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- W1981205839 abstract "LAX is a transmembrane adaptor protein that is expressed in both T and B cells. Upon stimulation via the antigen receptors, it is tyrosine-phosphorylated and binds Grb2 and the p85 subunit of phosphatidylinositol 3-kinase. Disruption of the Lax gene causes hyperresponsiveness in T and B lymphocytes. Here, we showed that LAX was also expressed in mast cells. Upon engagement of the Fc epsilonRI, LAX was also phosphorylated and interacted with Grb2 and p85. LAX-deficient mast cells were hyperresponsive to stimulation via the Fc epsilonRI, as evidenced by enhanced degranulation, p38 MAPK, Akt, and phosphatidylinositol 3-kinase activation. This hyperresponsiveness was likely a consequence of reduced LAB expression after sensitization of mast cells with anti-dinitrophenyl IgE. In addition, Fc epsilonRI-mediated cytokine production and cell survival were also enhanced. These data suggested that LAX negatively regulates mast cell function." @default.
- W1981205839 created "2016-06-24" @default.
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- W1981205839 date "2006-07-01" @default.
- W1981205839 modified "2023-10-16" @default.
- W1981205839 title "Negative Regulation of FcϵRI-mediated Signaling and Mast Cell Function by the Adaptor Protein LAX" @default.
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- W1981205839 doi "https://doi.org/10.1074/jbc.m601535200" @default.
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