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Submitted on July 30, 2003
Accepted on September 8, 2003
1 INSERM U478 and INSERM U409, IFR Claude Bernard, Faculté de Médecine Xavier Bichat, 75870 Paris cedex 18, FRANCE. INSERM U579, Institut Pasteur, 75724 Paris cedex 15, FRANCE.
* To whom correspondence should be addressed. E-mail: mlombes{at}bichat.inserm.fr.
Molecular mechanisms underlying mineralocorticoid receptor (MR) mediated gene expression are not fully understood but seem to largely depend upon interactions with specific coregulators. To identify novel hMR molecular partners, yeast two-hybrid screenings performed using the N-terminal domain (NTD) as bait, allowed to isolate PIAS1 and PIASx
, described as SUMO E3-ligases. Specific interaction between PIAS1 and hMR was confirmed by GST pull-down experiments and N-terminal subdomains responsible for physical contacts were delineated. Transient transfections demonstrated that PIAS1 is a corepressor of aldosterone-activated MR transactivation but has no significant effect on hGR transactivation. The agonist or antagonist nature of the bound ligand also determines PIAS1 corepressive action. We provided evidence that PIAS1 conjugated SUMO-1 to hMR both in vitro and in vivo. Deciphering the unique sumoylation pattern of hMR, which possesses five consensus SUMO-1 binding sites, by combinatorial lysine substitutions, revealed a major impact of sumoylation on hMR properties. Using a MMTV promoter, PIAS1 action was independent of sumoylation whereas with GRE promoter, PIAS1 corepressive action depended on hMR sumoylation status. Taken together, our results identify a novel function for PIAS1 which interacts with the NTD of hMR and represses its ligand-dependent transcriptional activity, at least in part, through SUMO modifications.
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