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

0353415 - ÚMG 2011 RIV GB eng J - Journal Article
Bugajev, Viktor - Bambousková, Monika - Dráberová, Lubica - Dráber, Petr
What precedes the initial tyrosine phosphorylation of the high affinity IgE receptor in antigen-activated mast cell?
FEBS Letters. Roč. 584, č. 24 (2010), s. 4949-4955. ISSN 0014-5793. E-ISSN 1873-3468
R&D Projects: GA MŠMT 1M0506; GA MŠMT LC545; GA ČR(CZ) GD204/05/H023; GA ČR GA301/09/1826; GA ČR GAP302/10/1759
Institutional research plan: CEZ:AV0Z50520514
Keywords : mast cell * cell signaling * plasma membrane
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 3.601, year: 2010

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.
Permanent Link: http://hdl.handle.net/11104/0192670