Gould K L, Woodgett J R, Cooper J A, Buss J E, Shalloway D, Hunter T
Cell. 1985 Oct;42(3):849-57. doi: 10.1016/0092-8674(85)90281-8.
The transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homolog (pp60c-src) are demonstrated to be phosphorylated at serine 12 in vivo under certain conditions. We propose that protein kinase C is responsible for this modification based on the following evidence. First, the tumor promoters, 12-O-tetradecanoylphorbol-13-acetate and teleocidin, and synthetic diacylglycerol, known activators of protein kinase C in vivo, cause nearly complete phosphorylation of pp60src at serine 12. Second, among five purified serine/threonine-specific protein kinases tested, only protein kinase C phosphorylates pp60c-src and pp60v-src in vitro at serine 12. Third, purified protein kinase C phosphorylates a synthetic peptide corresponding to the N-terminal 20 amino acids of pp60c-src at serine 12. The physiological significance of this novel phosphorylation is discussed.
劳氏肉瘤病毒的转化蛋白（pp60v-src）及其正常细胞同源物（pp60c-src）在某些条件下于体内丝氨酸12位点被磷酸化。基于以下证据，我们提出蛋白激酶C负责这种修饰。首先，肿瘤启动子12-O-十四烷酰佛波醇-13-乙酸酯和teleocidin以及合成二酰基甘油（体内已知的蛋白激酶C激活剂）可使pp60src在丝氨酸12位点几乎完全磷酸化。其次，在所测试的五种纯化的丝氨酸/苏氨酸特异性蛋白激酶中，只有蛋白激酶C能在体外使pp60c-src和pp60v-src在丝氨酸12位点磷酸化。第三，纯化的蛋白激酶C可使对应于pp60c-src N端20个氨基酸的合成肽在丝氨酸12位点磷酸化。本文讨论了这种新型磷酸化的生理意义。
