Signal-specific co-activator domain requirements for Pit-1 activation

Lan Xu, Robert M. Lavinsky, Jeremy S. Dasen, Sarah E. Flynn, Eileen M. McInerney, Tina-Marie Mullen, Thorsten Heinzel, Daniel Szeto, Edward Korzus, Riki Kurokawa, Aneel K. Aggarwal, David W. Rose, Christopher K. Glass and Michael G. Rosenfeld ()
Additional contact information
Lan Xu: Howard Hughes Medical Institute, University of California at San Diego
Robert M. Lavinsky: Howard Hughes Medical Institute, University of California at San Diego
Jeremy S. Dasen: Howard Hughes Medical Institute, University of California at San Diego
Sarah E. Flynn: Howard Hughes Medical Institute, University of California at San Diego
Eileen M. McInerney: Howard Hughes Medical Institute, University of California at San Diego
Tina-Marie Mullen: Howard Hughes Medical Institute, University of California at San Diego
Thorsten Heinzel: Howard Hughes Medical Institute, University of California at San Diego
Daniel Szeto: Howard Hughes Medical Institute, University of California at San Diego
Edward Korzus: Howard Hughes Medical Institute, University of California at San Diego
Riki Kurokawa: Cellular and Molecular Medicine, and University of California at San Diego
Aneel K. Aggarwal: Mount Sinai School of Medicine
David W. Rose: Whittier Diabetes Program, University of California at San Diego
Christopher K. Glass: Cellular and Molecular Medicine, and University of California at San Diego
Michael G. Rosenfeld: Howard Hughes Medical Institute, University of California at San Diego

Nature, 1998, vol. 395, issue 6699, 301-306

Abstract: Abstract POU-domain proteins, such as the pituitary-specific factor Pit-1, are members of the homeodomain family of proteins which are important in development and homeostasis, acting constitutively or in response to signal-transduction pathways to either repress or activate the expression of specific genes1. Here we show that whereas homeodomain-containing repressors such as Rpx2 seem to recruit only a co-repressor complex, the activity of Pit-1 (ref. 3) is determined by a regulated balance between a co-repressor complex that contains N-CoR/SMRT4,5, mSin3A/B6,7,8 and histone deacetylases6,7,8 and a co-activator complex that includes the CREB-binding protein (CBP)9 and p/CAF10. Activation of Pit-1 by cyclic AMP or growth factors depends on distinct amino- and carboxy-terminal domains of CBP, respectively. Furthermore, thehistone acetyltransferase functions of CBP11,12 or p/CAF10 are required for Pit-1 function that is stimulated by cyclic AMP or growth factors, respectively. These data show that there is a switch in specific requirements for histone acetyltransferases and CBP domains in mediating the effects of different signal-transduction pathways on specific DNA-bound transcription factors.

Date: 1998
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DOI: 10.1038/26270

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