Asymmetric Recruitment of cIAPs by TRAF2

被引：64

作者：

Mace, Peter D. ^{[1
]}

Smits, Callum ^{[1
]}

Vaux, David L. ^{[2
]}

Silke, John ^{[2
]}

Day, Catherine L. ^{[1
]}

机构：

[1] Univ Otago, Dept Biochem, Dunedin 9054, New Zealand

[2] La Trobe Univ, Dept Biochem, Bundoora, Vic 3086, Australia

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2010年 / 400卷 / 01期

关键词：

coiled coil; TRAF2; IAP; apoptosis; protein interactions; KAPPA-B ACTIVATION; SIGNALING COMPLEX; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; UBIQUITINATION; RECOGNITION; ASSOCIATION; INHIBITOR; BINDING; DOMAIN;

D O I：

10.1016/j.jmb.2010.04.055

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：

Cellular inhibitor of apoptosis protein (cIAP) 1 and cIAP2 set the balance between transcription factor and apoptosis signaling downstream of tumor necrosis factor (TNF) receptor superfamily members by acting as ubiquitin E3 ligases for substrates that are part of the TNF receptor complex. To fulfill this role, cIAPs must be recruited to the receptor complex by TNF-receptor-associated factor (TRAF) 2. In this study, we reconstituted the complex between baculoviral IAP repeat (BIR) 1 of cIAP1 and the coiled-coil region of TRAF2, solved the structure of BIR1 from cIAP1, and mapped key binding residues on each molecule using mutagenesis. Biophysical analysis indicates that a single BIR1 domain binds the trimeric TRAF2 coiled-coil domain. This suggests that only one TAP molecule binds to each TRAF timer and makes it likely that the dimeric cIAPs crosslink two TRAF trimers. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：8 / 15

页数：8

共 40 条

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