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Title: A common site of the Fc receptor gamma subunit interacts with the unrelated immunoreceptors FcalphaRI and FcepsilonRI.
Austin Authors: Wines, Bruce D;Trist, Halina M;Ramsland, Paul A ;Hogarth, P Mark
Affiliation: Helen Macpherson Smith Trust Inflammatory Disease Laboratory, The Macfarlane Burnet Institute for Medical Research and Public Health, Austin Health Campus, Heidelberg, Victoria 3084, Australia
Issue Date: 19-Apr-2006
Publication information: The Journal of Biological Chemistry 2006; 281(25): 17108-13
Abstract: The transmembrane (TM) region of the Fc receptor-gamma (FcRgamma) chain is responsible for the association of this ubiquitous signal transduction subunit with many immunoreceptor ligand binding chains, making FcRgamma 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 FcRgamma subunit, but otherwise the molecular basis for the FcRgamma subunit interactions is largely unknown. This study reports residues in the TM region of the FcRgamma subunit are important for association with the high affinity IgE receptor FcepsilonRI and a leukocyte receptor cluster member, the IgA receptor FcalphaRI. FcRgamma residue Leu-21 was essential for surface expression of FcepsilonRIalpha/gamma2 and Tyr-8, Leu-14, and Phe-15 contributed to expression. Likewise, detergent-stable FcRgamma association with FcalphaRI 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 FcRgamma dimer indicated these residues interacting with both FcalphaRI and FcepsilonRI are near the interface between the two FcRgamma TM helices. Furthermore, the FcRgamma residues interacting with FcalphaRI form a leucine zipper-like interface with mutagenesis confirming a complementary interface comprising FcalphaRI residues Leu-217, Leu-220, and Leu-224. The dependence of these two nonhomologous receptor interactions on FcRgamma 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 FcRgamma subunit.
Gov't Doc #: 16627486
DOI: 10.1074/jbc.M601640200
Journal: The Journal of biological chemistry
Type: Journal Article
Subjects: Amino Acid Sequence
Antigens, CD.chemistry
Antigens, CD3.chemistry
Cell Line
Models, Molecular
Molecular Conformation
Molecular Sequence Data
Protein Binding
Receptors, Fc.chemistry
Receptors, IgE.chemistry
Receptors, IgG.chemistry
Sequence Homology, Amino Acid
Appears in Collections:Journal articles

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