Tyrosine Phosphorylation of a 94-kDa Protein Associated with GRB2/ASH Is Implicated in the Signal Transduction of Hematopoietic Survival Factors
| Autor: | Hisamaru Hirai, Hideharu Odai, Yutaka Hanazono, Ko Sasaki, Yoshio Yazaki |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
inorganic chemicals
Cell Survival Recombinant Fusion Proteins Biophysics Protein tyrosine phosphatase SH2 domain Biochemistry Receptor tyrosine kinase Cell Line src Homology Domains chemistry.chemical_compound Tumor Cells Cultured medicine Animals Humans Staurosporine Phosphorylation Phosphotyrosine Molecular Biology Adaptor Proteins Signal Transducing GRB2 Adaptor Protein biology Kinase Granulocyte-Macrophage Colony-Stimulating Factor Proteins Tyrosine phosphorylation Cell Biology Hematopoietic Stem Cells Molecular biology Organophosphates ErbB Receptors Molecular Weight Kinetics chemistry biology.protein Rabbits GRB2 biological phenomena cell phenomena and immunity Signal transduction Cell Division Signal Transduction medicine.drug |
| Zdroj: | Biochemical and Biophysical Research Communications. 222:330-337 |
| ISSN: | 0006-291X |
| Popis: | Grb2/Ash is an adapter molecule that contains Src-homology (SH) 2 and 3 domains. We have examined Grb2/Ash-associated proteins in hematopoietic cells, and have noted a 94-kDa phosphotyrosine-containing protein (pp94) among them. It was shown that the SH2 domain of Grb2/Ash is necessary for the binding of pp94 to Grb2/Ash from the binding experiments using the GST fusion proteins and the phosphotyrosine analogue phenylphosphate. Tyrosine phosphorylation of pp94 was rapid and transient, and was only observed when the cells were stimulated with factors that were absolutely required for survival of the cells (survival factors). The kinase inhibitors, staurosporine and genistein, inhibit the proliferation of UT-7 cells. However, genistein does not inhibit the survival of the cells while staurosporine inhibits both the proliferation and the survival of the cells. Tyrosine phosphorylation of pp94 was sensitive to staurosporine but resistant to genistein. It is possible that tyrosine phosphorylation of pp94 might be related to the survival rather than to the proliferation of the cells. |
| Databáze: | OpenAIRE |
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