Association of a myristoylated protein with a biological membrane and its increased phosphorylation by protein kinase C.
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.
Utsumi
T
T
Laboratory of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Japan.
Yoshinaga
K
K
Koga
D
D
Ide
A
A
Nobori
K
K
Okimasu
E
E
Terada
S
S
Utsumi
K
K
D000818:Animals; D001921:Brain / Q000201:enzymology*; D007700:Kinetics; D008074:Lipoproteins / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D009113:Muramidase / Q000378:metabolism*; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats
D008074:Lipoproteins; D008565:Membrane Proteins; D009227:Myristic Acids; D019814:Myristic Acid; D011493:Protein Kinase C; D009113:Muramidase