Research ArticlePhosphoproteomics

Quantitative Phosphoproteomic Analysis of T Cell Receptor Signaling Reveals System-Wide Modulation of Protein-Protein Interactions

Science Signaling  18 Aug 2009:
Vol. 2, Issue 84, pp. ra46
DOI: 10.1126/scisignal.2000007

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The binding of antigen to the T cell receptor (TCR) complex triggers a cascade of responses that culminate in T cell activation. Key to the initial stages of this cascade is the phosphorylation of tyrosine residues in proteins proximal to the TCR, which enables the recruitment of other proteins that contain phosphotyrosine-binding domains. Given its importance to TCR signaling, tyrosine phosphorylation of target proteins has received considerable attention. To view protein phosphorylation from a larger perspective, Mayya et al. performed a system-level phosphoproteomics analysis of the events triggered by TCR activation in the human Jurkat T cell line. They found that the status of hundreds of phosphorylation sites was modulated in response to stimulation of the TCR. In addition to identifying previously unknown TCR-responsive phosphorylation events, this analysis also suggests a role for phosphorylated serine and threonine residues in modulating protein-protein interactions between many proteins involved in T cell responses.