Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/10142
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dc.contributor.authorWines, Bruce Den
dc.contributor.authorTrist, Halina Men
dc.contributor.authorRamsland, Paul Aen
dc.contributor.authorHogarth, P Marken
dc.date.accessioned2015-05-15T23:29:57Z
dc.date.available2015-05-15T23:29:57Z
dc.date.issued2006-04-19en
dc.identifier.citationThe Journal of Biological Chemistry 2006; 281(25): 17108-13en
dc.identifier.govdoc16627486en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/10142en
dc.description.abstractThe 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.en
dc.language.isoenen
dc.subject.otherAmino Acid Sequenceen
dc.subject.otherAnimalsen
dc.subject.otherAntigens, CD.chemistryen
dc.subject.otherAntigens, CD3.chemistryen
dc.subject.otherCell Lineen
dc.subject.otherDimerizationen
dc.subject.otherMiceen
dc.subject.otherModels, Molecularen
dc.subject.otherMolecular Conformationen
dc.subject.otherMolecular Sequence Dataen
dc.subject.otherProtein Bindingen
dc.subject.otherReceptors, Fc.chemistryen
dc.subject.otherReceptors, IgE.chemistryen
dc.subject.otherReceptors, IgG.chemistryen
dc.subject.otherSequence Homology, Amino Aciden
dc.titleA common site of the Fc receptor gamma subunit interacts with the unrelated immunoreceptors FcalphaRI and FcepsilonRI.en
dc.typeJournal Articleen
dc.identifier.journaltitleThe Journal of biological chemistryen
dc.identifier.affiliationHelen Macpherson Smith Trust Inflammatory Disease Laboratory, The Macfarlane Burnet Institute for Medical Research and Public Health, Austin Health Campus, Heidelberg, Victoria 3084, Australiaen
dc.identifier.doi10.1074/jbc.M601640200en
dc.description.pages17108-13en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/16627486en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
crisitem.author.deptSurgery (University of Melbourne)-
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