Dual modulation of the phosphorylation of endogenous yeast proteins by arachidonic acid and phosphatidylinositol.
Phosphorylation of endogenous yeast substrates in DE-52 fractions were analysed by SDS-polyacrylamide gel electrophoresis and autoradiography. In fractions 29 and 45, phosphatidylinositol inhibited the phosphorylation of multiple peptides with a wide range of molecular mass whereas it enhanced the phosphorylation of peptides smaller than 14 kD. Similar dual modulation of the phosphorylation by arachidonic acid was observed in fraction 37 which also contained potent phosphatidylserine-activating protein kinase C.
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Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32114.
Walbey
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Davis
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McCall
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D016718:Arachidonic Acid / Q000494:pharmacology*; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008823:Micelles; D008970:Molecular Weight; D010712:Phosphatidic Acids / Q000494:pharmacology; D010716:Phosphatidylinositols / Q000494:pharmacology*; D010766:Phosphorylation / Q000187:drug effects; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000378:metabolism*
D005656:Fungal Proteins; D008823:Micelles; D010712:Phosphatidic Acids; D010716:Phosphatidylinositols; D016718:Arachidonic Acid; D011493:Protein Kinase C