dc.citation.endPage |
1122 |
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dc.citation.number |
7 |
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dc.citation.startPage |
1109 |
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dc.citation.title |
CELL |
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dc.citation.volume |
57 |
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dc.contributor.author |
Meisenhelder, Jill |
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dc.contributor.author |
Suh, Pann-Ghill |
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dc.contributor.author |
Rhee, Sue Goo |
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dc.contributor.author |
Hunter, Tony |
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dc.date.accessioned |
2023-12-22T13:10:00Z |
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dc.date.available |
2023-12-22T13:10:00Z |
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dc.date.created |
2015-08-19 |
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dc.date.issued |
1989-06 |
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dc.description.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. |
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dc.identifier.bibliographicCitation |
CELL, v.57, no.7, pp.1109 - 1122 |
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dc.identifier.doi |
10.1016/0092-8674(89)90048-2 |
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dc.identifier.issn |
0092-8674 |
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dc.identifier.scopusid |
2-s2.0-0024380391 |
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dc.identifier.uri |
https://scholarworks.unist.ac.kr/handle/201301/16504 |
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dc.identifier.url |
http://www.sciencedirect.com/science/article/pii/0092867489900482 |
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dc.identifier.wosid |
A1989AE60100007 |
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dc.language |
영어 |
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dc.publisher |
CELL PRESS |
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dc.title |
PHOSPHOLIPASE-C-GAMMA IS A SUBSTRATE FOR THE PDGF AND EGF RECEPTOR PROTEIN-TYROSINE KINASES INVIVO AND INVITRO |
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dc.type |
Article |
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dc.description.journalRegisteredClass |
scopus |
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