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RING domain dimerization is essential for RNF4 function
Journal article   Peer reviewed

RING domain dimerization is essential for RNF4 function

Chu Wai Liew, Huaiyu Sun, Tony Hunter and Catherine L Day
Biochemical journal, Vol.431(1), pp.23-29
01/10/2010
DOI: https://doi.org/10.1042/bj20100957
Handle:
https://hdl.handle.net/10523/32336

Abstract

Animals Dimerization Mice Models, Molecular Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism Protein Structure, Tertiary Rats Schizosaccharomyces - genetics Schizosaccharomyces - metabolism Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - metabolism Ubiquitin - metabolism Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism
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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