Analysis of the autophosphorylation activity of transformation defective mutants of avian erythroblastosis virus.
The v-erb B protein of avian erythroblastosis virus (AEV) possesses an associated protein kinase activity in vitro. Analysis of temperature-sensitive mutants, and nonconditional host range mutants of AEV demonstrated that there was no simple correlation between this autophosphorylation activity and the transformation ability of the various AEV mutants. These data suggest that although this kinase activity may be central to transformation by AEV it is in itself insufficient.
D001355:Alpharetrovirus / Q000235:genetics*; D000818:Animals; D001354:Avian Leukosis Virus / Q000235:genetics*; D002462:Cell Membrane / Q000378:metabolism; D002472:Cell Transformation, Viral; D002478:Cells, Cultured; D004721:Endoplasmic Reticulum / Q000378:metabolism; D066246:ErbB Receptors; D009154:Mutation; D009856:Oncogene Proteins, Viral / Q000378:metabolism*; D009857:Oncogenes; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000378:metabolism; D013696:Temperature
D009856:Oncogene Proteins, Viral; D011956:Receptors, Cell Surface; D066246:ErbB Receptors; D011505:Protein-Tyrosine Kinases