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J. Biol. Chem., Vol. 281, Issue 25, 17108-17113, June 23, 2006

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A Common Site of the Fc Receptor Subunit Interacts with the Unrelated Immunoreceptors FcRI and FcRI^*

From the Helen Macpherson Smith Trust Inflammatory Disease Laboratory, The Macfarlane Burnet Institute for Medical Research and Public Health, Austin Health Campus, Heidelberg, Victoria 3084, Australia

The transmembrane (TM) region of the Fc receptor- (FcR) chain is responsible for the association of this ubiquitous signal transduction subunit with many immunoreceptor ligand binding chains, making FcR key to a number of leukocyte activities in immunity and disease. Some receptors contain a TM arginine residue that interacts with Asp-11 of the FcR subunit, but otherwise the molecular basis for the FcR subunit interactions is largely unknown. This study reports residues in the TM region of the FcR subunit are important for association with the high affinity IgE receptor FcRI and a leukocyte receptor cluster member, the IgA receptor FcRI. FcR residue Leu-21 was essential for surface expression of FcRI/₂ and Tyr-8, Leu-14, and Phe-15 contributed to expression. Likewise, detergent-stable FcR association with FcRI was also dependent on Leu-14 and Leu-21 and in addition required residues Tyr-17, Tyr-25, and Cys-26. Modeling the TM regions of the FcR dimer indicated these residues interacting with both FcRI and FcRI are near the interface between the two FcR TM helices. Furthermore, the FcR residues interacting with FcRI form a leucine zipper-like interface with mutagenesis confirming a complementary interface comprising FcRI residues Leu-217, Leu-220, and Leu-224. The dependence of these two nonhomologous receptor interactions on FcR Leu-14 and Leu-21 suggests that all the associated Fc receptors and the activating leukocyte receptor cluster members interact with this one site. Taken together these data provide a molecular basis for understanding how disparate receptor families assemble with the FcR subunit.

Received for publication, February 21, 2006 , and in revised form, April 19, 2006.

^* This work was supported by Grants 181627/315525 from the National Health and Medical Research Council. 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.

¹ To whom correspondence should be addressed: The Macfarlane Burnet Institute for Medical Research and Public Health, Austin Health Campus, Studley Rd., Heidelberg, Victoria 3084, Australia. Tel.: 613-9287-0644; Fax: 613-9287-0600; E-mail: b.wines{at}ari.unimelb.edu.au.

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