Ontology highlight
ABSTRACT:
SUBMITTER: Subramaniam S
PROVIDER: S-EPMC2898300 | biostudies-literature | 2010 Jul
REPOSITORIES: biostudies-literature
Subramaniam Srinivasa S Mealer Robert G RG Sixt Katherine M KM Barrow Roxanne K RK Usiello Alessandro A Snyder Solomon H SH
The Journal of biological chemistry 20100427 27
We recently reported that the small G-protein Rhes has the properties of a SUMO-E3 ligase and mediates mutant huntingtin (mHtt) cytotoxicity. We now demonstrate that Rhes is a physiologic regulator of sumoylation, which is markedly reduced in the corpus striatum of Rhes-deleted mice. Sumoylation involves activation and transfer of small ubiquitin-like modifier (SUMO) from the thioester of E1 to the thioester of Ubc9 (E2) and final transfer to lysines on target proteins, which is enhanced by E3s. ...[more]