| First Author | Christian M | Year | 2004 |
| Journal | J Biol Chem | Volume | 279 |
| Issue | 15 | Pages | 15645-51 |
| PubMed ID | 14736873 | Mgi Jnum | J:114142 |
| Mgi Id | MGI:3688378 | Doi | 10.1074/jbc.M313906200 |
| Citation | Christian M, et al. (2004) Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140. J Biol Chem 279(15):15645-51 |
| abstractText | Receptor interacting protein (RIP) 140 is a corepressor that can be recruited to nuclear receptors by means of LXXLL motifs. We have characterized four distinct autonomous repression domains in RIP140, termed RD1-4, that are highly conserved in mammals and birds. RD1 at the N terminus represses transcription in the presence of trichostatin A, suggesting that it functions by a histone deacetylase (HDAC)-independent mechanism. The repressive activity of RD2 is dependent upon carboxyl-terminal binding protein recruitment to two specific binding sites. Use of specific inhibitors indicates that RD2, RD3, and RD4 are capable of functioning by HDAC-dependent and HDAC-independent mechanisms, depending upon cell type. |
