Fluorescence Resonance Energy Transfer Imaging Reveals that Chemokine-Binding Modulates Heterodimers of CXCR4 and CCR5 Receptors 英文参考文献.docVIP

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Fluorescence Resonance Energy Transfer Imaging Reveals that Chemokine-Binding Modulates Heterodimers of CXCR4 and CCR5 Receptors 英文参考文献.doc

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Fluorescence Resonance Energy Transfer Imaging Reveals that Chemokine-Binding Modulates Heterodimers of CXCR4 and CCR5 Receptors 英文参考文献

FluorescenceResonanceEnergyTransferImaging RevealsthatChemokine-BindingModulates HeterodimersofCXCR4andCCR5Receptors NilgunIsik,DaleHereld¤,TianJin* Chemotaxis Signal Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Twinbrook II Facility, Rockville,Maryland,UnitedStatesofAmerica Abstract Background: Dimerization has emerged as an important feature of chemokine G-protein-coupled receptors. CXCR4 and CCR5 regulate leukocyte chemotaxis and also serve as a co-receptor for HIV entry. Both receptors are recruited to the immunological synapse during T-cell activation. However, it is not clear whether they form heterodimers and whether ligandbindingmodulatesthedimerformation. Methodology/Principal Findings:UsingasensitiveFluorescenceResonanceEnergyTransfer(FRET)imagingmethod,we investigatedtheformationofCCR5andCXCR4heterodimersontheplasmamembraneoflivecells.WefoundthatCCR5 andCXCR4existasconstitutiveheterodimersandligandsofCCR5andCXCR4promotedifferentconformationalchanges withinthesepreexistingheterodimers.LigandsofCCR5,incontrasttoaligandofCXCR4,inducedaclearincreaseinFRET efficiency, indicating that selective ligands promote and stabilize a distinct conformation of the heterodimers. We also foundthatmutationsatC-terminusofCCR5reduceditsabilitytoformheterodimerswithCXCR4.Inaddition,ligandsinduce differentconformationaltransitionsofheterodimersofCXCR4andCCR5orCCR5STA andCCR5D4 . Conclusions/Significance: Taken together, our data suggest a model in which CXCR4 and CCR5 spontaneously form heterodimersandligand-bindingtoCXCR4orCCR5causesdifferentconformationalchangesaffectingheterodimerization, indicatingthecomplexityofregulationofdimerization/functionofthesechemokinereceptorsbyligandbinding. Citation:IsikN,HereldD,JinT(2008)FluorescenceResonanceEnergyTransferImagingRevealsthatChemokine-BindingModulatesHeterodimersofCXCR4and CCR5Receptors.PLoSONE3(10):e3424.doi:10.1371/journal.pone.0003424 Edito