Spotlights on ubiquitin-specific protease 12 (USP12) in diseases: from multifaceted roles to pathophysiological mechanisms.


Journal

Journal of translational medicine
ISSN: 1479-5876
Titre abrégé: J Transl Med
Pays: England
ID NLM: 101190741

Informations de publication

Date de publication:
26 Sep 2023
Historique:
received: 18 07 2023
accepted: 16 09 2023
medline: 21 11 2023
pubmed: 27 9 2023
entrez: 26 9 2023
Statut: epublish

Résumé

Ubiquitination is one of the most significant post-translational modifications that regulate almost all physiological processes like cell proliferation, autophagy, apoptosis, and cell cycle progression. Contrary to ubiquitination, deubiquitination removes ubiquitin from targeted protein to maintain its stability and thus regulate cellular homeostasis. Ubiquitin-Specific Protease 12 (USP12) belongs to the biggest family of deubiquitinases named ubiquitin-specific proteases and has been reported to be correlated with various pathophysiological processes. In this review, we initially introduce the structure and biological functions of USP12 briefly and summarize multiple substrates of USP12 as well as the underlying mechanisms. Moreover, we discuss the influence of USP12 on tumorigenesis, tumor immune microenvironment (TME), disease, and related signaling pathways. This study also provides updated information on the roles and functions of USP12 in different types of cancers and other diseases, including prostate cancer, breast cancer, lung cancer, liver cancer, cardiac hypertrophy, multiple myeloma, and Huntington's disease. Generally, this review sums up the research advances of USP12 and discusses its potential clinical application value which deserves more exploration in the future.

Identifiants

pubmed: 37752518
doi: 10.1186/s12967-023-04540-6
pii: 10.1186/s12967-023-04540-6
pmc: PMC10521459
doi:

Substances chimiques

Ubiquitin-Specific Proteases EC 3.4.19.12
USP12 protein, human 0
Ubiquitin Thiolesterase EC 3.4.19.12

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

665

Subventions

Organisme : Major Program of the National Natural Science Foundation of China
ID : 62227803
Organisme : National Natural Science Foundation of China
ID : 62141109
Organisme : Foreword Leading Technology Fundamental Research Project of Jiangsu
ID : BK20212012
Organisme : Jiangsu Province Social Development Project
ID : BE2022812

Informations de copyright

© 2023. The Author(s).

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Auteurs

Kaiyi Niu (K)

Hepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.

Yanlong Shi (Y)

Hepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.

Qingpeng Lv (Q)

Hepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.

Yizhu Wang (Y)

Hepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.

Jiping Chen (J)

Hepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.

Wenning Zhang (W)

Hepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.

Kung Feng (K)

Hepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.

Yewei Zhang (Y)

Hepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China. zhangyewei@njmu.edu.cn.

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