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A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression

Heinzel, T. (author)
University of California, San Diego, USA
Lavinsky, R. M. (author)
University of California, San Diego, USA
Mullen, T. M. (author)
University of California, San Diego, USA
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Söderström, Mats (author)
University of California, San Diego, USA
Laherty, C. D. (author)
Fred Hutchinson Cancer Research Center, Seattle, Washington, USA
Torchia, J. (author)
University of California, San Diego, USA
Yang, W. M. (author)
University of South Florida, Tampa, USA
Brard, G. (author)
University of California, San Diego, USA
Ngo, S. D. (author)
University of California, San Diego, USA
Davie, J. R. (author)
University of Manitoba, Winnipeg, Canada
Seto, E. (author)
University of South Florida, Tampa, USA
Eisenman, R. N. (author)
Fred Hutchinson Cancer Research Center, Seattle, Washington, USA
Rose, D. W. (author)
University of California, San Diego, USA
Glass, C. K. (author)
University of California, San Diego, USA
Rosenfeld, M. G. (author)
University of California, San Diego, USA
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 (creator_code:org_t)
Nature Publishing Group, 1997
1997
English.
In: Nature. - : Nature Publishing Group. - 0028-0836 .- 1476-4687. ; 387:6628, s. 43-48
Related links:
https://urn.kb.se/re...
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https://doi.org/10.1...
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  • Journal article (peer-reviewed)
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  • 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.

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