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Alteration of the FcRIIa Dimer Interface Affects Receptor Signaling but Not Ligand Binding¹

Maree S. Powell^*, Nadine C. Barnes^*, Tessa M. Bradford^*, Ian F. Musgrave, Bruce D. Wines^*, John C. Cambier and P. Mark Hogarth^2,*

^* The Macfarlane Burnet Institute for Medical Research and Public Health Limited, Austin Health, Heidelberg, Victoria, Australia; Department of Clinical and Experimental Pharmacology, Adelaide University, Adelaide, Australia; and Integrated Department of Immunology, University of Colorado Health Sciences Centre, and National Jewish Medical Center, Denver, CO 80206

The aggregation of cell surface FcRs by immune complexes induces a number of important Ab-dependent effector functions. However, despite numerous studies that examine receptor function, very little is known about the molecular organization of these receptors within the cell. In this study, protein complementation, mutagenesis, and ligand binding analyses demonstrate that human FcRIIa is present as a noncovalent dimer form. Protein complementation studies found that FcRIIa molecules are closely associated. Mutagenesis of the dimer interface, as identified by crystallographic analyses, did not affect ligand binding yet caused significant alteration to the magnitude and kinetics of receptor phosphorylation. The data suggest that the ligand binding and the dimer interface are distinct regions within the receptor, and noncovalent dimerization of FcRIIa may be an essential feature of the FcRIIa signaling cascade.

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