Protein tyrosine kinase p59fyn is associated with the T cell receptor-CD3 complex in functional human lymphocytes

1992 ◽  
Vol 22 (1) ◽  
pp. 283-286 ◽  
Author(s):  
Martin Gassmann ◽  
Maria Guttinger ◽  
Kurt E. Amrein ◽  
Paul Burn
Keyword(s):  
T Cell ◽  
Tyrosine Kinase ◽  
T Cell Receptor ◽  
Protein Tyrosine Kinase ◽  
Human Lymphocytes ◽  
Cell Receptor ◽  
Protein Tyrosine

scholarly journals Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor

Nature ◽  
2007 ◽  
Vol 446 (7137) ◽  
pp. 824-824
Author(s):  
Marcos H. Hatada ◽  
Xiaode Lu ◽  
Ellen R. Laird ◽  
Jeremy Green ◽  
Jay P. Morgenstern ◽  
...  
Keyword(s):  
T Cell ◽  
Tyrosine Kinase ◽  
T Cell Receptor ◽  
Molecular Basis ◽  
Protein Tyrosine Kinase ◽  
Cell Receptor ◽  
Protein Tyrosine

Regulation of T cell receptor signaling by a src family protein-tyrosine kinase (p59fyn)

Cell ◽  
1991 ◽  
Vol 65 (2) ◽  
pp. 281-291 ◽  
Author(s):  
Michael P. Cooke ◽  
Kristin M. Abraham ◽  
Katherine A. Forbush ◽  
Roger M. Perimutter
Keyword(s):  
T Cell ◽  
Tyrosine Kinase ◽  
T Cell Receptor ◽  
Protein Tyrosine Kinase ◽  
Cell Receptor ◽  
Receptor Signaling ◽  
Protein Tyrosine ◽  
Family Protein ◽  
T Cell Receptor Signaling ◽  
Cell Receptor Signaling

scholarly journals ZAP-70 Association with T Cell Receptor ζ (TCRζ): Fluorescence Imaging of Dynamic Changes upon Cellular Stimulation

1998 ◽  
Vol 143 (3) ◽  
pp. 613-624 ◽  
Author(s):  
Joanne Sloan-Lancaster ◽  
John Presley ◽  
Jan Ellenberg ◽  
Tetsuo Yamazaki ◽  
Jennifer Lippincott-Schwartz ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
T Cell ◽  
Tyrosine Kinase ◽  
T Cell Receptor ◽  
Protein Tyrosine Kinase ◽  
Specific Interaction ◽  
Active Form ◽  
Lymphocyte Activation ◽  
Cell Receptor ◽  
Protein Tyrosine

The nonreceptor protein tyrosine kinase ZAP-70 is a critical enzyme required for successful T lymphocyte activation. After antigenic stimulation, ZAP-70 rapidly associates with T cell receptor (TCR) subunits. The kinetics of its translocation to the cell surface, the properties of its specific interaction with the TCRζ chain expressed as a chimeric protein (TTζ and Tζζ), and its mobility in different intracellular compartments were studied in individual live HeLa cells, using ZAP-70 and Tζζ fused to green fluorescent protein (ZAP-70 GFP and Tζζ–GFP, respectively). Time-lapse imaging using confocal microscopy indicated that the activation-induced redistribution of ZAP-70 to the plasma membrane, after a delayed onset, is of long duration. The presence of the TCRζ chain is critical for the redistribution, which is enhanced when an active form of the protein tyrosine kinase Lck is coexpressed. Binding specificity to TTζ was indicated using mutant ZAP-70 GFPs and a truncated ζ chimera. Photobleaching techniques revealed that ZAP-70 GFP has decreased mobility at the plasma membrane, in contrast to its rapid mobility in the cytosol and nucleus. Tζζ– GFP is relatively immobile, while peripherally located ZAP-70 in stimulated cells is less mobile than cytosolic ZAP-70 in unstimulated cells, a phenotype confirmed by determining the respective diffusion constants. Examination of the specific molecular association of signaling proteins using these approaches has provided new insights into the TCRζ–ZAP-70 interaction and will be a powerful tool for continuing studies of lymphocyte activation.

Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor

Nature ◽  
1995 ◽  
Vol 377 (6544) ◽  
pp. 32-38 ◽  
Author(s):  
Marcos H. Hatada ◽  
Xiaode Lu ◽  
Ellen R. Laird ◽  
Jeremy Green ◽  
Jay P. Morgenstern ◽  
...  
Keyword(s):  
T Cell ◽  
Tyrosine Kinase ◽  
T Cell Receptor ◽  
Molecular Basis ◽  
Protein Tyrosine Kinase ◽  
Cell Receptor ◽  
Protein Tyrosine

Protein tyrosine kinase p56lck controls allelic exclusion of T-cell receptor β-chain genes

Nature ◽  
1993 ◽  
Vol 365 (6446) ◽  
pp. 552-554 ◽  
Author(s):  
Steven J. Anderson ◽  
Steven D. Levin ◽  
Roger M. Perlmutter
Keyword(s):  
T Cell ◽  
Tyrosine Kinase ◽  
T Cell Receptor ◽  
Protein Tyrosine Kinase ◽  
Cell Receptor ◽  
Allelic Exclusion ◽  
Protein Tyrosine ◽  
Β Chain

scholarly journals 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.

1996 ◽  
Vol 184 (2) ◽  
pp. 365-376 ◽  
Author(s):  
V A Boussiotis ◽  
D L Barber ◽  
B J Lee ◽  
J G Gribben ◽  
G J Freeman ◽  
...  
Keyword(s):  
T Cell ◽  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
T Cell Receptor ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Kinase ◽  
Cell Receptor ◽  
Specific Protein ◽  
Protein Tyrosine ◽  
Potential Applications

When stimulated through their antigen receptor, without costimulation, T cells enter a state of antigen-specific unresponsiveness, termed anergy. B7-mediated costimulation, signaling via CD28, is sufficient to prevent the induction of anergy. Here we show that ligation of T cell receptor (TCR) by alloantigen alone, which results in anergy, activates tyrosine phosphorylation of TCR zeta and its association with fyn. In contrast, TCR ligation in the presence of B7 costimulation, which results in productive immunity, activates tyrosine phosphorylation of TCR zeta and CD3 chains, which associate with activated lck and zeta-associated protein (ZAP) 70. Under these conditions, CD28 associates with activated lck and TCR zeta. These data suggest that the induction of anergy is an active signaling process characterized by the association of TCR zeta and fyn. In addition, CD28-mediated costimulation may prevent the induction of anergy by facilitating the effective association of TCR zeta and CD3 epsilon with the critical protein tyrosine kinase lck, and the subsequent recruitment of ZAP-70. Strategies to inhibit or activate TCR-associated, specific protein tyrosine kinase-mediated pathways may provide a basis for drug development with potential applications in the fields of transplantation, autoimmunity, and tumor immunity.

Investigation of the kinetics and order of tyrosine phosphorylation in the T-cell receptor zeta chain by the protein tyrosine kinase Lck

2003 ◽  
Vol 270 (11) ◽  
pp. 2369-2376 ◽  
Author(s):  
Hazel R. Housden ◽  
Paul J. S. Skipp ◽  
Matthew P. Crump ◽  
Robert J. Broadbridge ◽  
Tom Crabbe ◽  
...  
Keyword(s):  
T Cell ◽  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
T Cell Receptor ◽  
Protein Tyrosine Kinase ◽  
Cell Receptor ◽  
Protein Tyrosine ◽  
Zeta Chain

scholarly journals Phosphorylation of SLP-76 by the ZAP-70 Protein-tyrosine Kinase Is Required for T-cell Receptor Function

1996 ◽  
Vol 271 (33) ◽  
pp. 19641-19644 ◽  
Author(s):  
Juliane Bubeck Wardenburg ◽  
Chong Fu ◽  
Janet K. Jackman ◽  
Horst Flotow ◽  
Sandra E. Wilkinson ◽  
...  
Keyword(s):  
T Cell ◽  
Tyrosine Kinase ◽  
T Cell Receptor ◽  
Protein Tyrosine Kinase ◽  
Cell Receptor ◽  
Receptor Function ◽  
Protein Tyrosine
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