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Publication : SUMOylation of the corepressor N-CoR modulates its capacity to repress transcription.

First Author  Tiefenbach J Year  2006
Journal  Mol Biol Cell Volume  17
Issue  4 Pages  1643-51
PubMed ID  16421255 Mgi Jnum  J:112468
Mgi Id  MGI:3656366 Doi  10.1091/mbc.E05-07-0610
Citation  Tiefenbach J, et al. (2006) SUMOylation of the corepressor N-CoR modulates its capacity to repress transcription. Mol Biol Cell 17(4):1643-51
abstractText  In the absence of ligands the corepressor N-CoR mediates transcriptional repression by some nuclear hormone receptors. Several protein-protein interactions of N-CoR are known, of which mainly complex formation with histone deacetylases (HDACs) leads to the repression of target genes. On the other hand, the role of posttranslational modifications in corepressor function is not well established. Here, we show that N-CoR is modified by Sumo-1. We found SUMO-E2-conjugating enzyme Ubc9 and SUMO-E3 ligase Pias1 as novel N-CoR interaction partners. The SANT1 domain of N-CoR was found to mediate this interaction. We show that K152, K1117, and K1330 of N-CoR can be conjugated to SUMO and that mutation of all sites is necessary to fully block SUMOylation in vitro. Because these lysine residues are located within repression domains I and III, respectively, we investigated a possible correlation between the functions of the repression domains and SUMOylation. Coexpression of Ubc9 protein resulted in enhanced N-CoR-dependent transcriptional repression. Studies using SUMOylation-deficient N-CoR RDI mutants suggest that SUMO modification contributes to repression by N-CoR. Mutation of K152 to R in RD1, for example, not only significantly reduced repression of a reporter gene, but also abolished the effect of Ubc9 on transcriptional repression.
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