Characterization of the family of dimers associated with Fc receptors (Fc∈RI and FcγRIII)

Odile Letourneur, Ian C S Kennedy, Anna T. Brini, John R. Ortaldo, John J. O'Shea, Jean Pierre Kinet

Research output: Contribution to journalArticlepeer-review


The receptor for IgE (Fc∈RI) is a multimeric complex containing one α chain, one β chain with four transmembrane domains and one homodimer of disulfide-linked γ-chains. The Fc∈RI γ-chains form additional disulfide-linked dimers with the homologous ζ- and η-chains, as part of the TCR complex. The low affinity receptor for IgG (FcγRIII)2 on NK cells is also associated with ζ-chains. Here we show that the γ-chain is expressed in NK cells both as a group of heterogenous γγ homodimers and also as a heterodimer bound to ζ. FcγRIIIA is associated with three types of dimers ζζ, γζ, and notably γγ as well. In fact, γγ appears to be the predominant species associating with FCγRIIIA. The surface expressed Fc∈RI also associates with the same group of heterogenous γγ homodimers. We also show that there is no C-terminal posttranslational cleavage of γ occurring before its insertion into the plasma membrane as previously suggested. Thus, like the TCR, FcγRIIIA may form a variety of receptor isoforms, though at present we do not understand the functional implications of these structures.

Original languageEnglish
Pages (from-to)2652-2656
Number of pages5
JournalJournal of Immunology
Issue number8
Publication statusPublished - Oct 15 1991

ASJC Scopus subject areas

  • Immunology


Dive into the research topics of 'Characterization of the family of dimers associated with Fc receptors (Fc∈RI and FcγRIII)'. Together they form a unique fingerprint.

Cite this