Zinc-finger UBPs: regulators of deubiquitylation

被引：74

作者：

Bonnet, Jacques ^{[1
]}

Romier, Christophe ^{[2
]}

Tora, Laszlo ^{[1
]}

Devys, Didier ^{[1
]}

机构：

[1] Univ Strasbourg 1, INSERM U 596, CNRS UMR 7104, IGBMC,Dept Funct Genom, Cu De Strasbourg, France

[2] Univ Strasbourg 1, INSERM U 596, CNRS UMR 7104, IGBMC,Dept Struct Biol & Genom, Cu De Strasbourg, France

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2008年 / 33卷 / 08期

关键词：

D O I：

10.1016/j.tibs.2008.05.005

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：

Deubiquitylating enzymes have key regulatory roles in multiple cellular processes by mediating ubiquitin removal and processing. The ubiquitin-specific processing proteases (USPs) represent the largest subclass of deubiquitylases. Recently, several USPs that recognize the monoubiquitylated histones H2A and/or H2B have been identified. Among these enzymes, three USPs contain a zinc-finger ubiquitin-specific protease (ZnF-UBP) domain, indicating that this domain plays a crucial part in regulating their activity. To address the putative function of this domain, we systematically analysed and aligned yeast and human ZnF-UBP-containing proteins. By complementing our analysis with structural and functional data, we present a classification of the different ZnF-UBP-containing proteins and a model for their regulation.

引用

页码：369 / 375

页数：7

共 38 条

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