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Sequential Interactions of the TCR with Two Distinct Cytoplasmic Tyrosine Kinases
Abstract
The T cell antigen receptor (TCR) initiates signals by interacting with cytoplasmic protein tyrosine kinases (PTKs) through a 17-residue sequence motif [called the antigen recognition activation motif (ARAM)] that is contained in the TCRζ and CD3 chains. TCR stimulation induces the tyrosine phosphorylation of several cellular substrates, including the ARAMs. Lck kinase activity is required for phosphorylation of two conserved tyrosine residues in an ARAM. This phosphorylation leads to the recruitment of a second cytoplasmic PTK, ZAP-70, through both of the ZAP-70 Src homology 2 domains and its phosphorylation. Thus, TCR signal transduction is initiated by the sequential interaction of two PTKs with TCR ARAMs.
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Citations
Cited by
Protein modules and signalling networks
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Dimerization of cell surface receptors in signal transduction
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Self-citationRegulation of T Cell Receptor Signaling by Tyrosine Phosphatase SYP Association with CTLA-4
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Interaction of SHP‐2 SH2 domains with PD‐1 ITSM induces PD‐1 dimerization and SHP‐2 activation
Patsoukis, N., Duke-Cohan, J. S., Chaudhri, A., Aksoylar, H.-I., Wang, Q., Council, A., Berg, A., Freeman, G. J., & Boussiotis, V. A. (2020) · Communications Biology · doi:10.1038/s42003-020-0845-0 · Cited by 169
Differential Intrinsic Enzymatic Activity of Syk and Zap-70 Protein-tyrosine Kinases
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Self-citationSyk and ZAP-70 mediate recruitment of p56lck/CD4 to the activated T cell receptor/CD3/zeta complex.
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Self-citationT-cell receptor–induced phosphorylation of the ζ chain is efficiently promoted by ZAP-70 but not Syk
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Self-citationKing-Smith (1997) · doi:10.1002/(sici)1097-0169(1997)38:3<229::aid-cm2>3.0.co;2-0
Metadata
- Authors
- Iwashima, M., Irving, B. A., van Oers, N. S. C., Chan, A. C., & Weiss, A.
- Venue
- Science
- Published
- 1994-02-25
- Volume
- 263
- Issue
- 5150
- Pages
- 1136-1139
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1983960385
- Cited by
- 714
- References
- 0
- FWCI
- 32.56
- Type
- journal article
- Language
- en
- Open access
- closed
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