Translocation of phospholipase C-gamma 2 induced by in vitro activation of protein tyrosine kinase activity in mast cell lysates.
Aggregation of the high-affinity receptor for IgE (Fc eta RI) on the surface of intact or permeabilized rodent mast cells results in tyrosine phosphorylation of phospholipase C-gamma 1 (PLC gamma 1) and PLC gamma 2, and translocation of both isozymes to the particulate fraction. We report here that activation of resident tyrosine kinases by the addition of adenosine triphosphate (ATP), orthovanadate, and Mg2+ to rat basophilic leukemia cell (RBL) lysates induces an association of PLC gamma 2 with the Triton-insoluble particulate fraction, with a parallel increase in tyrosine phosphorylation of cellular proteins. Both PLC gamma 2 translocation and tyrosine phosphorylation are supported by millimolar Mg2+ or Mn2+ but not by Ca2+. Both tyrosine phosphorylation and PLC gamma 2 translocation are inhibited by genistein. These data suggest that in vitro activation of tyrosine kinase activity in broken cell preparations induces the formation of association between PLC gamma 2 and ligands with the Triton-insoluble fraction.[1]References
- Translocation of phospholipase C-gamma 2 induced by in vitro activation of protein tyrosine kinase activity in mast cell lysates. Atkinson, T.P., Yang, Q. Cell. Signal. (1996) [Pubmed]
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