Chimeric receptors containing the FcεRI α and γ subunit domains were constructed, stably transfected into RBL-2H3 cells, and characterized for the biochemical events which are elicited upon receptor aggregation. Chimeric receptors containing the extracellular (EC) domain of the human FcεRIα subunit, or the EC domain of the p55 subunit of the interleukin-2 receptor were fused to the human FcεRIγ subunit transmembrane and cytoplasmic (CT) domains or only the CT domain. The chimeras generated included α/γ/γ, I/γ/γ, α/I/γ or I/I/γ. The results indicate that both the FcεRIα EC domain and the FcεRIα CT domain are essential for signalling.

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