Phosphorylation of liver gap junction protein by protein kinase C

FEBS Letters

Shimazu, Takashi²  Takeda, Akira²  Yamamura, Hirohei¹  Hashimoto, Eikichi¹ 

[1] Department of Biochemistry, Fukui Medical School, Matsuoka, Fukui 910-11, Japan;Department of Medical Biochemistry, School of Medicine, Ehime University, Shigenobu, Ehime 791-02, Japan

关键词: Gap junction;    Protein kinase C;    cyclic AMP;    Protein phosphorylation;    (Rat liver);    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(87)81330-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 27 kDa protein, a major component of rat liver gap junctions, was shown to be phosphorylated in vitro by protein kinase C. The stoichiometry of the phosphorylation indicated that approx. 0.33 mol phosphate was incorporated per mol 27 kDa protein. Phosphorylation was entirely dependent on the presence of calcium and was virtually specific for serine residues. For comparison, the gap junction protein was also examined for its phosphorylation by cAMP-dependent protein kinase, the extent of phosphorylation being one-tenth that exerted by protein kinase C.

【 授权许可】

Unknown