Breaking the chains: structure and function of the deubiquitinases

被引：1658

作者：

Komander, David ^{[1
]}

Clague, Michael J. ^{[2
]}

Urbe, Sylvie ^{[2
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

[2] Univ Liverpool, Physiol Lab, Sch Biomed Sci, Liverpool L69 3BX, Merseyside, England

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2009年 / 10卷 / 08期

基金：

英国医学研究理事会;

关键词：

NF-KAPPA-B; UBIQUITIN-BINDING; CRYSTAL-STRUCTURE; ENZYME; PROTEIN; DOMAIN; SPECIFICITY; PROTEASOME; COMPLEX; A20;

D O I：

10.1038/nrm2731

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Ubiquitylation is a reversible protein modification that is implicated in many cellular functions. Recently, much progress has been made in the characterization of a superfamily of isopeptidases that remove ubiquitin: the deubiquitinases (DUBs; also known as deubiquitylating or deubiquitinating enzymes). Far from being uniform in structure and function, these enzymes display a myriad of distinct mechanistic features. The small number (< 100) of DUBs might at first suggest a low degree of selectivity; however, DUBs are subject to multiple layers of regulation that modulate both their activity and their specificity. Due to their wide-ranging involvement in key regulatory processes, these enzymes might provide new therapeutic targets.

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收藏

页码：550 / 563

页数：14

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