IAPs, RINGs and ubiquitylation

被引：485

作者：

Vaux, DL ^{[1
]}

Silke, J ^{[1
]}

机构：

[1] Royal Melbourne Hosp, Walter & Eliza Hall Inst Med Res, Parkville, Vic 3050, Australia

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2005年 / 6卷 / 04期

关键词：

D O I：

10.1038/nrm1621

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The inhibitor of apoptosis (IAP) proteins all contain one or more baculoviral IAP repeat motifs, through which they interact with various other proteins. Many IAPs also have another zinc-binding motif, the RING domain, which can recruit E2 ubiquitin-conjugating enzymes and catalyse the transfer of ubiquitin onto target proteins. The number of targets of IAP-mediated ubiquitylation is increasing and recent results indicate that outcomes following ubiquitylation are tantalizingly complex. As well as regulating other proteins, the IAPs themselves are controlled by ubiquitin-mediated degradation.

引用

页码：287 / 297

页数：11

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