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The ability of purified Rous sarcoma virus transforming gene product, pp60v-src, to phosphorylate phosphatidylinositol and diacylglycerol was investigated. Phosphatidylinositol was phosphorylated to form both mono- and diphosphorylated derivatives. 1,2-Diacylglycerol was phosphorylated to form phosphatidic acid. These activities showed the same thermolability and the same sensitivity to inhibitors as shown by the casein kinase activity of pp60v-src. In addition, when serum-starved chicken embryo fibroblasts transformed by a virus mutant temperature-sensitive for transformation were shifted from the nonpermissive to permissive temperature, an increase of 50-100% in the labeling of phosphatidylinositol 4-phosphate, phosphatidylinositol 4,5-bisphosphate, and phosphatidic acid was observed, as compared to uninfected cells.
Sugimoto et al. (Sun,) studied this question.
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