Association of a myristoylated protein with a biological membrane and its increased phosphorylation by protein kinase C

FEBS Letters

Utsumi, Kozo¹  Koga, Daizo²  Okimasu, Eiji¹  Yoshinaga, Koji²  Utsumi, Toshihiko²  Ide, Akio²  Nobori, Koichi¹  Terada, Shigeo¹ 

[1] Department of Medical Biology, Kochi Medical School, Kochi 781-51, Japan;Laboratory of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753, Japan

关键词: Protein myristoylation;    Protein phosphorylation;    Protein kinase C;    Lysozyme;    Membrane-protein interaction;   

DOI  :  10.1016/0014-5793(88)80215-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A hydrophilic enzyme, lysozyme, was myristoylated in vitro by the N-hydroxysuccinimide ester of myristic acid, and the monomyristoylated lysozyme was isolated by CM-cellulose cation-exchange column chromatography. The monomyristoylated lysozyme associated with phospholipid vesicles, whereas the association of native lysozyme was negligible. The membrane-associated monomyristoylated lysozyme was phosphorylated with partially purified rat brain Ca²⁺- and phospholipid-dependent protein kinase (protein kinase C) in the presence of Ca²⁺, phosphatidylserine and phorbolmyristate acetate. Thus, the myristoylated lysozyme became a substrate of protein kinase C through its hydrophobic association with the membrane. The present results suggest that the myristoylation of cytoplasmic proteins may have an important role in signal transduction.

【 授权许可】

Unknown