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.
Original language | English |
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Pages (from-to) | 384-392 |
Number of pages | 9 |
Journal | Nature Immunology |
Volume | 15 |
Issue number | 4 |
DOIs | |
Publication status | Published - Apr 2014 |
All Science Journal Classification (ASJC) codes
- Immunology and Allergy
- Immunology