USP31

Last update 08 May 2025

Basic Info

Synonyms

Deubiquitinating enzyme 31, KIAA1203, Ubiquitin carboxyl-terminal hydrolase 31

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Introduction

Deubiquitinase that recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. May play a role in the regulation of NF-kappa-B signaling pathway by deubiquitinating TRAF2. (Microbial infection) Plays a positive role in foot-and-mouth disease and classical swine fever viral infection. Mechanistically, associates with internal ribosomal entry site (IRES) element within the 5'-untranslated region of viral genomes to promote translation of the virus-encoded polyprotein.

100 Clinical Results associated with USP31

100 Translational Medicine associated with USP31

0 Patents (Medical) associated with USP31

Literatures (Medical) associated with USP31

01 May 2025·Virus Research

Common host factors for internal ribosomal entry site-mediated translation of viral genomic RNA: An investigation in foot-and-mouth disease and classical swine fever viruses

Article

Author: Kitab, Bouchra ; Akhter, Rupaly ; Tsukiyama-Kohara, Kyoko ; Hossain, Kazi Anowar ; Sakoda, Yoshihiro

We previously proposed polycystic kidney disease1-like 3 (PKD1L3) and ubiquitin-specific peptidase 31 (USP31) as potential common host factors for IRES-mediated RNA translation in infections with foot-and-mouth disease virus (FMDV) and classical swine fever virus (CSFV). However, those findings required substantiation, and the specific roles of these factors in the IRES-mediated translation remained unclear. Accordingly, in this study, we aimed to confirm the roles of PKD1L3 and USP31 as host factors associated with IRES activity in bi-cistronic reporter assays, and to investigate the interactions of these host proteins during IRES activity. PKD1L3 and USP31 silencing suppressed IRES activity in both FMDV and CSFV RNAs. PKD1L3 and USP31 overexpression had no significant effects. PKD1L3 and USP31 silencing also suppressed viral RNA replication for CSFV and infection with another picornavirus (from the same family as FMDV), encephalomyocarditis virus. Immunoprecipitation assays revealed that PKD1L3 and USP31 can interact with each other. We also examined their interaction with a eukaryotic translation factor involved in the IRES of hepatitis C virus (HCV), eIF3c. PKD1L3 and more pronouncedly USP31 can interact with eIF3c. Immunofluorescent assays revealed partial, cytoplasmic co-localization of USP31 with PKD1L3, eIF3c, and Hsp90β. Moreover, silencing of eIF3c and Hsp90β suppressed FMDV- and CSFV-IRES activity. Our results indicate the possibility that PKD1L3 and USP31 can participate in IRES activity by interacting with eIF3c and Hsp90β.

01 May 2025·International Immunopharmacology

Ubiquitin specific peptidase 13 protects against inflammation-associated joint injury in collagen-induced rheumatoid arthritis mice by targeting TRAF6

Article

Author: Wang, Yan ; Wang, Haili ; Sun, Yuman ; Sun, Xinyi ; Cui, Kai

Rheumatoid arthritis (RA) is a chronic inflammatory autoimmune disease with complex pathogenesis. Ubiquitin-specific protease 13 (USP13), a member of the deubiquitinating enzyme (DUB) superfamily, plays diverse roles in cellular events. This study investigates the role of USP13 in RA, revealing its significant downregulation in peripheral blood mononuclear cells (PBMCs) from RA patients compared to healthy individuals. USP13 expression negatively correlates with RA characteristics, including erythrocyte sedimentation rate (ESR), C-reactive protein (CRP), and rheumatoid factor (RF). Consistent with these findings, USP13 levels were reduced in knee joint synovial tissues of collagen-induced arthritis (CIA) mice and lipopolysaccharide (LPS)-stimulated bone marrow-derived macrophages (BMDMs). Mechanistically, USP13 directly interacts with tumor necrosis factor receptor-associated factor 6 (TRAF6), reducing its K63-linked polyubiquitination and thereby inhibiting TRAF6 expression. This interaction restrains nuclear factor κB (NF-κB) signaling, leading to a marked attenuation of LPS-induced inflammatory responses in BMDMs. Importantly, the anti-inflammatory effects of USP13 over-expression are largely dependent on TRAF6 suppression. In vitro, USP13 over-expression in BMDMs inhibits the proliferation of fibroblast-like synoviocytes (FLS) and osteoclastogenesis. In addition, USP13-overexpressing BMDMs in CIA mice significantly alleviates RA development, as evidenced by reduced synovial hyperplasia, inflammatory cell infiltration, cartilage destruction, and bone loss. These findings highlight the essential role of USP13 in macrophages during RA progression and reveal its therapeutic potential by targeting TRAF6 signaling.

01 Feb 2025·Recent Patents on Anti-Cancer Drug Discovery

USP31 Activates the Wnt/β-catenin Signaling Pathway and Promotes Gastric Cancer Cell Proliferation, Invasion and Migration

Article

Author: Ye, Limin ; Wu, Yueting ; Nie, Zhao ; Li, Lan ; Shui, Ling ; Cui, Yinying ; Zong, Zheng

Background:Gastric cancer (GC) has a poor prognosis because it is highly aggressive, yet there are currently few effective therapies available. Although protein ubiquitination has been shown to play a complex role in the development of gastric cancer, to date, no efficient ubiquitinating enzymes have been identified as treatment targets for GC.Methods:The TCGA database was used for bioinformatic investigation of ubiquitin-specific protease 31 (USP31) expression in GC, and experimental techniques, including Western blotting, qRT-PCR, and immunohistochemistry, were used to confirm the findings. We also analyzed the relationship between USP31 expression and clinical prognosis in patients with GC. We further investigated the effects of USP31 on the proliferation, invasion, migration, and glycolysis of GC cells in vitro and in vivo by using colony formation, CCK-8 assays, Transwell chamber assays, cell scratch assays, and cell-derived xenograft. Furthermore, we examined the molecular processes by which USP31 influences the biological development of GC.Results:Patients with high USP31 expression have a poor prognosis because USP31 is abundantly expressed in GC. Therefore, USP31 reduces the level of ubiquitination of the Wnt/β-catenin pathway by binding to β-catenin, thereby activating glycolysis, which ultimately promotes GC proliferation and aggressive metastasis.Conclusion:USP31 inhibits ubiquitination of β-catenin by binding to it, stimulates the Wnt/β-- catenin pathway, activates glycolysis, and accelerates the biology of GCs, which are all demonstrated in this work.

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USP31

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