FcR chain has previously been shown to interact with the TCR-CD3 complex, the IgE Fc receptor I (FcRI), and the class I and IIIA IgG receptors (FcRI and FcRIIIa). Here, we demonstrate that the Fc receptor chain associates with FcR in transfected IIA1.6 B lymphocytes. FcR could be expressed at the surface of IIA1.6 B cells by itself, but was devoid of signaling capacity. Upon co-expression of FcR chain, a physical interaction with FcR could be demonstrated. This association proved crucial for the triggering of both proximal (intracellular calcium increase and tyrosine phosphorylation), as well as distal (IL-2 release), signal transduction responses. We next tested the hypothesis that a positively charged arginine residue (Arg) within the transmembrane domain of FcR promotes association with FcR chain. We therefore constructed FcR molecules where Arg was mutated to either a positively charged histidine, a negatively charged aspartic acid, or an uncharged leucine. A functional association between FcR and FcR chain was observed only with a positively charged residue (Arg or His) present within the FcR transmembrane domain. These data show that transmembrane signal transduction by the FcR is mediated via FcR chain, and that FcR requires a positively charged residue within the transmembrane domain to promote functional association.

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