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What precedes the initial tyrosine phosphorylation of the high affinity IgE receptor in antigen-activated mast cell?
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SYSNO ASEP 0353415 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title What precedes the initial tyrosine phosphorylation of the high affinity IgE receptor in antigen-activated mast cell? Author(s) Bugajev, Viktor (UMG-J) RID
Bambousková, Monika (UMG-J)
Dráberová, Lubica (UMG-J) RID
Dráber, Petr (UMG-J) RIDSource Title FEBS Letters. - : Wiley - ISSN 0014-5793
Roč. 584, č. 24 (2010), s. 4949-4955Number of pages 7 s. Language eng - English Country GB - United Kingdom Keywords mast cell ; cell signaling ; plasma membrane Subject RIV EB - Genetics ; Molecular Biology R&D Projects 1M0506 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LC545 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GD204/05/H023 GA ČR - Czech Science Foundation (CSF) GA301/09/1826 GA ČR - Czech Science Foundation (CSF) GAP302/10/1759 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50520514 - UMG-J (2005-2011) UT WOS 000284943600020 DOI 10.1016/j.febslet.2010.08.045 Annotation An interaction of multivalent antigen with its IgE bound to the high-affinity IgE receptor (FcepsilonRI) 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 FcepsilonRI beta 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 FcepsilonRI phosphorylation. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2011
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