Correlation between phosphorylation of a 34,000-molecular-weight protein, pp60src-associated kinase activity, and tumorigenicity in transformed and revertant vole cells.
The phosphorylation of a 34,000-molecular-weight (34K) cell protein, purported to be a substrate of the avian retrovirus pp60src-associated protein kinase activity, was compared in three types of Rous sarcoma virus-infected vole cells: fully transformed cells, partial revertants which are morphologically normal in appearance but retain their tumorigenic potential, and full revertants which are similar to normal vole cells in all parameters including a lack of tumorigenicity. Although similar amounts of 34K protein are present in all three cell types, phosphorylation of the 34K protein was significantly reduced in the full revertant cell type. The reduced phosphorylation occurred at the tyrosine residue.
D000818:Animals; D003411:Arvicolinae; D001358:Avian Sarcoma Viruses; D002471:Cell Transformation, Neoplastic; D002472:Cell Transformation, Viral; D008970:Molecular Weight; D015688:Oncogene Protein pp60(v-src); D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D011506:Proteins; D014764:Viral Proteins; D011494:Protein Kinases; D015688:Oncogene Protein pp60(v-src)