Number of the records: 1  

Transmembrane adaptor proteins in the high-affinity IgE receptor signaling

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    SYSNO ASEP0399709
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleTransmembrane adaptor proteins in the high-affinity IgE receptor signaling
    Author(s) Dráber, Petr (UMG-J) RID
    Hálová, Ivana (UMG-J) RID, ORCID
    Levi-Schaffer, F. (IL)
    Dráberová, Lubica (UMG-J) RID
    Source TitleFrontiers in Immunology. - : Frontiers Media - ISSN 1664-3224
    Roč. 2, 11.1. (2012), s. 95
    Number of pages11 s.
    Publication formOnline - E
    Languageeng - English
    CountryCH - Switzerland
    KeywordsIgE receptor ; LAT/LAT1 ; LAX ; NTAL/Lab/LAT2 ; PAG/Cbp ; mast cells ; plasma membrane ; transmembrane adaptor proteins
    Subject RIVEB - Genetics ; Molecular Biology
    R&D Projects1M0506 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    GA301/09/1826 GA ČR - Czech Science Foundation (CSF)
    GAP302/10/1759 GA ČR - Czech Science Foundation (CSF)
    KAN200520701 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    Institutional supportUMG-J - RVO:68378050
    CEZAV0Z50520514 - UMG-J (2005-2011)
    UT WOS000209501200011
    DOI10.3389/fimmu.2011.00095
    AnnotationAggregation of the high-affinity IgE receptor (FcεRI) initiates a cascade of signaling events leading to release of preformed inflammatory and allergy mediators and de novo synthesis and secretion of cytokines and other compounds. The first biochemically well defined step of this signaling cascade is tyrosine phosphorylation of the FcεRI subunits by Src family kinase Lyn, followed by recruitment and activation of spleen tyrosine kinase (Syk). Activity of Syk is decisive for the formation of multicomponent signaling assemblies, the signalosomes, in the vicinity of the receptors. Formation of the signalosomes is dependent on the presence of transmembrane adaptor proteins (TRAPs). These proteins are characterized by a short extracellular domain, a single transmembrane domain, and a cytoplasmic tail with various motifs serving as anchors for cytoplasmic signaling molecules. In mast cells five TRAPs have been identified [linker for activation of T cells (LAT), non-T cell activation linker (NTAL), linker for activation of X cells (LAX), phosphoprotein associated with glycosphingolipid-enriched membrane microdomains (PAG), and growth factor receptor-bound protein 2 (Grb2)-binding adaptor protein, transmembrane (GAPT)]; engagement of four of them (LAT, NTAL, LAX, and PAG) in FcεRI signaling has been documented. Here we discuss recent progress in the understanding of how TRAPs affect FcεRI-mediated mast cell signaling. The combined data indicate that individual TRAPs have irreplaceable roles in important signaling events such as calcium response, degranulation, cytokines production, and chemotaxis.
    WorkplaceInstitute of Molecular Genetics
    ContactNikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217
    Year of Publishing2014
Number of the records: 1  

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