title: RING domain dimerization is essential for RNF4 function.
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.
authors.affiliation: Biochemistry Department, University of Otago, Dunedin 9054, New Zealand.
authors.forename: Chu Wai
authors.initials: CW
authors.lastname: Liew
authors.forename: Huaiyu
authors.initials: H
authors.lastname: Sun
authors.forename: Tony
authors.initials: T
authors.lastname: Hunter
authors.forename: Catherine L
authors.initials: CL
authors.lastname: Day
mesh_terms: 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
chemical_list: D009687:Nuclear Proteins; D014157:Transcription Factors; D025801:Ubiquitin; C486410:Rnf4 protein, mouse; C486411:Rnf4 protein, rat; D044767:Ubiquitin-Protein Ligases