ARTS and Siah Collaborate in a Pathway for XIAP Degradation

被引：51

作者：

Garrison, Jason B. ^{[1
,2
]}

Correa, Ricardo G. ^{[2
]}

Gerlic, Motti ^{[2
]}

Yip, Kenneth W. ^{[2
]}

Krieg, Andreas ^{[2
]}

Tamble, Craig M. ^{[2
]}

Shi, Ranxin ^{[2
]}

Welsh, Kate ^{[2
]}

Duggineni, Srinivas ^{[2
]}

Huang, Ziwei ^{[2
]}

Ren, Keqin ^{[1
]}

Du, Chunying ^{[1
]}

Reed, John C. ^{[2
]}

机构：

[1] Univ Cincinnati, Dept Canc & Cell Biol, Cincinnati, OH 45267 USA

[2] Sanford Burnham Med Res Inst, La Jolla, CA 92037 USA

来源：

MOLECULAR CELL | 2011年 / 41卷 / 01期

关键词：

UBIQUITIN-LIGASE ACTIVITY; KAPPA-B ACTIVATION; APOPTOSIS PROTEINS; STRUCTURAL BASIS; INHIBITION; IAPS; SMAC/DIABLO; MECHANISMS; EXPRESSION; LEUKEMIA;

D O I：

10.1016/j.molcel.2010.12.002

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：

ARTS (apoptosis-related protein in the TGF-beta signaling pathway) is a mitochondrial protein that binds XIAP (X-linked inhibitor of apoptosis protein) upon entering the cytosol, thus promoting cell death. Expression of ARTS is lost in some malignancies. Here, we show that ARTS binds to XIAP at BIR1, a domain distinct from the caspase-binding sites. Furthermore, ARTS interacts with the E3 ligase Siah-1 (seven in absentia homolog 1) to induce ubiquitination and degradation of XIAP. Cells lacking either Siah or ARTS contain higher steady-state levels of XIAP. Thus, ARTS serves as an adaptor to bridge Siah-1 to XIAP, targeting it for destruction.

引用

页码：107 / 116

页数：10

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