Evidence that the insulin receptor-associated protein kinase acts as a phosphatidylinositol kinase.
Insulin receptor preparations from human placenta at various states of purity were shown to catalyze insulin-stimulated phosphate incorporation from [gamma-32P]ATP into endogenous (membrane) and exogenous phosphatidylinositol. Our data suggest that the insulin receptor associated protein (tyrosine) kinase can act as a phosphatidylinositol kinase, and that this mechanism may be of physiological importance in signal transduction of insulin.
D019870:1-Phosphatidylinositol 4-Kinase; D005260:Female; D006801:Humans; D007328:Insulin / Q000494:pharmacology; D007700:Kinetics; D010716:Phosphatidylinositols / Q000302:isolation & purification; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011494:Protein Kinases / Q000378:metabolism*; D011972:Receptor, Insulin / Q000302:isolation & purification
D007328:Insulin; D010716:Phosphatidylinositols; D010770:Phosphotransferases; D011494:Protein Kinases; D019870:1-Phosphatidylinositol 4-Kinase; D011972:Receptor, Insulin