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Localization of phospholipase C‐γ1 signaling in caveolae: importance in EGF‐induced phosphoinositide hydrolysis but not in tyrosine phosphorylation
Author(s) -
Jang Il-Ho,
Kim Jae Ho,
Lee Byoung Dae,
Bae Sun Sik,
Park Myung Hwan,
Suh Pann-Ghill,
Ryu Sung Ho
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02165-2
Subject(s) - caveolae , phosphorylation , tyrosine phosphorylation , phospholipase c , microbiology and biotechnology , cytosol , caveolin , tyrosine , signal transduction , epidermal growth factor , phosphatidylinositol , chemistry , biology , phosphoinositide phospholipase c , biochemistry , receptor , enzyme
Upon epidermal growth factor treatment, phospholipase C‐γ1 (PLC‐γ1) 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‐γ1 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‐β‐cyclodextrin (MβCD), a chemical disrupting caveolae structure, inhibits the translocation of PLC‐γ1 to CM as well as phosphatidylinositol (PtdIns) turnover. However, MβCD shows no effect on tyrosine phosphorylation level of PLC‐γ1. Our findings suggest that, for proper signaling, PLC‐γ1 phosphorylation has to occur at PtdInsP 2 ‐enriched sites.