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Role of USP13 in physiology and diseases

Ubiquitin specific protease (USP)-13 is a deubiquitinase that removes ubiquitin from substrates to prevent protein degradation by the proteasome. Currently, the roles of USP13 in physiology and pathology have been reported. In physiology, USP13 is highly associated with cell cycle regulation, DNA da...

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Autores principales: Wang, Qian, Sun, Zhenzhen, Xia, Weiwei, Sun, Le, Du, Yang, Zhang, Yue, Jia, Zhanjun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9515447/
https://www.ncbi.nlm.nih.gov/pubmed/36188217
http://dx.doi.org/10.3389/fmolb.2022.977122
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author Wang, Qian
Sun, Zhenzhen
Xia, Weiwei
Sun, Le
Du, Yang
Zhang, Yue
Jia, Zhanjun
author_facet Wang, Qian
Sun, Zhenzhen
Xia, Weiwei
Sun, Le
Du, Yang
Zhang, Yue
Jia, Zhanjun
author_sort Wang, Qian
collection PubMed
description Ubiquitin specific protease (USP)-13 is a deubiquitinase that removes ubiquitin from substrates to prevent protein degradation by the proteasome. Currently, the roles of USP13 in physiology and pathology have been reported. In physiology, USP13 is highly associated with cell cycle regulation, DNA damage repair, myoblast differentiation, quality control of the endoplasmic reticulum, and autophagy. In pathology, it has been reported that USP13 is important in the pathogenesis of infection, inflammation, idiopathic pulmonary fibrosis (IPF), neurodegenerative diseases, and cancers. This mini-review summarizes the most recent advances in USP13 studies involving its pathophysiological roles in different conditions and provides new insights into the prevention and treatment of relevant diseases, as well as further research on USP13.
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spelling pubmed-95154472022-09-29 Role of USP13 in physiology and diseases Wang, Qian Sun, Zhenzhen Xia, Weiwei Sun, Le Du, Yang Zhang, Yue Jia, Zhanjun Front Mol Biosci Molecular Biosciences Ubiquitin specific protease (USP)-13 is a deubiquitinase that removes ubiquitin from substrates to prevent protein degradation by the proteasome. Currently, the roles of USP13 in physiology and pathology have been reported. In physiology, USP13 is highly associated with cell cycle regulation, DNA damage repair, myoblast differentiation, quality control of the endoplasmic reticulum, and autophagy. In pathology, it has been reported that USP13 is important in the pathogenesis of infection, inflammation, idiopathic pulmonary fibrosis (IPF), neurodegenerative diseases, and cancers. This mini-review summarizes the most recent advances in USP13 studies involving its pathophysiological roles in different conditions and provides new insights into the prevention and treatment of relevant diseases, as well as further research on USP13. Frontiers Media S.A. 2022-09-14 /pmc/articles/PMC9515447/ /pubmed/36188217 http://dx.doi.org/10.3389/fmolb.2022.977122 Text en Copyright © 2022 Wang, Sun, Xia, Sun, Du, Zhang and Jia. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Wang, Qian
Sun, Zhenzhen
Xia, Weiwei
Sun, Le
Du, Yang
Zhang, Yue
Jia, Zhanjun
Role of USP13 in physiology and diseases
title Role of USP13 in physiology and diseases
title_full Role of USP13 in physiology and diseases
title_fullStr Role of USP13 in physiology and diseases
title_full_unstemmed Role of USP13 in physiology and diseases
title_short Role of USP13 in physiology and diseases
title_sort role of usp13 in physiology and diseases
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9515447/
https://www.ncbi.nlm.nih.gov/pubmed/36188217
http://dx.doi.org/10.3389/fmolb.2022.977122
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