Deubiquitinating enzymes as cellular regulators

被引：125

作者：

Kim, JH ^{[1
]}

Park, KC ^{[1
]}

Chung, SS ^{[1
]}

Bang, O ^{[1
]}

Chung, CH ^{[1
]}

机构：

[1] Seoul Natl Univ, Sch Biol Sci, NRL Prot Biochem, Seoul 151742, South Korea

来源：

JOURNAL OF BIOCHEMISTRY | 2003年 / 134卷 / 01期

基金：

新加坡国家研究基金会;

关键词：

deubiquitinating enzyme; JAMM; otubain; ubiquitin C-terminal hydrolase; ubiquitin-specific processing protease;

D O I：

10.1093/jb/mvg107

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：

Modification of proteins by the covalent attachment of ubiquitin is a key regulatory mechanism of many cellular processes including protein degradation by the 26S proteasome. Deubiquitination, reversal of this modification, must also regulate the fate and function of ubiquitin-conjugated proteins. Deubiquitinating enzymes catalyze the removal of ubiquitin from ubiquitin-conjugated substrate proteins as well as from its precursor proteins. Deubiquitinating enzymes occupy the largest family of enzymes in the ubiquitin system, implying their diverse function in regulation of the ubiquitin-mediated pathways. Here we explore the diversity of deubiquitinating enzymes and their emerging roles as cellular regulators.

引用

页码：9 / 18

页数：10

共 112 条

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