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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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

Cited 28 times inthomson ciCited 32 times inthomson ci
Title
Localization of phospholipase C-gamma 1 signaling in caveolae: importance in EGF-induced phosphoinositide hydrolysis but not in tyrosine phosphorylation
Author
Jang, Il-HoKim, Jae HoLee, Byoung DaeBae, Sun SikPark, Myung HwanSuh, Pann-GhillRyu, Sung Ho
Issue Date
2001-02
Publisher
ELSEVIER SCIENCE BV
Citation
FEBS LETTERS, v.491, no.1-2, pp.4 - 8
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
URI
https://scholarworks.unist.ac.kr/handle/201301/16476
URL
http://www.sciencedirect.com/science/article/pii/S0014579301021652
DOI
10.1016/S0014-5793(01)02165-2
ISSN
0014-5793
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BIO_Journal Papers
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