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Epidermal growth factor and platelet‐derived growth factor promote translocation of phospholipase C‐γ from cytosol to membrane
Author(s) -
Kim Uh-Hyun,
Kim Hee-Sook,
Rhee Sue Goo
Publication year - 1990
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 - 10.1016/0014-5793(90)81228-g
Subject(s) - tyrosine phosphorylation , microbiology and biotechnology , epidermal growth factor , cytosol , phosphorylation , platelet derived growth factor receptor , phospholipase c , tyrosine kinase , growth factor receptor , receptor tyrosine kinase , biochemistry , biology , growth factor , chemistry , signal transduction , receptor , enzyme
Treatment of HER 14 cells with epidermal growth factor (EGF) or platelet‐derived growth factor (PDGF) induced a translocation of phospholipase C‐γ (PLC‐γ) from cytosol to membrane. In such growth factor‐treated cells, cytosolic PLC‐γ was found to contain more phosphotyrosine than membrane‐associated enzyme. Because these growth factors have been shown to promote both the physical association of PLC‐γ with their receptors and the subsequent phosphorylation of the enzyme directly by the membrane‐bound receptor tyrosine kinases, the membrane assocation of PLC‐γ may simply be due to the formation of transient enzyme (receptor)‐substrate (PLC‐γ) complexes. If this is the case, membrane‐associated PLC‐γ would be expected to be released from membrane after undergoing tyrosine phosphorylation. However, tyrosine phosphorylation of membrane‐associated PLC‐γ by the EGF receptor in vitro did not result in the release of PLC‐γ from membrane. Thus, the association of PLC‐γ with membrane would appear to involve more than enzyme‐substrate complex.