Protein kinase C phosphorylates tau and induces its functional alterations

FEBS Letters

Nishida, Eisuke¹  Miyoshi, Tomoko²  Akiyama, Tetsu²  Ogawara, Hiroshi²  Sakai, Hikoichi¹  Hoshi, Minako¹  Miyata, Yoshihiko¹ 

[1] Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Hongo, Tokyo 113 Japan;Department of Biochemistry, Meiji College of Pharmacy, Nozawa, Setagaya-ku, Tokyo 154, Japan

关键词: Phosphorylation;    Protein kinase C;    Actin cross-linking;    Microtubule assembly;    Microtubule-associated protein;   

DOI  :  10.1016/0014-5793(87)80670-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We found that tau, one of the major microtubule-associated proteins, is a good substrate for protein kinase C. The phosphorylation occurred mainly on serine residues and the sites phosphorylated by protein kinase C were largely different from those phosphorylated by cAMP-dependent protein kinase as analyzed by phosphopeptide mapping. The protein kinase C-mediated phosphorylation of tau reduced its abilities to promote tubulin polymerization and to cross-link actin filaments. The reduction in its abilities was in proportion to the number of phosphates incorporated into tau.

【 授权许可】

Unknown