| First Author | Voisinne G | Year | 2019 |
| Journal | Nat Immunol | Volume | 20 |
| Issue | 11 | Pages | 1530-1541 |
| PubMed ID | 31591574 | Mgi Jnum | J:282407 |
| Mgi Id | MGI:6380825 | Doi | 10.1038/s41590-019-0489-8 |
| Citation | Voisinne G, et al. (2019) Quantitative interactomics in primary T cells unveils TCR signal diversification extent and dynamics. Nat Immunol 20(11):1530-1541 |
| abstractText | The activation of T cells by the T cell antigen receptor (TCR) results in the formation of signaling protein complexes (signalosomes), the composition of which has not been analyzed at a systems level. Here, we isolated primary CD4(+) T cells from 15 gene-targeted mice, each expressing one tagged form of a canonical protein of the TCR-signaling pathway. Using affinity purification coupled with mass spectrometry, we analyzed the composition and dynamics of the signalosomes assembling around each of the tagged proteins over 600 s of TCR engagement. We showed that the TCR signal-transduction network comprises at least 277 unique proteins involved in 366 high-confidence interactions, and that TCR signals diversify extensively at the level of the plasma membrane. Integrating the cellular abundance of the interacting proteins and their interaction stoichiometry provided a quantitative and contextual view of each documented interaction, permitting anticipation of whether ablation of a single interacting protein can impinge on the whole TCR signal-transduction network. |
