title: Substitution of Ser-17 of pp60c-src: biological and biochemical characterization in chicken embryo fibroblasts.
abstract: 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.
authors: Institute for Chemical Research, Kyoto University, Japan.
authors: Y
authors: Y
authors: Hirota
authors: J
authors: J
authors: Kato
authors: T
authors: T
authors: Takeya
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D002642:Chick Embryo; D005347:Fibroblasts / Q000166:cytology / Q000201:enzymology; D005796:Genes; D014644:Genetic Variation; D009154:Mutation; D011494:Protein Kinases / Q000235:genetics*; D011518:Proto-Oncogene Proteins / Q000235:genetics* / Q000378:metabolism; D016392:Proto-Oncogene Proteins pp60(c-src); D011519:Proto-Oncogenes; D012694:Serine
chemical_list: D011518:Proto-Oncogene Proteins; D012694:Serine; D011494:Protein Kinases; D016392:Proto-Oncogene Proteins pp60(c-src)