| First Author | Chrivia JC | Year | 1993 |
| Journal | Nature | Volume | 365 |
| Issue | 6449 | Pages | 855-9 |
| PubMed ID | 8413673 | Mgi Jnum | J:34578 |
| Mgi Id | MGI:82033 | Doi | 10.1038/365855a0 |
| Citation | Chrivia JC, et al. (1993) Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 365(6449):855-9 |
| abstractText | 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. |
