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Department of Immunology, Duke University Medical Center, Durham, NC 27710
Linker for activation of T cells (LAT) is a membrane-associated
adaptor protein that is phosphorylated on multiple tyrosines upon TCR
cross-linking. Previous studies show that LAT is essential for
TCR-mediated signaling and thymocyte development. In this study, we
expressed a series of LAT Tyr to Phe mutants in LAT-deficient J.CaM2.5
cells and examined their tyrosine phosphorylation; association with
Grb2, Gads, and phospholipase C (PLC)-
1; and function in T cell
activation. Our results showed that the five membrane-distal tyrosines
were phosphorylated upon T cell activation. Grb2, Gads, and PLC-1
associated with LAT preferentially via different sets of tyrosine
residues; however, they failed to interact with LAT mutants containing
only one tyrosine. We also determined the minimal requirement of LAT
tyrosine residues in T cell activation and thymocyte development. Our
results showed that a minimum of three tyrosines is required for LAT to
function in T cell activation and thymocyte development. LAT mutants
that were capable of binding Grb2 and PLC-1 could reconstitute T
cell activation in LAT-deficient cells and thymocyte development in
LAT-deficient mice.
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