Phosphorylation of endogenous substrates of yeast protein kinase C regulated by lipid-triton micelles.
In the DE-52 fraction 19 of the crude cytosolic extract of Saccharomyces cerevisiae, the 31-kDa endogenous substrate(s) of protein kinase C were detected by SDS-polyacrylamide gel electrophoresis and autoradiography. Phosphorylation of the substrate(s) depended on Ca2+, phosphatidylserine and diacylglycerol. It was also enhanced by phosphatidylinositol, phosphatidylethanolamine and phosphatidylglycerol (dioleoyl), but inhibited by arachidonic acid and sphingosine.
Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32114.
W N
WN
Kuo
D L
DL
Davis
M N
MN
Jean
L K
LK
McCall
D L
DL
Jones
J
J
Jn-Baptiste
D016718:Arachidonic Acid / Q000494:pharmacology; D008823:Micelles; D010743:Phospholipids / Q000494:pharmacology; D010766:Phosphorylation; D011493:Protein Kinase C / Q000032:analysis / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013110:Sphingosine / Q000494:pharmacology
D008823:Micelles; D010743:Phospholipids; D016718:Arachidonic Acid; D011493:Protein Kinase C; D013110:Sphingosine