Building ubiquitin chains: E2 enzymes at work

被引：756

作者：

Ye, Yihong ^{[1
]}

Rape, Michael ^{[2
]}

机构：

[1] NIDDK, Mol Biol Lab, Natl Inst Hlth, Bethesda, MD 20892 USA

[2] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2009年 / 10卷 / 11期

关键词：

ANAPHASE-PROMOTING COMPLEX; KAPPA-B ACTIVATION; CONJUGATING ENZYME; POLYUBIQUITIN CHAINS; IN-VITRO; DNA-REPAIR; YEAST RAD6; BRCA1/BARD1; HETERODIMER; MOLECULAR DETERMINANTS; ALLOSTERIC ACTIVATION;

D O I：

10.1038/nrm2780

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The modification of proteins with ubiquitin chains can change their localization, activity and/or stability. Although ubiquitylation requires the concerted action of ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s), it is the E2s that have recently emerged as key mediators of chain assembly. These enzymes are able to govern the switch from ubiquitin chain initiation to elongation, regulate the processivity of chain formation and establish the topology of assembled chains, thereby determining the consequences of ubiquitylation for the modified proteins.

引用

页码：755 / 764

页数：10

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