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, 12 (7), 3176-82

Fc Epsilon R1-mediated Tyrosine Phosphorylation of Multiple Proteins, Including Phospholipase C Gamma 1 and the Receptor Beta Gamma 2 Complex, in RBL-2H3 Rat Basophilic Leukemia Cells

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Fc Epsilon R1-mediated Tyrosine Phosphorylation of Multiple Proteins, Including Phospholipase C Gamma 1 and the Receptor Beta Gamma 2 Complex, in RBL-2H3 Rat Basophilic Leukemia Cells

W Li et al. Mol Cell Biol.

Abstract

In basophils, mast cells, and the RBL-2H3 tumor mast cell line, cross-linking the high-affinity immunoglobulin E receptor (Fc epsilon R1) stimulates a series of responses, particularly the activation of phospholipase C (PLC), that lead to allergic and other immediate hypersensitivity reactions. The mechanism of activation of PLC, however, is not clear. Here, we show that cross-linking Fc epsilon R1 on RBL-2H3 cells causes the tyrosine phosphorylation of at least 12 cellular proteins, including PLC gamma 1 (PLC gamma 1) and the receptor beta and gamma subunits. 32P-labeled PLC gamma 1 can be detected by anti-phosphotyrosine antibody as early as 10 s after the addition of antigen. The tyrosine-phosphorylated 33-kDa beta subunit and 9- to 11-kDa gamma subunit of the Fc epsilon R1 are additionally phosphorylated on serine and theonine residues, respectively, and are found as complexes with other phosphotyrosine-containing proteins in antigen-stimulated cells. Our results indicate a means by which the Fc epsilon R1 may control PLC activity in RBL-2H3 cells and raise the possibility that other receptor-mediated signalling events in mast cells may also be controlled through protein tyrosine phosphorylation.

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