What precedes the initial tyrosine phosphorylation of the high affinity IgE receptor in antigen-activated mast cell?

Viktor Bugajev, Monika Bambousková, Lubica Dráberová, Petr Dráber

Research output: Contribution to journalReview articlepeer-review

25 Scopus citations

Abstract

An interaction of multivalent antigen with its IgE bound to the high-affinity IgE receptor (FcεRI) on the surface of mast cells or basophils initiates a series of signaling events leading to degranulation and release of inflammatory mediators. Earlier studies showed that the first biochemically defined step in this signaling cascade is tyrosine phosphorylation of the FcεRI β subunit by Src family kinase Lyn. However, the processes affecting this step remained elusive. In this review we critically evaluate three current models (transphosphorylation, lipid raft, and our preferential protein tyrosine kinase-protein tyrosine phosphatase interplay model) substantiating three different mechanisms of FcεRI phosphorylation.

Original languageEnglish
Pages (from-to)4949-4955
Number of pages7
JournalFEBS Letters
Volume584
Issue number24
DOIs
StatePublished - Dec 15 2010

Keywords

  • Cell signaling
  • Immunoreceptor
  • Mast cell
  • Plasma membrane
  • Protein tyrosine kinase
  • Protein tyrosine phosphatase

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