ArticleProceedings of the National Academy of Sciences of the United States of America1994
Delineation of a T-cell activation motif required for binding of protein tyrosine kinases containing tandem SH2 domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 67 citations in OpenAlex.
- ITAM-mediated signaling by the T-cell antigen receptor.Cold Spring Harbor perspectives in biology · 2010Review
- Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- The pattern recognition receptor Dectin-1: from fungi to mycobacteria.Current drug targets · 2008Review
- The C-type lectin receptors CLEC-2 and Dectin-1, but not DC-SIGN, signal via a novel YXXL-dependent signaling cascade.The Journal of biological chemistry · 2007Article
- ZAP-70 association with T cell receptor zeta (TCRzeta): fluorescence imaging of dynamic changes upon cellular stimulation.The Journal of cell biology · 1998Article
- ITIMs and ITAMs. The Yin and Yang of antigen and Fc receptor-linked signaling machinery.Immunologic research · 1997Review
- Differential association of protein tyrosine kinases with the T cell receptor is linked to the induction of anergy and its prevention by B7 family-mediated costimulation.The Journal of experimental medicine · 1996Article
- Conformational changes induced in the protein tyrosine kinase p72syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides.Molecular and cellular biology · 1996Article
- Dominant-negative zeta-associated protein 70 inhibits T cell antigen receptor signaling.The Journal of experimental medicine · 1996Article
- Activation of the high-affinity immunoglobulin E receptor Fc epsilon RI in RBL-2H3 cells is inhibited by Syk SH2 domains.Molecular and cellular biology · 1995Article
- Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function.The EMBO journal · 1995Article
- Analysis of the interaction of ZAP-70 and syk protein-tyrosine kinases with the T-cell antigen receptor by plasmon resonance.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- The intracellular signal transduction mechanism of interleukin 5 in eosinophils: the involvement of lyn tyrosine kinase and the Ras-Raf-1-MEK-microtubule-associated protein kinase pathway.The Journal of experimental medicine · 1995Article
- ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity.The Journal of experimental medicine · 1995Article
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8 authors at 2 institutions in 1 country.
Funding
Abstract
To define the T-cell receptor signal transduction motif, we have transfected human and murine T-cell lines with a chimeric receptor consisting of the extracellular and transmembrane domains of human CD8 alpha and the membrane-proximal portion of CD3 zeta containing at its C terminus either an 18-amino acid segment (NQLYNELNLGRREEYDVL) or alanine-scanning point mutant derivatives. Crosslinking of the extracellular domain of the chimera is sufficient to initiate Ca2+ flux, interleukin 2 production, and tyrosine phosphorylation of cellular proteins including the chimera. Subsequently, the chimera becomes associated with several tyrosine-phosphorylated proteins, among them the 70-kDa protein tyrosine kinase ZAP70. Mutational data identify the T-cell activation motif as Y(X)2L(X)7Y(X)2L and show that each of the four designated residues is necessary for the above activation events. Recombinant protein containing the two tandem SH2 domains derived from ZAP70 binds to a synthetic peptide corresponding to the above 18-amino acid motif but only when both tyrosines are phosphorylated; in contrast, little or no binding is observed to monophosphorylated or nonphosphorylated analogues. These results imply that after receptor crosslinking in T cells, and by inference also in B cells and mast cells, the motif is phosphorylated on both tyrosine residues, thereafter serving as a docking site for protein tyrosine kinases containing tandem SH2 domains.
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