环磷酸腺苷（cAMP）依赖性蛋白激酶和蛋白激酶C对环磷酸腺苷反应元件结合蛋白（CRE-BP1）的磷酸化作用
Phosphorylation of cAMP response element-binding protein, CRE-BP1, by cAMP-dependent protein kinase and protein kinase C.
作者信息
Sakurai A, Maekawa T, Sudo T, Ishii S, Kishimoto A
机构信息
Department of Biochemistry, Kobe University School of Medicine, Japan.
出版信息
Biochem Biophys Res Commun. 1991 Dec 16;181(2):629-35. doi: 10.1016/0006-291x(91)91237-7.
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.
在体外，人重组CRE - BP1被环磷酸腺苷（cAMP）依赖性蛋白激酶和蛋白激酶C磷酸化。这两种蛋白激酶修饰CRE - BP1不同的丝氨酸残基。CRE - BP1假定金属指结构下游的Ser - 62是cAMP依赖性蛋白激酶的磷酸化位点，而位于该蛋白碱性区域的两个丝氨酸残基Ser - 340和Ser - 367是蛋白激酶C的主要磷酸化位点。CRE - BP1的转录和DNA结合活性似乎有可能通过这些蛋白激酶的磷酸化作用来调节。
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