Phosphorylation of PD-1

Stable Identifier
R-HSA-389762
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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The cytoplasmic domain of PD-1 features two critical tyrosine-based motifs: the Immunoreceptor Tyrosine-based Inhibitory Motif (ITIM) and the Immunoreceptor Tyrosine-based Switch Motif (ITSM). Upon engagement with its ligands, PD-L1 (B7-H1) and PD-L2 (B7-DC), PD-1 becomes phosphorylated at tyrosine residues 223 and 248 within these motifs. This phosphorylation is catalyzed by kinases such as Lck and Csk, which bind to these motifs and are likely involved in initiating and regulating the phosphorylation of PD-1. These phosphorylation events are crucial for recruiting downstream signaling molecules that mediate PD-1’s inhibitory effects on T cell activation and immune response (Sheppard et al. 2004).
Literature References
PubMed ID Title Journal Year
18759926 Control of peripheral T-cell tolerance and autoimmunity via the CTLA-4 and PD-1 pathways

Fife, BT, Bluestone, JA

Immunol Rev 2008
18173375 PD-1 and its ligands in tolerance and immunity

Keir, ME, Sharpe, AH, Freeman, GJ, Butte, MJ

Annu Rev Immunol 2008
12947224 Cytotoxic T-lymphocyte antigen-4 and programmed death-1 function as negative regulators of lymphocyte activation

Carter, LL, Carreno, BM

Immunol Res 2003
Participants
Participates
Catalyst Activity

protein tyrosine kinase activity of LCK, CSK [cytosol]

Orthologous Events
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