| First Author | Kim JY | Year | 2009 |
| Journal | Biochem Biophys Res Commun | Volume | 379 |
| Issue | 3 | Pages | 780-4 |
| PubMed ID | 19133230 | Mgi Jnum | J:145151 |
| Mgi Id | MGI:3833761 | Doi | 10.1016/j.bbrc.2008.12.155 |
| Citation | Kim JY, et al. (2009) A role of helix 12 of the vitamin D receptor in SMRT corepressor interaction. Biochem Biophys Res Commun 379(3):780-4 |
| abstractText | To repress gene transcription, the unliganded nuclear receptor (NR) recruits the N-CoR and SMRT corepressors via its direct association with the conserved motif within bipartite NR-interaction domains (IDs) of corepressors. We recently reported that SMRT is directly involved in the VDR-mediated repression via an ID1-specific interaction with the VDR. Here we show that removal of helix 12 from VDR (VDRDeltaAF2) converts it to a more potent repressor through additional interaction between the VDR and SMRT-ID2 in yeast and mammalian systems. These data suggest that the VDR helix 12 actively regulates the ID1 preference of the VDR by inhibiting ID2-VDR association. Using the one- plus two-hybrid system, we identified specific residues within the extended helix motif of SMRT-ID2 that are required for VDRDeltaAF2 binding. Analyses of these mutants also revealed the specific residues of SMRT-ID2 generally required for optimal NR binding as well as those involved in preferential interaction with specific NRs. |
