About: Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor.     Goto   Sponge   NotDistinct   Permalink

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Description
  • PAG/Cbp is a transmembrane adaptor molecule found in lipid rafts, tyrosine phosphorylated and associated with Csk. PAG tyrosine phosphorylation and association with Csk are suppressed in response to activation of normal mouse T cells. By expressing wild-type and phosphorylation-defective (dominant-negative) PAG polypeptides in these cells, we found that the inhibitory effect of PAG is dependent on its capacity to be tyrosine phosphorylated and to associate with Csk. PAG-mediated inhibition was accompanied by a repression of proximal TCR signaling and was rescued by expression of a constitutively activated Src-related kinase, implying that it is due to an inactivation of Src kinases by PAG-associated Csk. Transmembrane PTP CD45 seems to play an important role in PAG dephosphorylation. Thus, PAG is a bona fide negative regulator of T-cell activation as a result of its capacity to recruit Csk; its inhibitory function in T cells is suppressed by CD45.
  • PAG/Cbp is a transmembrane adaptor molecule found in lipid rafts, tyrosine phosphorylated and associated with Csk. PAG tyrosine phosphorylation and association with Csk are suppressed in response to activation of normal mouse T cells. By expressing wild-type and phosphorylation-defective (dominant-negative) PAG polypeptides in these cells, we found that the inhibitory effect of PAG is dependent on its capacity to be tyrosine phosphorylated and to associate with Csk. PAG-mediated inhibition was accompanied by a repression of proximal TCR signaling and was rescued by expression of a constitutively activated Src-related kinase, implying that it is due to an inactivation of Src kinases by PAG-associated Csk. Transmembrane PTP CD45 seems to play an important role in PAG dephosphorylation. Thus, PAG is a bona fide negative regulator of T-cell activation as a result of its capacity to recruit Csk; its inhibitory function in T cells is suppressed by CD45. (en)
Title
  • Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor.
  • Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor. (en)
skos:prefLabel
  • Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor.
  • Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor. (en)
skos:notation
  • RIV/68378050:_____/03:23033078!RIV/2004/AV0/A23004/N
http://linked.open.../vavai/riv/strany
  • 2017;2028
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(LN00A026), Z(AV0Z5052915)
http://linked.open...iv/cisloPeriodika
  • 6
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 620808
http://linked.open...ai/riv/idVysledku
  • RIV/68378050:_____/03:23033078
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • PAG; Csk; T cell activation (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [DFCFB608525F]
http://linked.open...i/riv/nazevZdroje
  • Molecular and Cellular Biology
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...ocetUcastnikuAkce
http://linked.open...nichUcastnikuAkce
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 23
http://linked.open...iv/tvurceVysledku
  • Hořejší, Václav
  • Davidson, D.
  • Veillette, A.
  • Thomas, M. L.
  • Bakinowski, M.
http://linked.open...n/vavai/riv/zamer
issn
  • 0270-7306
number of pages
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