Protein phosphorylation at tyrosine is induced by the v-erbB gene product in vivo and in vitro
| Autor: | Jeffrey E. Declue, Thomas D. Gilmore, G. Steven Martin |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
animal structures
Genes Viral Receptors Cell Surface Chick Embryo Protein tyrosine phosphatase Biology SH2 domain Alpharetrovirus General Biochemistry Genetics and Molecular Biology Receptor tyrosine kinase Viral Proteins chemistry.chemical_compound Animals Protein phosphorylation Phosphorylation Tyrosine Avian Leukosis Virus Cell Membrane Tyrosine phosphorylation Fibroblasts Protein-Tyrosine Kinases Cell Transformation Viral Phosphoproteins Molecular biology IRS2 ErbB Receptors chemistry Mutation embryonic structures biology.protein Protein Kinases |
| Zdroj: | Cell. 40:609-618 |
| ISSN: | 0092-8674 |
| Popis: | The v-erbB gene product of avian erythroblastosis virus (AEV) has extensive homology with the receptor for epidermal growth factor (EGF). We report here that chicken embryo fibroblasts (CEF) transformed by AEV show enhanced tyrosine phosphorylation of a number of cellular polypeptides, including the 36 kd protein, which is phosphorylated in avian sarcoma virus-transformed fibroblasts, and the 42 kd protein, which is phosphorylated in mitogen-stimulated cells. CEF infected by AEV mutants with deletions in v-erbA showed enhanced tyrosine phosphorylation, whereas CEF infected by mutants with deletions in v-erbB did not. When membranes from AEV-transformed cells were incubated with γ- 32 P-ATP, both the v-erbB gene product and the 36 kd cellular protein became phosphorylated at tyrosine. These results indicate that the v-erbB protein induces tyrosine phosphorylation in vivo and in vitro, and suggest that, like the EGF receptor, it possesses tyrosine-specific protein kinase activity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|