Association of a myristoylated protein with a biological membrane and its increased phosphorylation by protein kinase C.
FEBS Lett
; 238(1): 13-6, 1988 Sep 26.
Article
em En
| MEDLINE
| ID: mdl-3169245
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.
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Base de dados:
MEDLINE
Assunto principal:
Encéfalo
/
Proteína Quinase C
/
Muramidase
/
Lipoproteínas
/
Proteínas de Membrana
/
Ácidos Mirísticos
Tipo de estudo:
Risk_factors_studies
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1988
Tipo de documento:
Article
País de afiliação:
Japão