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Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB

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Abstract

A nuclear protein, CREB, has been isolated from rat brain and shown to stimulate transcription of the cyclic AMP-responsive gene somatostatin as a dimer. Biochemical analysis suggests that dimerization and transcriptional efficacy of CREB protein in vitro are regulated by phosphorylation. These findings demonstrate that cellular signals can modulate gene expression by regulating the covalent modification of pre-existing nuclear factors.

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Authors and Affiliations

  1. The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, 10010 North Torrey Pines Road, La Jolla, California, 92037, USA

    K. K. Yamamoto, G. A. Gonzalez, W. H. Biggs III & M. R. Montminy

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  1. K. K. Yamamoto
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  2. G. A. Gonzalez
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  3. W. H. Biggs III
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  4. M. R. Montminy
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Yamamoto, K., Gonzalez, G., Biggs, W. et al. Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB. Nature 334, 494–498 (1988). https://doi.org/10.1038/334494a0

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