Phosphorylated CREB binds specifically to the nuclear protein CBP

John C. Chrivia, Roland P.S. Kwok, Ned Lamb, Masatoshi Hagiwara, Marc R. Montminy, Richard H. Goodman

Research output: Contribution to journalArticle

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Abstract

CYCLIC AMP-regulated gene expression frequently involves a DNA element known as the cAMP-regulated enhancer (CRE)1-4. Many transcription factors bind to this element, including the protein CREB5,6, which is activated as a result of phosphorylation by protein kinase A7. This modification stimulates interaction with one or more of the general transcription factors or, alternatively, allows recruitment of a co-activator. Here we report that CREB phosphorylated by protein kinase A binds specifically to a nuclear protein of M265K which we term CBP (for CREB-binding protein). Fusion of a heterologous DNA-binding domain to the amino terminus of CBP enables the chimaeric protein to function as a protein kinase A-regulated transcriptional activator. We propose that CBP may participate in cAMP-regulated gene expression by interacting with the activated phosphorylated form of CREB.

Original languageEnglish (US)
Pages (from-to)855-859
Number of pages5
JournalNature
Volume365
Issue number6449
DOIs
StatePublished - Jan 1 1993

ASJC Scopus subject areas

  • General

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    Chrivia, J. C., Kwok, R. P. S., Lamb, N., Hagiwara, M., Montminy, M. R., & Goodman, R. H. (1993). Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature, 365(6449), 855-859. https://doi.org/10.1038/365855a0