Syk and Lyn mediate distinct Syk phosphorylation events in FcɛRI-signal transduction: implications for regulation of IgE-mediated degranulation.

@article{Sanderson2010SykAL,
  title={Syk and Lyn mediate distinct Syk phosphorylation events in FcɛRI-signal transduction: implications for regulation of IgE-mediated degranulation.},
  author={Michael P. Sanderson and Eva Wex and Takeshi Kono and Katsuhiro Uto and Andreas Schnapp},
  journal={Molecular immunology},
  year={2010},
  volume={48 1-3},
  pages={171-8}
}
Spleen tyrosine kinase (Syk) is a key regulatory factor in the IgE-mediated allergic signal transduction pathway in mast cells and basophils. Syk is phosphorylated on a number of tyrosines following the binding of IgE/allergen complexes to FcɛRI receptors leading to initiation of inflammatory signaling via downstream enzymes and scaffolding proteins. We examined the kinases responsible for the phosphorylation of key Syk tyrosines in rat RBL-2H3 basophilic cells and bone marrow-derived mast… CONTINUE READING
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