| Literature DB >> 24584089 |
Romain Roncagalli1,2,3, Simon Hauri4,5, Fréderic Fiore6,7,8, Yinming Liang1,2,3, Zhi Chen9, Amandine Sansoni6,7,8, Kartiek Kanduri9, Rachel Joly1,2,3, Aurélie Malzac1,2,3, Harri Lähdesmäki9,10, Riitta Lahesmaa9, Sho Yamasaki11, Takashi Saito12, Marie Malissen1,2,3, Ruedi Aebersold4,13, Matthias Gstaiger4,5, Bernard Malissen1,2,3,6,7,8.
Abstract
T cell antigen receptor (TCR)-mediated activation of T cells requires the interaction of dozens of proteins. Here we used quantitative mass spectrometry and activated primary CD4(+) T cells from mice in which a tag for affinity purification was knocked into several genes to determine the composition and dynamics of multiprotein complexes that formed around the kinase Zap70 and the adaptors Lat and SLP-76. Most of the 112 high-confidence time-resolved protein interactions we observed were previously unknown. The surface receptor CD6 was able to initiate its own signaling pathway by recruiting SLP-76 and the guanine nucleotide-exchange factor Vav1 regardless of the presence of Lat. Our findings provide a more complete model of TCR signaling in which CD6 constitutes a signaling hub that contributes to the diversification of TCR signaling.Entities:
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Year: 2014 PMID： 24584089 PMCID： PMC4037560 DOI： 10.1038/ni.2843
Source DB: PubMed Journal: Nat Immunol ISSN： 1529-2908 Impact factor: 25.606