Plasma membrane phosphoproteins in normal and Rous sarcoma virus transformed chick embryo fibroblasts: characterization by in vitro phosphorylation.
Plasma membranes isolated from normal and RSV transformed chick embryo fibroblasts were phosphorylated in vitro using endogenous protein kinase and ATP (gamma32P) and the labeled phosphoproteins were analyzed by SDS-PAGE. A number of protein phosphorylation changes were observed following transformation, however in most cases they were relatively small quantitative differences. The four major changes were in proteins of 47,000, 58,000, 75,000 and 135,000 daltons. Decreased phosphorylation of the 47,000 dalton polypeptide was found in transformed cell membranes but this alteration was shown to be due to differences in cell growth rather than transformation. Increase phosphorylation of the 75,000 dalton protein was at least partially related to virus infection. However, increased phosphorylation of the 58,000 and 135,000 dalton polypeptides were entirely transformation specific.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D001345:Autoradiography; D001358:Avian Sarcoma Viruses; D002455:Cell Division / Q000187:drug effects; D002472:Cell Transformation, Viral; D002642:Chick Embryo; D006152:Cyclic GMP / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts / Q000502:physiology; D008565:Membrane Proteins / Q000032:analysis / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation
D008565:Membrane Proteins; D010750:Phosphoproteins; D000255:Adenosine Triphosphate; D006152:Cyclic GMP