Syk and ZAP-70 mediate recruitment of p56lck/CD4 to the activated T cell receptor/CD3/zeta complex.

Détails

ID Serval
serval:BIB_585ED2ABC41F
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Syk and ZAP-70 mediate recruitment of p56lck/CD4 to the activated T cell receptor/CD3/zeta complex.
Périodique
Journal of Experimental Medicine
Auteur(s)
Thome M., Duplay P., Guttinger M., Acuto O.
ISSN
0022-1007 (Print)
ISSN-L
0022-1007
Statut éditorial
Publié
Date de publication
1995
Peer-reviewed
Oui
Volume
181
Numéro
6
Pages
1997-2006
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
During antigen recognition by T cells, CD4 and the T-cell receptor (TCR)/CD3/zeta complex are thought to interact with the same major histocompatibility complex II molecule in a stable ternary complex. Evidence has suggested that the association of CD4 with TCR/CD3/zeta requires the interaction of the protein tyrosine kinase p56lck with CD4. We have taken a biochemical approach to understand the mechanism by which p56lck and, in particular, its src homology (SH) 2 domain contributes to the association of CD4 with TCR/CD3/zeta during activation. We have previously shown that the p56lck SH2 domain binds directly to tyrosine-phosphorylated ZAP-70. Here we formally demonstrate the in vivo association of p56lck with the homologous protein tyrosine kinases Syk and ZAP-70 after CD3 stimulation of Jurkat cells. A tyrosine-phosphorylated peptide containing the sequence predicted to be optimal for binding to the SH2 domain of src family kinases specifically competes for this association, indicating that tyrosine-phosphorylated ZAP-70 and Syk bind to p56lck by an SH2-mediated interaction. We also show that the same peptide is able to compete for the activation-dependent TCR/CD4 association in Jurkat cells. Moreover, ZAP-70 and CD4 cocap only after CD3 stimulation in human T lymphoblasts. We propose that the interaction of the p56lck SH2 domain with zeta-associated tyrosine-phosphorylated ZAP-70 and/or Syk enables CD4 to associate with antigen-stimulated TCR/CD3/zeta complexes.
Mots-clé
Antigens, CD/immunology, Antigens, CD4/immunology, Cell Line, Electrophoresis, Polyacrylamide Gel, Enzyme Precursors/isolation & purification, Enzyme Precursors/metabolism, Humans, Intracellular Signaling Peptides and Proteins, Kinetics, Lymphocyte Activation, Lymphocyte Specific Protein Tyrosine Kinase p56(lck), Membrane Proteins/immunology, Phosphorylation, Phosphotyrosine, Protein Binding, Protein-Tyrosine Kinases/isolation & purification, Protein-Tyrosine Kinases/metabolism, Receptor-CD3 Complex, Antigen, T-Cell/immunology, Receptors, Antigen, T-Cell/immunology, T-Lymphocytes/immunology, Tumor Cells, Cultured, Tyrosine/analogs & derivatives, Tyrosine/analysis, ZAP-70 Protein-Tyrosine Kinase
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:11
Dernière modification de la notice
20/08/2019 15:12
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