1999
Phosphatidylinositol 3-Phosphate Recognition by the FYVE Domain
Kutateladze T, Ogburn K, Watson W, de Beer T, Emr S, Burd C, Overduin M. Phosphatidylinositol 3-Phosphate Recognition by the FYVE Domain. Molecular Cell 1999, 3: 805-811. PMID: 10394369, DOI: 10.1016/s1097-2765(01)80013-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesConserved SequenceDimerizationHumansLiposomesMembrane ProteinsMolecular Sequence DataMolecular WeightMutationNuclear Magnetic Resonance, BiomolecularPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphatidylinositolsProtein BindingProtein FoldingProtein Structure, SecondarySolubilitySubstrate SpecificityVesicular Transport ProteinsZincZinc FingersConceptsFYVE domainEndosome autoantigen 1Membrane trafficking eventsHeteronuclear magnetic resonance spectroscopyZinc-binding motifSpecific amino acidsTrafficking eventsEndosome fusionCellular signalingAlpha-helixBeta hairpinAmino acidsPhosphoinositidePhosphatidylinositolMotifStructural featuresRing fingerDomainPtdlnsSignalingProteinHairpinHelixBroad rangeLipidsMolecular Dissection of Guanine Nucleotide Dissociation Inhibitor Function in Vivo Rab-INDEPENDENT BINDING TO MEMBRANES AND ROLE OF RAB RECYCLING FACTORS*
Luan P, Balch W, Emr S, Burd C. Molecular Dissection of Guanine Nucleotide Dissociation Inhibitor Function in Vivo Rab-INDEPENDENT BINDING TO MEMBRANES AND ROLE OF RAB RECYCLING FACTORS*. Journal Of Biological Chemistry 1999, 274: 14806-14817. PMID: 10329679, DOI: 10.1074/jbc.274.21.14806.Peer-Reviewed Original ResearchConceptsRecycling factorNucleotide Dissociation InhibitorFusion of vesiclesSite-directed mutagenesisAmino acid residuesRab deliveryDistinct RabsRab GTPasesRab proteinsRab-GDPDissociation inhibitorMembrane associationEssential proteinsMolecular dissectionEndocytic pathwayGDI functionAcid residuesRabCellular membranesDominant inhibitionMultiple effectorsRate of recyclingInhibitor functionProteinEndogenous poolVac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome
Peterson M, Burd C, Emr S. Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome. Current Biology 1999, 9: 159-s1. PMID: 10021387, DOI: 10.1016/s0960-9822(99)80071-2.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingCytoskeletal ProteinsEndosomesFungal ProteinsGolgi ApparatusGTP PhosphohydrolasesGTP-Binding ProteinsGuanine Nucleotide Dissociation InhibitorsGuanosine TriphosphateMacromolecular SubstancesMembrane ProteinsPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesProtein BindingQa-SNARE ProteinsRab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsConceptsVacuolar protein sorting (VPS) pathwayVesicle docking/fusionProtein sorting pathwaysDocking/fusionVacuolar protein precursorsMultivalent adaptor proteinLysosome-like vacuolePrevacuolar endosomeVPS genesVps34 phosphatidylinositolLate GolgiGTPase signalsRab GTPaseSorting pathwaysVesicle dockingEndosome transportVacuolar proteinAdaptor proteinEndosomal compartmentsVac1pProtein precursorGolgiTransport stepsVps21pVps45p
1998
Phosphatidylinositol(3)-Phosphate Signaling Mediated by Specific Binding to RING FYVE Domains
Burd C, Emr S. Phosphatidylinositol(3)-Phosphate Signaling Mediated by Specific Binding to RING FYVE Domains. Molecular Cell 1998, 2: 157-162. PMID: 9702203, DOI: 10.1016/s1097-2765(00)80125-2.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBiological TransportCell CompartmentationFungal ProteinsGenes, ReporterGreen Fluorescent ProteinsLiposomesLuminescent ProteinsLysosomesPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphorylationProtein BindingRecombinant Fusion ProteinsSaccharomyces cerevisiaeSignal TransductionVacuolesZinc FingersConceptsFYVE domain-containing proteinsLysosomal protein traffickingDomain-containing proteinsGFP reporter proteinDomain fusion proteinLipid-binding assaysReceptor signaling cascadesFYVE fingerFYVE domainMembrane traffickingProtein traffickingPhosphate signalingInositol ringProtein domainsReporter proteinRING domainDownstream effectorsEndocytic compartmentsSignaling cascadesMolecular linkFusion proteinIntracellular localizationVps34Important regulatorRecruit/
1997
A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast.
Burd C, Peterson M, Cowles C, Emr S. A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast. Molecular Biology Of The Cell 1997, 8: 1089-1104. PMID: 9201718, PMCID: PMC305716, DOI: 10.1091/mbc.8.6.1089.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesBiological TransportCell CompartmentationCytoskeletal ProteinsEndosomesFungal ProteinsGolgi ApparatusGTP-Binding ProteinsMacromolecular SubstancesMembrane FusionMembrane ProteinsProtein BindingQa-SNARE ProteinsRab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipVacuolesVesicular Transport ProteinsZincConceptsVacuolar protein sortingProtein sortingVPS pathwayEndosome transportSevere synthetic growth defectVacuolar protein sorting (VPS) genesVacuolar protein sorting (VPS) pathwaySynthetic growth defectsProtein sorting pathwaysZinc finger motifsRab family GTPaseCoiled-coil motifLocalization of proteinsSite-directed mutationsSDS-resistant complexesDominant negative mutationTsf phenotypeTsf mutationsFinger motifVesicle receptorsEndosome traffickingVacuole inheritanceVac1pVacuolar proteinTrans-Golgi