FYVE-Dependent Endosomal Targeting of an Arrestin-Related Protein in Amoeba 英文参考文献.docVIP

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FYVE-Dependent Endosomal Targeting of an Arrestin-Related Protein in Amoeba 英文参考文献.doc

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FYVE-Dependent Endosomal Targeting of an Arrestin-Related Protein in Amoeba 英文参考文献

FYVE-DependentEndosomalTargetingofanArrestin- RelatedProteininAmoeba DorianGuetta1,2,3,KarineLangou1¤,DidierGrunwald3,4,5,Ge′rardKlein1,2,3,LaurenceAubry1,2,3 * 1CEA, DSV, iRTSV, Laboratoire de Biochimie et Biophysique des Syste`mes Inte′gre′s, Grenoble, France, 2LBBSI, UMR5092 CNRS, Grenoble, France, 3Universite′ Joseph Fourier,Grenoble,France,4CEA,DSV,iRTSV,Lab.TransductionduSignal,Grenoble,France,5LTS,EMI104INSERM,Grenoble,France Abstract Background:Visualandb-arrestinsarescaffoldingproteinsinvolvedintheregulationofreceptor-dependentintracellular signaling and their trafficking. The arrestin superfamilly includes several arrestin domain-containing proteins and the structurallyrelatedproteinVps26.InDictyosteliumdiscoideum,thearrestin-domaincontainingproteinsformafamilyofsix members, namely AdcA to -F. In contrast to canonical arrestins, Dictyostelium Adc proteins show a more complex architecture,astheypossess,inadditiontothearrestincore,otherdomains,suchasC2,FYVE,LIM,MITandSAM,which potentiallymediateselectiveinteractionswitheitherlipidsorproteins. MethodologyandPrincipalFindings:AdetailedanalysisofAdcAhasbeenperformed.AdcAextendsonbothsidesofthe arrestin core, in particular by a FYVE domain which mediates selective interactions with PI(3)P, as disclosed by intrinsic fluorescence measurements and lipid overlay assays. Localization studies showed an enrichment of tagged- and endogenousAdcAontherimofearlymacropinosomesandphagosomes.Thisvesiculardistributionreliesonafunctional FYVE domain. Our dataalso show that the arrestin core binds the ADP-ribosylation factor ArfA, the uniqueamoebal Arf member,initsGDP-boundconformation. Significance:Thisworkdescribesoneofthe6arrestindomain-containingproteinsofDictyostelium,anovelandatypical member of the arrestin clan. It provides the basis for a better understanding of arrestin-related protein involvement in traffickingprocessesandforfurtherstudiesontheexpandingrolesofarrestinsineukaryotes. Citation: Guetta D, Langou K, Grun