T-cell activation is a consequence of the clonotypic T-cell antigen receptor (TCR) binding to an antigen followed by signal transduction via the invariant subunits of the TCR/CD3 complex. γδ TCR cells are a small subset of T cells that populate both the epithelial and lymphoid tissues and have unique antigen specificity and function. However, the composition of invariant chains within the γδ TCR/CD3 complex has not been well characterized. Here we report that, unlike the majority of αβ T cells, γδ T cells isolated from spleen and intestinal epithelial tissue express high levels of the γ chain of the high-affinity receptor for IgE (FcεRIγ) as one invariant subunit of their TCR/CD3 complex. FcεRIγ exists as both a homodimer and a heterodimer associated with the TCRζ chain. Moreover, stimulation of the γδ TCR results in rapid tyrosine phosphorylation of FcεRIγ. Our results suggest that utilization of distinct receptor signaling components may enable the coupling of antigen stimulation to the activation of different signal transduction pathways in αβ and γδ T cells.
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - 1993|
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