RING domain dimerization is essential for RNF4 function.
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.
Liew
Chu Wai
CW
Biochemistry Department, University of Otago, Dunedin 9054, New Zealand.
Sun
Huaiyu
H
Hunter
Tony
T
Day
Catherine L
CL
D000818:Animals; D019281:Dimerization; D051379:Mice; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D051381:Rats; D012568:Schizosaccharomyces / Q000235:genetics / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D025801:Ubiquitin / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D009687:Nuclear Proteins; D014157:Transcription Factors; D025801:Ubiquitin; C486410:Rnf4 protein, mouse; C486411:Rnf4 protein, rat; D044767:Ubiquitin-Protein Ligases