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Localization of phospholipase C-gamma 1 signaling in caveolae: importance in EGF-induced phosphoinositide hydrolysis but not in tyrosine phosphorylation

Title
Localization of phospholipase C-gamma 1 signaling in caveolae: importance in EGF-induced phosphoinositide hydrolysis but not in tyrosine phosphorylation
Authors
Jang, IHKim, JHLee, BDBae, SSPark, MHSuh, PGRyu, SH
POSTECH Authors
Ryu, SH
Date Issued
Jan-2001
Publisher
ELSEVIER SCIENCE BV
Abstract
Upon epidermal growth factor treatment, phospholipase C-gamma1 (PLC-gamma1) translocates from cytosol to membrane where it is phosphorylated at tyrosine residues. Caveolae are small plasma membrane invaginations whose structural protein is caveolin. In this study, we show that the translocation of PLC-gamma1 and its tyrosine phosphorylation are localized in caveolae by caveolin-enriched low-density membrane (CM) preparation and immunostaining of cells, Pretreatment of cells with methyl-beta -cyclodextrin (M beta CD), a chemical disrupting caveolae structure, inhibits the translocation of PLC-gamma1 to CM as well as phosphatidylinositol (PtdIns) turnover. However, M beta CD shows no effect on tyrosine phosphorylation level of PLC-gamma1. Our findings suggest that, for proper signaling, PLC-gamma1 phosphorylation has to occur at PtdInsP(2)-enriched sites. (C) 2001 Federation of European Biochemical Societies, Published by Elsevier Science B.V. All rights reserved.
Keywords
phospholipase C-gamma 1; caveola; tyrosine phosphorylation; EPIDERMAL GROWTH-FACTOR; MEMBRANE DOMAINS; C-GAMMA; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; CHOLESTEROL DEPLETION; CELLS; PROTEIN; KINASE; PDGF; RESIDUES
URI
http://oasis.postech.ac.kr/handle/2014.oak/19653
ISSN
0014-5793
Article Type
Article
Citation
FEBS LETTERS, vol. 491, no. 1-2, page. 4 - 8, 2001-01
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 RYU, SUNG HO
Dept of Life Sciences
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