Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: defining the nature of a signalling motif
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Summary
It is proposed that the activation of cells by the tyrosine activating motif occurs in four discrete steps: binding of p59fyn, phosphorylation of the motif, binding of Zap-70, and activation of ZAP-70 kinase activity.
- Type
- article
- Published
- 1994-06-01
- Cited by
- 158
- References
- 53
- Access
- Open access
- OpenAlex
- https://openalex.org/W1817318311
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:23591391
Keywords
Immunoreceptor tyrosine-based activation motif, Biology, SH2 domain, Sequence motif, Tyrosine
References
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- The T cell antigen receptor zeta chain is tyrosine phosphorylated upon activation.
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- Increases in tyrosine phosphorylation are detectable before phospholipase C activation after T cell receptor stimulation.
- Physical association of CD4 with the T cell receptor.
- T cell antigen receptor activation pathways: the tyrosine kinase connection.
- Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src.
- Association of tyrosine kinase p56lck with CD4 inhibits the induction of growth through the αβ T-cell receptor
- Reconstitution of T cell receptor zeta-mediated calcium mobilization in nonlymphoid cells.
- Signalling through SH2 and SH3 domains.
- Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation.
- Cellular immunity to HIV activated by CD4 fused to T cell or Fc receptor polypeptides.
- Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase.
- The zeta chain is associated with a tyrosine kinase and upon T-cell antigen receptor stimulation associates with ZAP-70, a 70-kDa tyrosine phosphoprotein.
- The cytoplasmic domain of the T cell receptor zeta chain is sufficient to couple to receptor-associated signal transduction pathways.
- Increase of the catalytic activity of phospholipase C-gamma 1 by tyrosine phosphorylation.
- Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation.
Cited by
- Transmembrane signaling by antigen receptors of B and T lymphocytes.
- Partial T cell signaling: Altered phospho-ζ and lack of zap70 recruitment in APL-induced T cell anergy
- Fyn, a Src family tyrosine kinase.
- Therapeutic targeting of Src-kinase Lyn in myeloid leukemic cell growth
- The T-Cell Receptor ζ Chain Contains Two Homologous Domains with Which Simian Immunodeficiency Virus Nef Interacts and Mediates Down-Modulation
- Positive and negative signaling in B lymphocytes.
- The signal transduction of motion and antigen recognition: factors affecting T cell function and differentiation.
- Development and function of thymocyte-selected CD4 T cells
- Characterization of Grb2-binding proteins in human platelets activated by Fc gamma RIIA cross-linking.
- Synthèse et évaluation pharmacologique d'imidazolidin-2-ones et d'analogues à potentialités immunosuppressives
- Signaling in Mast Cells
- Reconstitution of interactions between tyrosine kinases and the high affinity IgE receptor which are controlled by receptor clustering.
- Role of immunoreceptor tyrosine-based activation motif in signal transduction from antigen and Fc receptors.
- Activating and Inhibitory Mutations in Adjacent Tyrosines in the Kinase Domain of ZAP-70 (*)
- Enrichment of Lck in Lipid Rafts Regulates Colocalized Fyn Activation and the Initiation of Proximal Signals through TCRαβ1
- The Fates of Dendritic Cells and Antigen Regulate CD4+ T Cell Responses
- Fyn membrane localization is necessary to induce the constitutive tyrosine phosphorylation of Sam68 in the nucleus of T lymphocytes.
- Distinct Functions of the FcεR1 γ and β Subunits in the Control of FcεR1-mediated Tyrosine Kinase Activation and Signaling Responses in RBL-2H3 Mast Cells (*)
- Inefficient phospholipase C activation and reduced Lck expression characterize the signaling defect of umbilical cord T lymphocytes.
- Interaction of p72syk with the gamma and beta subunits of the high-affinity receptor for immunoglobulin E, Fc epsilon RI
Related papers
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