RING domain dimerization is essential for RNF4 function.
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ABSTRACT:
SUBMITTER: Liew CW
PROVIDER: S-EPMC3104014 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Publications
RING domain dimerization is essential for RNF4 function.
Liew Chu Wai CW Sun Huaiyu H Hunter Tony T Day Catherine L CL
The Biochemical journal 20101001 1
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. ...[more]
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