Biochem. J. (2002) 367
(907–911) (Printed in Great Britain)
Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor
Sha TIAN* , Hetti POUKKA* , Jorma J. PALVIMO*† and Olli A. JÄNNE*‡1
*Biomedicum Helsinki, Institute of Biomedicine, University of Helsinki, P.O. Box 63 (Haartmaninkatu 8), FIN-00014 Helsinki, Finland, †Institute of Biotechnology, P.O. Box 56, University of Helsinki, FIN-00014 Helsinki, Finland, and ‡Department of Clinical Chemistry, P.O. Box 63, University of Helsinki and Helsinki University Central Hospital, FIN-00014 Helsinki, Finland
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.
Key words: nuclear receptor, sumoylation, transactivation.
Abbreviations used: AR, androgen receptor; FBS, foetal bovine serum; GR, glucocorticoid receptor; K277R, Lys277
Arg; LUC, luciferase; PR, progesterone receptor; SUMO-1, small ubiquitin-related modifier-1.
1To whom correspondence should be addressed at Biomedicum Helsinki (e-mail olli.janne@helsinki.fi).
Received 10 July 2002; accepted 29 July 2002
Published as BJ Immediate Publication 29 July 2002, DOI 10.1042/BJ20021085
The Biochemical Society, London ©
2002
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