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Biochem J. 2010 Oct 1;431(1):23-9. doi: 10.1042/BJ20100957.

RING domain dimerization is essential for RNF4 function.

Author information

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

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.

PMID:
20681948
PMCID:
PMC3104014
DOI:
10.1042/BJ20100957
[Indexed for MEDLINE]
Free PMC Article

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