RING domain dimerization is essential for RNF4 function
- 14 September 2010
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 431 (1), 23-29
- https://doi.org/10.1042/bj20100957
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.Keywords
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