Glycoprotein tyrosine phosphorylation in Rous sarcoma virus-transformed chicken embryo fibroblasts.
The level of tyrosine phosphorylation of cellular glycoproteins isolated by wheat germ agglutinin chromatography in cells infected with a variety of kinase-positive/transformation-defective src mutants was examined in an effort to identify cellular membrane proteins whose phosphorylation correlates with phenotypic transformation. We have identified two glycoproteins, with molecular masses of 95 and 135 kilodaltons, whose phosphorylation correlates with morphological transformation, growth in soft agar, and an increase in the rate of 2-deoxyglucose uptake. The strong correlation obtained between transformation and phosphorylation of these proteins suggests that they may be substrates for pp60src which are important in the process of transformation.
Department of Microbiology and Cancer Center, University of Virginia School of Medicine, Charlottesville 22908.
L M
LM
Kozma
A B
AB
Reynolds
M J
MJ
Weber
D000818:Animals; D001358:Avian Sarcoma Viruses / Q000235:genetics*; D002471:Cell Transformation, Neoplastic; D002478:Cells, Cultured; D002642:Chick Embryo; D005347:Fibroblasts / Q000378:metabolism; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D009154:Mutation; D010766:Phosphorylation; D019000:Phosphotyrosine; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000032:analysis
D006023:Glycoproteins; D019000:Phosphotyrosine; D014443:Tyrosine