Increase of the Catalytic Activity of Phospholipase C-γ1 by Tyrosine Phosphorylation
| Autor: | Graham Carpenter, Matthew I. Wahl, Shunzo Nishibe, Sue Goo Rhee, Nicholas K. Tonks, S. M. Hernandez-Sotomayor |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Phosphatidylinositol 4
5-Diphosphate Inositol 1 4 5-Trisphosphate Protein tyrosine phosphatase Phosphatidylinositols SH2 domain Catalysis Receptor tyrosine kinase Diglycerides chemistry.chemical_compound Phosphoinositide phospholipase C Phosphorylation Phosphotyrosine Immunosorbent Techniques Multidisciplinary Epidermal Growth Factor biology Phosphoric Diester Hydrolases Phosphatidylinositol Diacylglycerol-Lyase Tyrosine phosphorylation Protein-Tyrosine Kinases Cell biology Enzyme Activation ErbB Receptors Isoenzymes Kinetics chemistry Biochemistry biology.protein Tyrosine Tyrosine kinase Platelet-derived growth factor receptor Signal Transduction |
| Zdroj: | Science. 250:1253-1256 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.1700866 |
| Popis: | Phospholipase C-gamma 1 (PLC-gamma 1), an isozyme of the phosphoinositide-specific phospholipase C family, which occupies a central role in hormonal signal transduction pathways, is an excellent substrate for the epidermal growth factor (EGF) receptor tyrosine kinase. Epidermal growth factor elicits tyrosine phosphorylation of PLC-gamma 1 and phosphatidylinositol 4,5-bisphosphate hydrolysis in various cell lines. The ability of tyrosine phosphorylation to activate the catalytic activity of PLC-gamma 1 was tested. Tyrosine phosphorylation in intact cells or in vitro increased the catalytic activity of PLC-gamma 1. Also, treatment of EGF-activated PLC-gamma 1 with a tyrosine-specific phosphatase substantially decreased the catalytic activity of PLC-gamma 1. These results suggest that the EGF-stimulated formation of inositol 1,4,5-trisphosphate and diacylglycerol in intact cells results, at least in part, from catalytic activation of PLC-gamma 1 through tyrosine phosphorylation. |
| Databáze: | OpenAIRE |
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