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Statements

Subject Item
n2:RIV%2F68378050%3A_____%2F12%3A00399709%21RIV14-GA0-68378050
rdf:type
n5:Vysledek skos:Concept
dcterms:description
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. 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.
dcterms:title
Transmembrane adaptor proteins in the high-affinity IgE receptor signaling Transmembrane adaptor proteins in the high-affinity IgE receptor signaling
skos:prefLabel
Transmembrane adaptor proteins in the high-affinity IgE receptor signaling Transmembrane adaptor proteins in the high-affinity IgE receptor signaling
skos:notation
RIV/68378050:_____/12:00399709!RIV14-GA0-68378050
n5:predkladatel
n20:ico%3A68378050
n3:aktivita
n17:I n17:P n17:Z
n3:aktivity
I, P(1M0506), P(GA301/09/1826), P(GAP302/10/1759), P(KAN200520701), Z(AV0Z50520514)
n3:cisloPeriodika
11.1.
n3:dodaniDat
n13:2014
n3:domaciTvurceVysledku
n6:5182581 n6:1820648 n6:6550789
n3:druhVysledku
n16:J
n3:duvernostUdaju
n19:S
n3:entitaPredkladatele
n10:predkladatel
n3:idSjednocenehoVysledku
174943
n3:idVysledku
RIV/68378050:_____/12:00399709
n3:jazykVysledku
n15:eng
n3:klicovaSlova
IgE receptor; LAT/LAT1; LAX; NTAL/Lab/LAT2; PAG/Cbp; mast cells; plasma membrane; transmembrane adaptor proteins
n3:klicoveSlovo
n4:transmembrane%20adaptor%20proteins n4:NTAL%2FLab%2FLAT2 n4:IgE%20receptor n4:mast%20cells n4:PAG%2FCbp n4:plasma%20membrane n4:LAT%2FLAT1 n4:LAX
n3:kodStatuVydavatele
CH - Švýcarská konfederace
n3:kontrolniKodProRIV
[F36425861A70]
n3:nazevZdroje
Frontiers in Immunology
n3:obor
n18:EB
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:projekt
n11:KAN200520701 n11:1M0506 n11:GA301%2F09%2F1826 n11:GAP302%2F10%2F1759
n3:rokUplatneniVysledku
n13:2012
n3:svazekPeriodika
2
n3:tvurceVysledku
Hálová, Ivana Dráberová, Lubica Dráber, Petr Levi-Schaffer, F.
n3:zamer
n12:AV0Z50520514
s:issn
1664-3224
s:numberOfPages
11
n14:doi
10.3389/fimmu.2011.00095