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  • Title: In vitro tyrosine phosphorylation of PLC-gamma 1 and PLC-gamma 2 by src-family protein tyrosine kinases.
    Author: Liao F, Shin HS, Rhee SG.
    Journal: Biochem Biophys Res Commun; 1993 Mar 31; 191(3):1028-33. PubMed ID: 7682059.
    Abstract:
    The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. Comparison of the in vitro phosphorylation rates revealed no distinct specificity between PLC-gamma 1 and PLC-gamma 2, or between the five PTKs.
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