Molecular Basis of T Cell Inactivation by CTLA-4
0301 basic medicine
Mice, Inbred BALB C
Immunoconjugates
Protein Tyrosine Phosphatase, Non-Receptor Type 6
Intracellular Signaling Peptides and Proteins
Models, Immunological
Membrane Proteins
Protein Tyrosine Phosphatase, Non-Receptor Type 11
Lymphocyte Activation
Antigens, Differentiation
Cell Line
Abatacept
Mice
03 medical and health sciences
0302 clinical medicine
Antigens, CD
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
Animals
Humans
CTLA-4 Antigen
Phosphorylation
Phosphotyrosine
Cells, Cultured
DOI:
10.1126/science.282.5397.2263
Publication Date:
2002-07-27T09:37:56Z
AUTHORS (10)
ABSTRACT
CTLA-4, a negative regulator of T cell function, was found to associate with the T cell receptor (TCR) complex ζ chain in primary T cells. The association of TCRζ with CTLA-4, reconstituted in 293 transfectants, was enhanced by p56
lck
-induced tyrosine phosphorylation. Coexpression of the CTLA-4–associated tyrosine phosphatase, SHP-2, resulted in dephosphorylation of TCRζ bound to CTLA-4 and abolished the p56
lck
-inducible TCRζ–CTLA-4 interaction. Thus, CTLA-4 inhibits TCR signal transduction by binding to TCRζ and inhibiting tyrosine phosphorylation after T cell activation. These findings have broad implications for the negative regulation of T cell function and T cell tolerance.
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