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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-01

AUTHORS

Eiseman, Joseph B. Bolen

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. More... »

PAGES

78-80

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/355078a0

DOI

http://dx.doi.org/10.1038/355078a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1039508343

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1370575


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