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

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PHOSPHOLIPASE-C-GAMMA IS A SUBSTRATE FOR THE PDGF AND EGF RECEPTOR PROTEIN-TYROSINE KINASES INVIVO AND INVITRO

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Title
PHOSPHOLIPASE-C-GAMMA IS A SUBSTRATE FOR THE PDGF AND EGF RECEPTOR PROTEIN-TYROSINE KINASES INVIVO AND INVITRO
Author
Meisenhelder, JillSuh, Pann-GhillRhee, Sue GooHunter, Tony
Issue Date
1989-06
Publisher
CELL PRESS
Citation
CELL, v.57, no.7, pp.1109 - 1122
Abstract
Phospholipase C-γ (PLC-γ) was rapidly phosphorylated on tyrosines and serines following PDGF and EGF treatment of quiescent 3T3 mouse fibroblasts and A431 human epidermoid cells, respectively. PDGF treatment increased PLC-γ phosphorylation within 30 sec. This lasted for up to 1 hr, and occurred at high stoichiometry. Continuous receptor occupancy was required to maintain this phosphorylation. Three major sites of tyrosine phosphorylation were detected in PLC-γ, two of which were phosphorylated in EGF-treated A431 cells. Under certain conditions PDGF receptor coimmunoprecipitated with PLC-γ, suggesting that PDGF receptor can phosphorylate PLC-γ directly. Indeed, purified PDGF or EGF receptor phosphorylated purified PLC-γ on tyrosines identical to those phosphorylated in vivo. Tyrosine phosphorylation of PLC-γ was not induced by bombesin, TPA, or insulin. Stimulation of PLC-γ tyrosine phosphorylation and the reported ability of PDGF and EGF to induce phosphatidylinositol turnover in different cells were strongly correlated. We propose that tyrosine phosphorylation of PLC-γ by PDGF and EGF receptors leads to its activation, and a consequent increase in phosphatidylinositol turnover. © 1989.
URI
https://scholarworks.unist.ac.kr/handle/201301/16504
URL
http://www.sciencedirect.com/science/article/pii/0092867489900482
DOI
10.1016/0092-8674(89)90048-2
ISSN
0092-8674
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