• Publications
  • Influence
LAT The ZAP-70 Tyrosine Kinase Substrate that Links T Cell Receptor to Cellular Activation
The cloning of the cDNA is reported for a highly tyrosine-phosphorylated 36-38 kDa protein, previously characterized by its association with Grb2, phospholipase C-gamma1, and the p85 subunit of phosphoinositide 3-kinase, which is phosphorylated by ZAP-70/Syk protein tyrosines leading to recruitment of multiple signaling molecules. Expand
LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation.
It is demonstrated that human LAT is palmitoylated and that palMIToylated LAT predominantly localizes into glycolipid-enriched microdomains (GEMs). Expand
Fyn kinase initiates complementary signals required for IgE-dependent mast cell degranulation
It is reported here that FcεRI also uses a Fyn kinase–dependent pathway that does not require Lyn kinase or the adapter LAT for its initiation, but is necessary for mast cell degranulation. Expand
Genetic Evidence for Differential Coupling of Syk Family Kinases to the T-Cell Receptor: Reconstitution Studies in a ZAP-70-Deficient Jurkat T-Cell Line
In isolation and phenotypic characterization of a Syk- and ZAP-70-negative somatic mutant derived from the Jurkat T-cell line, transfection experiments with Zap-70–Syk chimeric proteins indicated that both the amino- terminal regulatory regions and the carboxy-terminal catalytic domains of Syk and Z AP-70 contribute to the distinctive functional properties of these PTKs. Expand
Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins.
  • L. Samelson
  • Biology, Medicine
  • Annual review of immunology
  • 2002
This chapter reviews some of the critical substrates of these PTKs, the adapter proteins that, following phosphorylation on tyrosine residues, serve as binding sites for many of thecritical effector enzymes and other adapter proteins required for T cell activation. Expand
T cell receptor ligation induces the formation of dynamically regulated signaling assemblies
It is indicated that these complexes can form within seconds of TCR engagement, in the absence of either lipid raft aggregation or the formation of a central TCR-rich cluster. Expand
Association of Grb2, Gads, and phospholipase C-gamma 1 with phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations on T cell angigen receptor-mediated signaling.
The results strongly suggest that PLC-gamma activation regulates Ras activation in these cells, and show that three distal tyrosines, Tyr(171), Tyr(191), and Tyr(226), are responsible for Grb2-binding; Tyr( 171, and Tyr (191), but not Tyr( 226), are necessary for Gads binding. Expand
Identification of a monoclonal antibody specific for a murine T3 polypeptide.
Results identify T3-epsilon as a cell surface protein involved in the transduction of activation signals and can both activate and inhibit T-cell function. Expand
Molecular basis of T cell inactivation by CTLA-4.
CTLA-4 inhibits TCR signal transduction by binding to TCRzeta and inhibiting tyrosine phosphorylation after T cell activation, and these findings have broad implications for the negative regulation of T cell function and T cell tolerance. Expand
T cell antigen-receptor signal transduction.
Glycolipid-enriched microdomains play a crucial role in T cell activation and TCR-induced cytoskeletal changes involve signalling through SLP-76-Vav-Nck to activate effectors of the Rho-family of GTPases. Expand