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- W4313383854 abstract "Abstract PD-1 is a cell surface receptor with immunoregulatory properties expressed in activated T cells. PD-1 binds to either PD-L1 or PD-L2 and mediates downstream tyrosine dephosphorylation of key proteins critical for TCR signaling. This prevents excessive inflammation as well as T cell mediated anti-tumor immunity. Anti-PD-1 therapy is effective in ~30% of cancer patients, of which up to 25% develop off-target immune inflammation. Little is known about downstream signaling triggered by PD-1 and further analysis will provide better rationales for safer and more effective PD-1 targeting therapies. We performed tandem mass tag spectrometry and examined protein phosphorylation in Jurkat T cells following PD-1 ligation by PD-L2. Computational analysis revealed the PD-1/PD-L2 phosphoproteomic landscape. Our results confirm previous reports that PD-1 ligation dephosphorylates key proteins in the TCR signaling cascade. In addition, compared to unstimulated cells and to cells stimulated via the TCR alone, αCD3 stimulation in the presence of PD-1 ligation led to significant dephosphorylation of proteins involved in cytoskeletal organization and cellular adhesion. Surprisingly, we observed increased S/T phosphorylation of proteins associated with cell cycle regulation, chromosomal organization and negative regulation of gene expression triggered by PD-1 ligation. Further analysis in primary human cells revealed that these PD-1 triggered pathways were T cell subset specific, which is key for developing T cell subset specific targeted therapies. Our study provides a comprehensive system wide view of the signaling cascade downstream of PD-1 and may serve as a springboard for future therapeutic approaches targeting the PD-1 pathway." @default.
- W4313383854 created "2023-01-06" @default.
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- W4313383854 date "2018-05-01" @default.
- W4313383854 modified "2023-09-23" @default.
- W4313383854 title "Global phosphoproteomic analysis of PD-1 signaling reveals T cell subset specific PD-1 functions" @default.
- W4313383854 doi "https://doi.org/10.4049/jimmunol.200.supp.112.6" @default.
- W4313383854 hasPublicationYear "2018" @default.
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