Phosphorylation of cAMP response element-binding protein, CRE-BP1, by cAMP-dependent protein kinase and protein kinase C.
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.
Sakurai
A
A
Department of Biochemistry, Kobe University School of Medicine, Japan.
Maekawa
T
T
Sudo
T
T
Ishii
S
S
Kishimoto
A
A
D000595:Amino Acid Sequence; D001665:Binding Sites; D000242:Cyclic AMP / Q000494:pharmacology*; D017362:Cyclic AMP Response Element-Binding Protein; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D014357:Trypsin
D017362:Cyclic AMP Response Element-Binding Protein; D004268:DNA-Binding Proteins; D011994:Recombinant Proteins; D010768:Phosphoserine; D000242:Cyclic AMP; D011494:Protein Kinases; D011493:Protein Kinase C; D014357:Trypsin