Interaction of Csk with PAG

Stable Identifier
R-HSA-203774
Type
Reaction [binding]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
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

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

J Exp Med 2000
12938237 The activation of Csk by CD4 interferes with TCR-mediated activatory signaling

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

Eur J Immunol 2003
Participants
Participant Of
Orthologous Events
Authored
Reviewed
Created