A SIM-ultaneous role for SUMO and ubiquitin

被引：185

作者：

Perry, J. Jefferson P. ^{[1
,2
]}

Tainer, John A. ^{[1
,3
]}

Boddy, Michael N. ^{[1
]}

机构：

[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

[2] Amrita Vishwa Vidyapeetham, Sch Biotechnol, Kollam, Kerala, India

[3] Lawrence Berkeley Natl Lab, Berkeley, CA 94720 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2008年 / 33卷 / 05期

关键词：

D O I：

10.1016/j.tibs.2008.02.001

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：

Ubiquitin and ubiquitin-like proteins (UbIs) share a P-GRASP fold and have key roles in cellular growth and suppression of genome instability. Despite their common fold, SUMO and ubiquitin are classically portrayed as distinct, and they can have antagonistic roles. Recently, a new family of proteins, the small ubiquitin-related modifier (SUMO)-targeted ubiquitin ligases (STUbLs), which directly connect sumoylation and ubiquitylation, has been discovered. Uniquely, STUbLs use SUMO-interaction motifs (SIMs) to recognize their sumoylated targets. STUbLs are global regulators of protein sumoylation levels, and cells lacking STUbLs display genomic instability and hypersensitivity to genotoxic stress. The human STUbL, RNF4, is implicated in several diseases including cancer, highlighting the importance of characterizing the cellular functions of STUbLs.

引用

页码：201 / 208

页数：8

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