Phospholipids stimulate phosphorylation of vinculin by the tyrosine-specific protein kinase of Rous sarcoma virus.
The phosphorylation of vinculin by a highly purified tyrosine-specific protein kinase was enhanced more than 10-fold by anionic phospholipids: the phosphorylation of casein, actin, and alpha-actinin was inhibited. The effect of phospholipid was dependent on the divalent cation used. Stimulation was observed by phosphatidylinositol or phosphatidylglycerol in the presence of either 0.5 mM Mn2+ of 5 mM Mg2+; with either phospholipid, more enzyme activity was observed with Mn2+. Maximal stimulation by phosphatidylinositol was observed at about 400 micrograms/ml. In contrast, marked stimulation by phosphatidylserine was observed only with Mn2+ and marked stimulation by phosphatidic acid was observed only with Mg2+. These results raise the possibility that phospholipids modulate vinculin phosphorylation in Rous sarcoma virus-transformed cells.
D001358:Avian Sarcoma Viruses / Q000201:enzymology; D002472:Cell Transformation, Viral; D004789:Enzyme Activation; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D009124:Muscle Proteins / Q000378:metabolism*; D010716:Phosphatidylinositols / Q000494:pharmacology; D010743:Phospholipids / Q000494:pharmacology*; D010766:Phosphorylation; D019000:Phosphotyrosine; D011494:Protein Kinases / Q000378:metabolism*; D013379:Substrate Specificity; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000378:metabolism; D016596:Vinculin
D009124:Muscle Proteins; D010716:Phosphatidylinositols; D010743:Phospholipids; D016596:Vinculin; D019000:Phosphotyrosine; D014443:Tyrosine; D008345:Manganese; D011494:Protein Kinases; D008274:Magnesium