Regulation of Deubiquitinating Enzymes by Post-Translational Modifications

被引：42

作者：

Das, Tanuza ^{[1
]}

Shin, Sang Chul ^{[1
]}

Song, Eun Joo ^{[2
,3
]}

Kim, Eunice EunKyeong ^{[1
]}

机构：

[1] Korea Inst Sci & Technol, Biomed Res Inst, Seoul 02792, South Korea

[2] Ewha Womans Univ, Grad Sch Pharmaceut Sci, Seoul 03760, South Korea

[3] Ewha Womans Univ, Coll Pharm, Seoul 03760, South Korea

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2020年 / 21卷 / 11期

基金：

新加坡国家研究基金会;

关键词：

post-translational modification (PTM); deubiquitinase (DUB); deubiquitinating enzyme; activity; localization; interaction; disease; TUMOR-SUPPRESSOR; UBIQUITIN DYNAMICS; PROTEIN STABILITY; DOWN-REGULATION; PHOSPHORYLATION; ACTIVATION; USP4; LOCALIZATION; SUMOYLATION; MECHANISMS;

D O I：

10.3390/ijms21114028

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Ubiquitination and deubiquitination play a critical role in all aspects of cellular processes, and the enzymes involved are tightly regulated by multiple factors including posttranslational modifications like most other proteins. Dysfunction or misregulation of these enzymes could have dramatic physiological consequences, sometimes leading to diseases. Therefore, it is important to have a clear understanding of these regulatory processes. Here, we have reviewed the posttranslational modifications of deubiquitinating enzymes and their consequences on the catalytic activity, stability, abundance, localization, and interaction with the partner proteins.

引用

页数：18

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