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J. Biol. Chem., Vol. 279, Issue 25, 26339-26345, June 18, 2004

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Fc Receptor Chain Residues at the Interface of the Cytoplasmic and Transmembrane Domains Affect Association with FcRI, Surface Expression, and Function^*

Bruce D. Wines, Halina M. Trist, Renato C. Monteiro¶, Cees van Kooten||, and P. Mark Hogarth

From the Helen Macpherson Smith Trust Inflammatory Disease Laboratory, Austin Research Institute, Austin Repatriation Medical Centre, Studley Road, Heidelberg, Victoria, 3084, Australia, ^¶Institut National de la Santé et de la Recherche Médicale, E-0225, Bichat Medical School, 75870 Paris, France, and the ^||Department of Nephrology, Leiden University Medical Center, 2333ZA Leiden, The Netherlands

The assembly of multiple subunit immunoreceptors is dependent on transmembrane interactions. The Fc receptor (FcR-) chain is a ubiquitous immune receptor tyrosine-based activation motif-containing dimeric subunit, ₂, which in humans associates with both the activating members of the leukocyte receptor cluster, including the IgA receptor FcRI, and the classical Fc receptors, including the IgE receptor FcRI. This study identifies a new site in the transmembrane region of FcR- that affects receptor assembly and surface expression with FcRI but not with FcRI. The wild type complex, FcRI-₂WT, remains robustly associated in both Brij-96 and Thesit detergent conditions. However, mutation of either Tyr²⁵ or Cys²⁶ of FcR-, near the interface of the transmembrane and cytoplasmic regions, resulted in impaired FcR- association with FcRI. This association was disrupted in the presence of the detergent Brij-96 but was preserved in milder conditions using the detergent Thesit. Ligand-mediated cross-linking of the FcRI-₂Y25F mutant receptor resulted in diminished signal transduction, including an abnormal calcium response, compared with the FcRI-₂WT receptor. Furthermore, the FcRI-₂Y25F mutant receptor was expressed at the cell surface at 10% of that of the wild type, whereas the surface expression of FcRI-₂Y25F was not significantly different from the wild type. In contrast, although the FcRI-₂C26S mutant was also less stably associated, it was not reduced in surface expression or function. Thus, these TM residues of FcR- are important for association with FcRI and probably other activating LRC members but not with the classical FcR, FcRI.

Received for publication, April 2, 2004

^* This work was supported by National Health and Medical Research Council Grant 181627. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Austin Research Institute, Studley Road, Heidelberg, Vic 3084, Australia. Tel.: 613-9287-0684; Fax: 613-9287-0600; E-mail: b.wines{at}ari.unimelb.edu.au.

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