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• W1771590610 endingPage "7781" @default.
• W1771590610 startingPage "7773" @default.
• W1771590610 abstract "Phosphorylated tyrosine residues in receptor tyrosine kinases serve as binding sites for signal transduction molecules. We have identified two autophosphorylation sites, Tyr-988 and Tyr-1018, in the platelet-derived growth factor (PDGF) α-receptor carboxyl-terminal tail, which are involved in binding of phospholipase C-γ (PLC-γ). The capacities of the Y988F and Y1018F mutant PDGF α-receptors, expressed in porcine aortic endothelial cells, to bind PLC-γ are 60 and 5% of that of the wild-type receptor, respectively. Phosphorylated but not unphosphorylated peptides containing Tyr-1018 are able to compete with the intact receptor for binding to immobilized PLC-γ SH2 domains; a phosphorylated Tyr-988 peptide competes 10 times less efficiently. The complex between PLC-γ and the PDGF α-receptor is more stable than that of PLC-γ and the PDGF β-receptor. However, PDGF stimulation results in a smaller fraction of tyrosine-phosphorylated PLC-γ and a smaller accumulation of inositol trisphosphate in cells expressing the α-receptor as compared with cells expressing the β-receptor. We conclude that phosphorylated Tyr-988 and Tyr-1018 in the PDGF α-receptor carboxyl-terminal tail bind PLC-γ, but this association leads to only a relatively low level of tyrosine phosphorylation and activation of PLC-γ. Phosphorylated tyrosine residues in receptor tyrosine kinases serve as binding sites for signal transduction molecules. We have identified two autophosphorylation sites, Tyr-988 and Tyr-1018, in the platelet-derived growth factor (PDGF) α-receptor carboxyl-terminal tail, which are involved in binding of phospholipase C-γ (PLC-γ). The capacities of the Y988F and Y1018F mutant PDGF α-receptors, expressed in porcine aortic endothelial cells, to bind PLC-γ are 60 and 5% of that of the wild-type receptor, respectively. Phosphorylated but not unphosphorylated peptides containing Tyr-1018 are able to compete with the intact receptor for binding to immobilized PLC-γ SH2 domains; a phosphorylated Tyr-988 peptide competes 10 times less efficiently. The complex between PLC-γ and the PDGF α-receptor is more stable than that of PLC-γ and the PDGF β-receptor. However, PDGF stimulation results in a smaller fraction of tyrosine-phosphorylated PLC-γ and a smaller accumulation of inositol trisphosphate in cells expressing the α-receptor as compared with cells expressing the β-receptor. We conclude that phosphorylated Tyr-988 and Tyr-1018 in the PDGF α-receptor carboxyl-terminal tail bind PLC-γ, but this association leads to only a relatively low level of tyrosine phosphorylation and activation of PLC-γ." @default.
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• W1771590610 date "1995-03-01" @default.
• W1771590610 modified "2023-10-17" @default.
• W1771590610 title "Demonstration of Functionally Different Interactions between Phospholipase C-γ and the Two Types of Platelet-derived Growth Factor Receptors" @default.
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• W1771590610 doi "https://doi.org/10.1074/jbc.270.13.7773" @default.
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