| Literature DB >> 9702189 |
C D Laherty1, A N Billin, R M Lavinsky, G S Yochum, A C Bush, J M Sun, T M Mullen, J R Davie, D W Rose, C K Glass, M G Rosenfeld, D E Ayer, R N Eisenman.
Abstract
The transcriptional corepressor mSin3 is found in a large multiprotein complex containing the histone deacetylases HDAC1 and HDAC2, in addition to at least five tightly associated polypeptides. We have cloned and characterized a novel component of the mSin3 complex, SAP30, SAP30 binds to mSin3 and is capable of mediating transcriptional repression via histone deacetylases. SAP30 also binds the N-CoR corepressor and is required for N-CoR-mediated repression by antagonist-bound estrogen receptor and the homeodomain protein Rpx, as well as N-CoR suppression of transactivation by the POU domain protein Pit-1. However, SAP30 is not required for N-CoR-mediated repression by unliganded retinoic acid receptor or thyroid hormone receptor, suggesting that SAP30 is involved in the functional recruitment of the mSin3-histone deacetylase complex to a specific subset of N-CoR corepressor complexes.Entities:
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Year: 1998 PMID： 9702189 DOI： 10.1016/s1097-2765(00)80111-2
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970