Abstract
Phospholipase C-γ1 (PLC-γ1), 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-γ1 and phosphatidylinositol 4,5-bisphosphate hydrolysis in various cell lines. The ability of tyrosine phosphorylation to activate the catalytic activity of PLC-γ1 was tested. Tyrosine phosphorylation in intact cells or in vitro increased the catalytic activity of PLC-γ1. Also, treatment of EGF-activated PLC-γ1 with a tyrosine-specific phosphatase substantially decreased the catalytic activity of PLC-γ1. 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-γ1 through tyrosine phosphorylation.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 6:10 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 11, 2024, 9:41 a.m.) |
Indexed | 4 months, 2 weeks ago (April 5, 2025, 5:07 a.m.) |
Issued | 34 years, 8 months ago (Nov. 30, 1990) |
Published | 34 years, 8 months ago (Nov. 30, 1990) |
Published Print | 34 years, 8 months ago (Nov. 30, 1990) |
@article{Nishibe_1990, title={Increase of the Catalytic Activity of Phospholipase C-γ1 by Tyrosine Phosphorylation}, volume={250}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1700866}, DOI={10.1126/science.1700866}, number={4985}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Nishibe, Shunzo and Wahl, Matthew I. and Hernandez-Sotomayor, S. M. and Tonks, Nicholas K. and Rhee, Sue Goo and Carpenter, Graham}, year={1990}, month=nov, pages={1253–1256} }