Small ubiquitin-related modifier-1 ( SUMO-1) modification of the glucocorticoid receptor.
Small ubiquitin-related modifier-1 ( SUMO-1) is covalently attached to many cellular targets to regulate protein-protein and protein-DNA interactions, as well as localization and stability of the target protein. The SUMO-1-conjugating E2 enzyme Ubc9 is known to interact with the glucocorticoid receptor ( GR), a ligand-dependent transcription factor. In the present study, we show that GR is post-translationally modified by SUMO-1 (sumoylated) in a ligand-enhanced fashion. We identify experimentally three consensus SUMO attachment sites, two in the N-terminal transactivation region and one in the ligand-binding domain of GR. The two N-terminal sites are the major acceptor sites for SUMO-1 attachment. Mutation of these sites enhances transcriptional activity of GR on minimal promoters, but has no clear effect on the more complex mouse mammary tumour virus promoter. Thus SUMO-1 modification of GR influences receptor function in a promoter context-dependent fashion.[1]References
- Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor. Tian, S., Poukka, H., Palvimo, J.J., Jänne, O.A. Biochem. J. (2002) [Pubmed]
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