RING domain dimerization is essential for RNF4 function-Reference-Cited by-同舟云学术

RING domain dimerization is essential for RNF4 function

Published:2010-09-14 Issue:1 Volume:431 Page:23-29
ISSN:0264-6021
Container-title:Biochemical Journal
language:en
Short-container-title:

Author:

Liew Chu Wai¹,Sun Huaiyu²,Hunter Tony²,Day Catherine L.¹

Affiliation:

1. Biochemistry Department, University of Otago, Dunedin 9054, New Zealand

2. Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, U.S.A.

Abstract

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~ubiquitin thioester bond is regulated by RING domain dimerization.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://portlandpress.com/biochemj/article-pdf/431/1/23/662779/bj4310023.pdf

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