Gould K L, Hunter T
Molecular Biology and Virology Laboratory, Salk Institute, San Diego, California 92138.
Mol Cell Biol. 1988 Aug;8(8):3345-56. doi: 10.1128/mcb.8.8.3345-3356.1988.
We have shown previously that pp60c-src is a substrate for protein kinase C in vivo and that the target of protein kinase C phosphorylation in mammalian pp60c-src is serine 12. We now demonstrate that in addition to tumor promoters, all activators of phosphatidylinositol turnover that we have tested in fibroblasts (platelet-derived growth factor, fibroblast growth factor, serum, vasopressin, sodium orthovanadate, and prostaglandin F2 alpha) lead to the phosphorylation of pp60c-src at serine 12. In addition to stimulating serine 12 phosphorylation in pp60c-src, platelet-derived growth factor treatment of quiescent fibroblasts induces phosphorylation of one or two additional serine residues and one tyrosine residue within the N-terminal 16 kilodaltons of the enzyme and activates its immune complex protein-tyrosine kinase activity.
我们先前已经表明，pp60c-src在体内是蛋白激酶C的底物，并且在哺乳动物pp60c-src中蛋白激酶C磷酸化的靶点是丝氨酸12。我们现在证明，除了肿瘤启动子外，我们在成纤维细胞中测试的所有磷脂酰肌醇代谢激活剂（血小板衍生生长因子、成纤维细胞生长因子、血清、血管加压素、原钒酸钠和前列腺素F2α）都会导致pp60c-src在丝氨酸12处磷酸化。除了刺激pp60c-src中丝氨酸12的磷酸化外，用血小板衍生生长因子处理静止的成纤维细胞会诱导该酶N端16千道尔顿内另外一个或两个丝氨酸残基和一个酪氨酸残基的磷酸化，并激活其免疫复合物蛋白酪氨酸激酶活性。
