Structural features of the carboxy terminus of p60c-src that are required for the regulation of its intrinsic kinase activity.
The major structural difference between p60c-src and p60v-src resides in the carboxy-terminal region. We introduced substitution, replacement and deletion into the carboxy-terminal region of chicken p60c-src and examined the effects on its biochemical and biological properties in chicken embryo fibroblasts. The replacement of the carboxy-terminal region after amino acid position 515 of p60c-src with the corresponding region of p60v-src converted p60c-src to a transforming protein with elevated kinase activity. The substitution of Tyr527, which is a major tyrosine phosphorylation site of p60c-src, with phenylalanine resulted in an increase of kinase activity and in transforming ability. On the other hand, a deletion after position 515 abolished the kinase activity. These results revealed the structural features of the carboxy terminus of p60c-src that are required for the regulation of its intrinsic protein kinase activity.
D000818:Animals; D002642:Chick Embryo; D005347:Fibroblasts / Q000378:metabolism; D015688:Oncogene Protein pp60(v-src); D010766:Phosphorylation; D010957:Plasmids; D011494:Protein Kinases; D012191:Retroviridae Proteins; D014162:Transfection
D012191:Retroviridae Proteins; D011494:Protein Kinases; D015688:Oncogene Protein pp60(v-src)