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Phosphorylated CREB binds specifically to the nuclear protein CBP.

Nature | Oct 28, 1993

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.

Pubmed ID: 8413673 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Base Sequence | Binding Sites | CREB-Binding Protein | Cell Line | Cloning, Molecular | Cyclic AMP | Cyclic AMP Response Element-Binding Protein | Cyclic AMP-Dependent Protein Kinases | DNA | Gene Expression Regulation | Genes, Reporter | Humans | Mice | Molecular Sequence Data | Nuclear Proteins | Phosphorylation | Protein Binding | Recombinant Fusion Proteins | Thyroid Gland | Trans-Activators | Transcription Factors

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