Molecular basis of T cell inactivation by CTLA-4.
basic_science · Level V
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Abstract
CTLA-4, a negative regulator of T cell function, was found to associate with the T cell receptor (TCR) complex zeta chain in primary T cells. The association of TCRzeta 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 TCRzeta bound to CTLA-4 and abolished the p56(lck)-inducible TCRzeta-CTLA-4 interaction. Thus, CTLA-4 inhibits TCR signal transduction by binding to TCRzeta 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.
Medical subject headings
- Antigens, Differentiation
- Immunoconjugates
- Lymphocyte Activation
- Membrane Proteins
- Receptors, Antigen, T-Cell
- Signal Transduction
- T-Lymphocytes