Nuclear protein CBP is a coactivator for the transcription factor CREB

Roland P.S. Kwok, James R. Lundblad, John C. Chrivia, Jane P. Richards, Hans Peter Bächinger, Richard G. Brennan, Stefan G.E. Roberts, Michael R. Green, Richard H. Goodman

Research output: Contribution to journalArticlepeer-review

1287 Scopus citations


The transcription factor CREB binds to a DNA element known as the cAMP-regulated enhancer (CRE)1-5. CREB is activated through phosphorylation by protein kinase A (PKA)6, but precisely how phosphorylation stimulates CREB function is unknown. One model is that phosphorylation may allow the recruitment of coactivators which then interact with basal transcription factors. We have previously identified a nuclear protein of Mr 265K, CBP, that binds specifically to the PKA-phosphorylated form of CREB7. We have used fluorescence anisotropy measurements to define the equi-librium binding parameters of the phosphoCREB:CBP interaction and report here that CBP can activate transcription through a region in its carboxy terminus. The activation domain of CBP interacts with the basal transcription factor TFIIB through a domain that is conserved in the yeast coactivator ADA-1 (ref. 8). Consistent with its role as a coactivator, CBP augments the activ-ity of phosphorylated CREB to activate transcription of cAMP-responsive genes.

Original languageEnglish (US)
Pages (from-to)223-226
Number of pages4
Issue number6486
StatePublished - 1994

ASJC Scopus subject areas

  • General


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