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Fidelity of T Cell Activation Through Multistep T Cell Receptor ζ Phosphorylation
Abstract
The T cell receptor (TCR) αβ heterodimer interacts with its ligands with high specificity, but surprisingly low affinity. The role of the ζ component of the murine TCR in contributing to the fidelity of antigen recognition was examined. With sequence-specific phosphotyrosine antibodies, it was found that ζ undergoes a series of ordered phosphorylation events upon TCR engagement. Completion of phosphorylation steps is dependent on the nature of the TCR ligand. Thus, the phosphorylation steps establish thresholds for T cell activation. This study documents the sophisticated molecular events that follow the engagement of a low-affinity receptor.
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Metadata
- Authors
- Kersh, E. N., Shaw, A. S., & Allen, P. M.
- Venue
- Science
- Published
- 1998-07-24
- Volume
- 281
- Issue
- 5376
- Pages
- 572-575
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1980754944
- Cited by
- 341
- References
- 0
- FWCI
- 14.93
- Type
- journal article
- Language
- en
- Open access
- closed
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