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Phosphorylation of cAMP response element-binding protein, CRE-BP1, by cAMP-dependent protein kinase and protein
1Department of Biochemistry, Kobe University School of Medicine, Japan.
Biochemical and Biophysical Research Communications
|December 16, 1991
Abstract:
The human recombinant CRE-BP1 was phosphorylated by cAMP-dependent protein kinase and protein kinase C, in vitro. These two protein kinases modified distinct serine residues of CRE-BP1. Ser-62 downstream of a putative metal finger structure of CRE-BP1 was the phosphorylation site by cAMP-dependent protein kinase, whereas two serine residues, Ser-340 and Ser-367, located in the basic region of this protein were the major protein kinase C phosphorylation sites. It seems possible that transcriptional and DNA-binding activities of CRE-BP1 are regulated by phosphorylation with these protein kinases.