Hirota Y, Kato J, Takeya T
Institute for Chemical Research, Kyoto University, Japan.
Mol Cell Biol. 1988 Apr;8(4):1826-30. doi: 10.1128/mcb.8.4.1826-1830.1988.
pp60c-src is phosphorylated mainly on Ser-17 and Tyr-527 in vivo. In this study, we examined the effect of the phosphorylation of Ser-17 on the properties of pp60c-src by introducing Rous sarcoma virus variants carrying pp60c-src in which Ser-17 had been substituted, into chicken embryo fibroblasts. The Ala-17 substitution in wild-type pp60c-src and pp60c-src carrying Phe-527 caused a two- to threefold elevation in the kinase activity in vitro of these proteins; the former variant resulted in no morphological changes of infected cells, whereas the latter variant transformed chicken embryo fibroblasts. Since the substitution of Tyr-527 per se has been reported to activate pp60c-src, these results suggest that the abolishment of the phosphorylation of Ser-17 does not affect noticeably the properties of pp60c-src in chicken embryo fibroblasts.
pp60c-src在体内主要在丝氨酸-17和酪氨酸-527位点发生磷酸化。在本研究中,我们通过将携带丝氨酸-17已被替换的pp60c-src的劳氏肉瘤病毒变体引入鸡胚成纤维细胞,来检测丝氨酸-17磷酸化对pp60c-src特性的影响。野生型pp60c-src和携带苯丙氨酸-527的pp60c-src中的丙氨酸-17替换导致这些蛋白质的体外激酶活性提高了两到三倍;前一种变体未导致感染细胞的形态变化,而后一种变体则使鸡胚成纤维细胞发生转化。由于据报道酪氨酸-527的替换本身可激活pp60c-src,这些结果表明丝氨酸-17磷酸化的消除对鸡胚成纤维细胞中pp60c-src的特性没有明显影响。