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Transmembrane adaptor proteins in the high-affinity IgE receptor signaling
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SYSNO ASEP 0399709 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Transmembrane adaptor proteins in the high-affinity IgE receptor signaling Tvůrce(i) Dráber, Petr (UMG-J) RID
Hálová, Ivana (UMG-J) RID, ORCID
Levi-Schaffer, F. (IL)
Dráberová, Lubica (UMG-J) RIDZdroj.dok. Frontiers in Immunology. - : Frontiers Media - ISSN 1664-3224
Roč. 2, 11.1. (2012), s. 95Poč.str. 11 s. Forma vydání Online - E Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova IgE receptor ; LAT/LAT1 ; LAX ; NTAL/Lab/LAT2 ; PAG/Cbp ; mast cells ; plasma membrane ; transmembrane adaptor proteins Vědní obor RIV EB - Genetika a molekulární biologie CEP 1M0506 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GA301/09/1826 GA ČR - Grantová agentura ČR GAP302/10/1759 GA ČR - Grantová agentura ČR KAN200520701 GA AV ČR - Akademie věd Institucionální podpora UMG-J - RVO:68378050 CEZ AV0Z50520514 - UMG-J (2005-2011) UT WOS 000209501200011 DOI 10.3389/fimmu.2011.00095 Anotace Aggregation 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. Pracoviště Ústav molekulární genetiky Kontakt Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Rok sběru 2014
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