Interaction of Csk with PAG

Stable Identifier
Reaction [binding]
Homo sapiens
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Csk is a tyrosine kinase that phosphorylates the negative regulatory C-terminal tyrosine residue Y505 of Lck to maintain Lck in an inactive state. In resting T cells, Csk is targeted to lipid rafts through engagement of its SH2 domain with phosphotyrosine residue pY317 of PAG. PAG is expressed as a tyrosine phosphorylated protein in nonstimulated T-cells. This interaction of Csk and PAG allows activation of Csk and inhibition of Lck. Given that PAG-1 T cell knock out show a weak phenotype, some other protein may substitute in activating Csk.

Literature References
PubMed ID Title Journal Year
12938237 The activation of Csk by CD4 interferes with TCR-mediated activatory signaling

Tuosto, L, Marinari, B, Piccolella, E, Simeoni, L, Schraven, B

Eur J Immunol 2003
10790433 Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation

Shevchenko, A, Korinek, V, Bruyns, E, Scherer, J, Hilgert, I, Brdicka, T, Cerny, J, Horejsi, V, Kornacker, B, Leo, A, Angelisova, P, Pavlistova, D, Schraven, B, Drbal, K, Kuramitsu, Y

J Exp Med 2000
Orthologous Events
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