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RING domain dimerization is essential for RNF4 function.

Authors
Type
Published Article
Journal
Biochemical Journal
Publisher
Portland Press
Volume
431
Issue
1
Pages
23–29
Identifiers
DOI: 10.1042/BJ20100957
Source
Hunter Lab
License
Unknown

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.

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