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Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein


Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein



Journal of Biological Chemistry 271(30): 17957-17960



ISSN/ISBN: 0021-9258

PMID: 8663317

DOI: 10.1074/jbc.271.30.17957

Activating transcription factor 1 (ATF1) and the cAMP response element-binding protein (CREB) are members of the CREB/ATF family implicated in cAMP- and calcium-induced transcriptional activation. Although ATF1 and CREB share extensive homology, the function of ATF1 is poorly understood. Its phosphorylation state and activation by Ca-2+- and calmodulin-dependent protein kinase (CaMK) II were therefore examined. Phosphopeptide mapping analysis and Western blotting studies demonstrated that in vitro, CaMK II phosphorylates only Ser-63 (corresponding to Ser-133 of CREB), which is essential for the activation, and not Ser-72 (corresponding to Ser-142 of CREB), which is a negative regulation site. Both ATF1 and CREB bound CBP in a phosphorylation-dependent manner. As expected from these in vitro studies, transient transfection studies revealed that ATF1 is activated by CaMK II. Our findings suggest that CaMK II mediates transactivation of cAMP responsive genes via ATF1.

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Accession: 008258440

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