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Nature. 1993 Oct 28;365(6449):855-9.

Phosphorylated CREB binds specifically to the nuclear protein CBP.

Author information

1
Vollum Institute, Oregon Health Sciences University, Portland 97201.

Abstract

Cyclic AMP-regulated gene expression frequently involves a DNA element known as the cAMP-regulated enhancer (CRE). Many transcription factors bind to this element, including the protein CREB, which is activated as a result of phosphorylation by protein kinase A. 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 M(r) 265K 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.

PMID:
8413673
DOI:
10.1038/365855a0
[Indexed for MEDLINE]

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