SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors

  • Mol Cell. 1998 Jul;2(1):33-42. doi: 10.1016/s1097-2765(00)80111-2.
C D Laherty  1 ,  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
Affiliations
  • 1. Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98104, USA.
PMID: 9702189 DOI: 10.1016/s1097-2765(00)80111-2
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.