IL-2 binding activates a tyrosine-phosphorylated phosphatidylinositol-3-kinase.

IL-2 was shown to induce phosphatidylinositol-3-kinase activity in the CTLL-2 murine lymphocyte line. Tyrosine phosphorylation of phosphatidylinositol-3-kinase was demonstrated by immunoabsorption with antiphosphotyrosine antibody and was coincident with activation of an IL-2R-associated tyrosine kinase. Half-maximal activation of this enzyme, and of cell proliferation, occurred at 30 pM IL-2. Incubation of cells with genistein, a selective tyrosine kinase inhibitor, blocked IL-2-dependent activation of receptor-associated tyrosine kinase and phosphatidylinositol-3-kinase activities, suggesting that tyrosine phosphorylation-dependent activation of phosphatidylinositol-3-kinase is a component of the IL-2R signal transduction process.