Spotlight on USP4: Structure, Function, and Regulation
The deubiquitinating enzyme (DUB)–mediated cleavage of ubiquitin plays a critical role in balancing protein synthesis and degradation. Ubiquitin-specific protease 4 (USP4), a member of the largest subfamily of cysteine protease DUBs, removes monoubiquitinated and polyubiquitinated chains from its ta...
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2021-02-01
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doaj-dc1e5b5ee1ce4a4a88ea8a52882c3d122021-02-18T06:42:29ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2021-02-01910.3389/fcell.2021.595159595159Spotlight on USP4: Structure, Function, and RegulationBinbin Hu0Dingyue Zhang1Kejia Zhao2Yang Wang3Lijiao Pei4Qianmei Fu5Xuelei Ma6Department of Biotherapy, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Thoracic Surgery, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, ChinaThe deubiquitinating enzyme (DUB)–mediated cleavage of ubiquitin plays a critical role in balancing protein synthesis and degradation. Ubiquitin-specific protease 4 (USP4), a member of the largest subfamily of cysteine protease DUBs, removes monoubiquitinated and polyubiquitinated chains from its target proteins. USP4 contains a DUSP (domain in USP)–UBL (ubiquitin-like) domain and a UBL-insert catalytic domain, sharing a common domain organization with its paralogs USP11 and USP15. USP4 plays a critical role in multiple cellular and biological processes and is tightly regulated under normal physiological conditions. When its expression or activity is aberrant, USP4 is implicated in the progression of a wide range of pathologies, especially cancers. In this review, we comprehensively summarize the current knowledge of USP4 structure, biological functions, pathological roles, and cellular regulation, highlighting the importance of exploring effective therapeutic interventions to target USP4.https://www.frontiersin.org/articles/10.3389/fcell.2021.595159/fullUSP4deubiquitinaseNF-κBcancerinflammation |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Binbin Hu Dingyue Zhang Kejia Zhao Yang Wang Lijiao Pei Qianmei Fu Xuelei Ma |
spellingShingle |
Binbin Hu Dingyue Zhang Kejia Zhao Yang Wang Lijiao Pei Qianmei Fu Xuelei Ma Spotlight on USP4: Structure, Function, and Regulation Frontiers in Cell and Developmental Biology USP4 deubiquitinase NF-κB cancer inflammation |
author_facet |
Binbin Hu Dingyue Zhang Kejia Zhao Yang Wang Lijiao Pei Qianmei Fu Xuelei Ma |
author_sort |
Binbin Hu |
title |
Spotlight on USP4: Structure, Function, and Regulation |
title_short |
Spotlight on USP4: Structure, Function, and Regulation |
title_full |
Spotlight on USP4: Structure, Function, and Regulation |
title_fullStr |
Spotlight on USP4: Structure, Function, and Regulation |
title_full_unstemmed |
Spotlight on USP4: Structure, Function, and Regulation |
title_sort |
spotlight on usp4: structure, function, and regulation |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Cell and Developmental Biology |
issn |
2296-634X |
publishDate |
2021-02-01 |
description |
The deubiquitinating enzyme (DUB)–mediated cleavage of ubiquitin plays a critical role in balancing protein synthesis and degradation. Ubiquitin-specific protease 4 (USP4), a member of the largest subfamily of cysteine protease DUBs, removes monoubiquitinated and polyubiquitinated chains from its target proteins. USP4 contains a DUSP (domain in USP)–UBL (ubiquitin-like) domain and a UBL-insert catalytic domain, sharing a common domain organization with its paralogs USP11 and USP15. USP4 plays a critical role in multiple cellular and biological processes and is tightly regulated under normal physiological conditions. When its expression or activity is aberrant, USP4 is implicated in the progression of a wide range of pathologies, especially cancers. In this review, we comprehensively summarize the current knowledge of USP4 structure, biological functions, pathological roles, and cellular regulation, highlighting the importance of exploring effective therapeutic interventions to target USP4. |
topic |
USP4 deubiquitinase NF-κB cancer inflammation |
url |
https://www.frontiersin.org/articles/10.3389/fcell.2021.595159/full |
work_keys_str_mv |
AT binbinhu spotlightonusp4structurefunctionandregulation AT dingyuezhang spotlightonusp4structurefunctionandregulation AT kejiazhao spotlightonusp4structurefunctionandregulation AT yangwang spotlightonusp4structurefunctionandregulation AT lijiaopei spotlightonusp4structurefunctionandregulation AT qianmeifu spotlightonusp4structurefunctionandregulation AT xueleima spotlightonusp4structurefunctionandregulation |
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