A complex containing N-CoR, mSln3 and histone deacetylase mediates transcriptional repression

Thorsten Heinzel, Robert M. Lavinsky, Tina-Marie Mullen, Mats Söderström, Carol D. Laherty, Joseph Torchia, Wen-Ming Yang, Gyan Brard, Sally D. Ngo, James R. Davie, Edward Seto, Robert N. Eisenman, David W. Rose, Christopher K. Glass and Michael G. Rosenfeld
Additional contact information
Thorsten Heinzel: University of California
Robert M. Lavinsky: University of California
Tina-Marie Mullen: University of California
Mats Söderström: University of California
Carol D. Laherty: Fred Hutchinson Cancer Research Center
Joseph Torchia: University of California
Wen-Ming Yang: University of South Florida
Gyan Brard: University of California
Sally D. Ngo: University of California
James R. Davie: University of Manitoba
Edward Seto: University of South Florida
Robert N. Eisenman: Fred Hutchinson Cancer Research Center
David W. Rose: University of California
Christopher K. Glass: University of California
Michael G. Rosenfeld: University of California

Nature, 1997, vol. 387, issue 6628, 43-48

Abstract: Abstract Transcriptional repression by nuclear receptors has been correlated to binding of the putative co-repressor, N-CoR. A complex has been identified that contains N-CoR, the Mad presumptive co-repressor mSin3, and the histone deacetylase mRPD3, and which is required for both nuclear receptor- and Mad-dependent repression, but not for repression by transcription factors of the ets-domain family. These data predict that the ligand-induced switch of heterodimeric nuclear receptors from repressor to activator functions involves the exchange of complexes containing histone deacetylases with those that have histone acetylase activity.

Date: 1997
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DOI: 10.1038/387043a0

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