RING domain dimerization is essential for RNF4 function

被引：70

作者：

Liew, Chu Wai ^{[1
]}

Sun, Huaiyu ^{[2
]}

Hunter, Tony ^{[2
]}

Day, Catherine L. ^{[1
]}

机构：

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

[2] Salk Inst Biol Studies, Mol & Cell Biol Lab, La Jolla, CA 92037 USA

来源：

BIOCHEMICAL JOURNAL | 2010年 / 431卷

关键词：

E3; ligase; protein domain; protein protein interaction; really interesting new gene finger (RING finger); RING finger protein 4 (RNF4); small ubiquitin-like modifier (SUMO); ubiquitin; UBIQUITIN-CONJUGATING ENZYME; SUMO; LIGASE; HETERODIMER; PML;

D O I：

10.1042/BJ20100957

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：

RNF4 [RING (really interesting new gene) finger protein 4] family ubiquitin ligases are RING E3 ligases that regulate the homoeostasis of SUMOylated proteins by promoting their ubiquitylation. In the present paper we report that the RING domain of RNF4 forms a stable dimer, and that dimerization is required for ubiquitin transfer. Our results suggest that the stability of the E2 similar to ubiquitin thioester bond is regulated by RING domain dimerization.

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页码：23 / 29

页数：7

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