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Association of a myristoylated protein with a biological membrane and its increased phosphorylation by protein kinase C
Author(s) -
Utsumi Toshihiko,
Yoshinaga Koji,
Koga Daizo,
Ide Akio,
Nobori Koichi,
Okimasu Eiji,
Terada Shigeo,
Utsumi Kozo
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80215-1
Subject(s) - lysozyme , myristoylation , biochemistry , protein kinase a , protein kinase c , myristic acid , chemistry , phospholipid , muramidase , vesicle , enzyme , phosphorylation , biology , membrane , palmitic acid , fatty acid
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 Ca 2+ ‐ and phospholipid‐dependent protein kinase (protein kinase C) in the presence of Ca 2+ , 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.