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.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
MeSH terms
-
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
Substances
-
Nuclear Proteins
-
Transcription Factors
-
Ubiquitin
-
Rnf4 protein, mouse
-
Rnf4 protein, rat
-
Ubiquitin-Protein Ligases