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Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases

Nature volume 355, pages 78–80 (1992)Cite this article

Abstract

THE high-affinity IgE receptor (FcɛRI), which is expressed on the surface of mast cells and basophils, has a central role in immediate allergic responses. In the rat basophilic leukaemia cell line RBL-2H3, which is a model system for the analysis of FcɛRI-mediated signal transduction, surface engagement of FcɛRI induces histamine release and the tyrosine phosphorylation of several distinct proteins1. Although the α, β and γ subunits of FcɛRI lack intrinsic tyrosine protein kinase (TPK) activity, a kinase that copurifies with FcɛRI phosphorylates the β and γ subunits of the receptor on tyrosine residues2,3. We report here that in RBL-2H3 cells, p56lyn and pp60c-src are activated after FcɛRI crosslinking, and p56lyn coimmunoprecipitates with FcɛRI. In the mouse mastcell line PT-18, another cell type used to study FCɛRI-mediated signalling, tyrosine phosphorylation of proteins is also an immediate consequence of receptor crosslinking. Notably, the only detectable src protein-related TPK in PT-18 cells is p62c-yes, and it is this TPK that is activated on FcɛRI engagement and coimmunoprecipitates with the receptor. Therefore, it seems that different src protein-related TPKs can associate with the same receptor and become activated after receptor engagement.

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Affiliations

  1. Department of Molecular Biology, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey, 08543-4000, USA

    Eiseman & Joseph B. Bolen

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  1. Eiseman
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  2. Joseph B. Bolen
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Eiseman, Bolen, J. Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases. Nature 355, 78–80 (1992). https://doi.org/10.1038/355078a0

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