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Science 30 November 1990: Vol. 250. no. 4985, pp. 1253 - 1256 DOI: 10.1126/science.1700866
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Articles
Science, Vol 250, Issue 4985, 1253-1256
Copyright © 1990 by American Association for the Advancement of Science
Increase of the catalytic activity of phospholipase C-gamma 1 by tyrosine phosphorylation
S Nishibe,
MI Wahl,
SM Hernandez-Sotomayor,
NK Tonks,
SG Rhee,
and
G Carpenter
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146.
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.
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