PMID: 9551968Apr 29, 1998Paper

Regulation of TCR signal transduction in murine thymocytes by multiple TCR zeta-chain signaling motifs

The Journal of Immunology : Official Journal of the American Association of Immunologists
N S van OersA Weiss

Abstract

The alphabeta TCR is a multimeric protein complex comprising ligand-binding and signal-transducing subunits. The signal transduction processes are mediated by the immunoreceptor tyrosine-based activation motifs (ITAMs), and up to 10 ITAMs are present within a single TCR complex. This multiplicity may allow for signal amplification and/or the formation of qualitatively distinct intracellular signals. Notably, the TCR-zeta subunit contains three ITAMs, and exists as a disulfide-linked homodimer in the TCR complex. In normal murine thymocytes and peripheral T cells, a proportion of TCR-zeta molecules is constitutively tyrosine phosphorylated and associated with the ZAP-70 protein tyrosine kinase. We examined the contribution of the different TCR-zeta ITAMs in regulating the constitutive phosphorylation of the TCR-zeta subunit in thymocytes by analyzing TCR-zeta-deficient mice that had been reconstituted with either full-length or single ITAM-containing TCR-zeta subunits. We report in this work that in the absence of a full-length TCR-zeta subunit, there is no apparent constitutive phosphorylation of the remaining TCR/CD3 ITAMs. Following TCR ligation, all of the CD3 ITAMs become inducibly phosphorylated and associate with the ZAP-...Continue Reading

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