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• W2017100096 startingPage "1253" @default.
• W2017100096 abstract "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." @default.
• W2017100096 created "2016-06-24" @default.
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• W2017100096 date "1990-11-30" @default.
• W2017100096 modified "2023-10-18" @default.
• W2017100096 title "Increase of the Catalytic Activity of Phospholipase C-γ1 by Tyrosine Phosphorylation" @default.
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• W2017100096 doi "https://doi.org/10.1126/science.1700866" @default.
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