What precedes the initial tyrosine phosphorylation of the high affinity IgE receptor in antigen-activated mast cell?
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
20828563
DOI
10.1016/j.febslet.2010.08.045
PII: S0014-5793(10)00707-6
Knihovny.cz E-resources
- MeSH
- Phosphorylation MeSH
- Humans MeSH
- Mast Cells immunology metabolism MeSH
- Receptors, IgE metabolism MeSH
- Models, Theoretical MeSH
- Tyrosine metabolism MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- Receptors, IgE MeSH
- Tyrosine MeSH
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.
References provided by Crossref.org
Molecular Mechanisms of Mast Cell Activation by Cholesterol-Dependent Cytolysins
ORMDL2 Deficiency Potentiates the ORMDL3-Dependent Changes in Mast Cell Signaling
Signal transduction and chemotaxis in mast cells
New Regulatory Roles of Galectin-3 in High-Affinity IgE Receptor Signaling
Cytoskeleton in mast cell signaling
Transmembrane adaptor proteins in the high-affinity IgE receptor signaling