CREB-binding Protein and p300 in Transcriptional Regulation*

By Ngan K. Vo, R. Goodman. Journal of Biological Chemistry, 2001

890 citations recorded by the source corpus.

CREB-binding protein (CBP) and p300 are believed to participate in the activities of hundreds of different transcription factors (see Fig. 1). Current models suggest that the binding of these coactivators to transcription factor activation domains positions histone acetyltransferases (HATs) near specific nucleosomes in target gene promoter regions (for review, see Ref. 1). Interactions with components of the general transcriptional machinery, such as TFIID, TFIIB, and the RNA polymerase II holoenzyme (RNAPII) have also been suggested to contribute to CBP/p300 function. The simultaneous interaction of multiple transcription factors with CBP/p300 has been proposed to contribute to transcriptional synergy. Conversely, competition for CBP/p300 binding has been suggested to mediate some examples of signal-induced transcriptional repression. An overview of CBP/p300 in cellular growth and differentiation has recently been published (2), but many questions regarding their role in transcriptional regulation remain unanswered. This review deals with some of the more controversial aspects of CBP/p300 function. In particular, we will ask whether CBP and p300 have distinct functions, review the evidence for their regulation by phosphorylation, and ask whether they function primarily by acetylating histones or other proteins. We will also revisit the evidence for the role of CBP/p300 as transcriptional “integrators.” Finally, we will attempt to localize CBP/p300 function within the complex series of processes involved in transcriptional activation.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/910851ceedaf4bd90964bb0e8f4871fcf78663cb

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In Molecular Biology

  1. Cécile Rochette-Egly
  2. Bart Staels
  3. R. Simerly
  4. J. Bastien

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