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Tyrosine-based activation motifs (TAMs) define a conserved
signaling sequence,
EX
YXL/IX
YXL/I, that
couples the T cell antigen receptor to protein tyrosine kinases and
adapter molecules. The present study shows that phosphorylation of both
tyrosines within the motif is required for high affinity binding of the
tyrosine kinase ZAP-70 whereas phosphorylation of the single
COOH-terminal tyrosine within the motif is optimal for the binding of
the adapter Shc. There were also quantitative differences in the ZAP-70
and Shc association with the 1-TAM since nM
concentrations of the doubly phosphorylated
1-TAM are sufficient
for ZAP-70 recruitment whereas micromolar levels of singly
phosphorylated TAMs are necessary for Shc binding. Shc is tyrosine
phosphorylated in antigen receptor-activated T cells and can
potentially form a complex with the adapter molecule Grb2 and could
thus recruit the Ras guanine nucleotide exchange protein Sos into the
antigen receptor complex. The present data show that Grb2 can bind to
the phosphorylated TAM, but this binding is independent of Shc and
there is no formation of
1-TAM
Shc
Grb2
Sos
complexes in antigen receptor-activated cells. Accordingly, Shc
function should not be considered in the context of Grb2/Sos
recruitment to the T cell antigen receptor complex.
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