2018
Lipid trafficking by yeast Snx4 family SNX-BAR proteins promotes autophagy and vacuole membrane fusion
Ma M, Kumar S, Purushothaman L, Babst M, Ungermann C, Chi RJ, Burd CG. Lipid trafficking by yeast Snx4 family SNX-BAR proteins promotes autophagy and vacuole membrane fusion. Molecular Biology Of The Cell 2018, 29: 2190-2200. PMID: 29949447, PMCID: PMC6249802, DOI: 10.1091/mbc.e17-12-0743.Peer-Reviewed Original ResearchConceptsVacuole fusionAutophagy pathwaySNX-BAR proteinsCore autophagy machinerySelective autophagy pathwaysHomotypic vacuole fusionVacuole membrane fusionPhosphatidylserine-containing membranesRetrograde transport carriersTurnover of macromoleculesAutophagy intermediatesGlycerophospholipid homeostasisNonselective autophagyBAR domainEndosomal sortingAutophagy machineryFusion competenceLipid traffickingPhosphatidylserine-rich membranesCoat proteinMembrane fusionVacuole membranePhosphatidylethanolamine biosynthesisYeast cellsPhosphatidylethanolamine synthesis
2001
FYVE Domain Targets Pib1p Ubiquitin Ligase to Endosome and Vacuolar Membranes*
Shin M, Ogburn K, Varban O, Gilbert P, Burd C. FYVE Domain Targets Pib1p Ubiquitin Ligase to Endosome and Vacuolar Membranes*. Journal Of Biological Chemistry 2001, 276: 41388-41393. PMID: 11526110, DOI: 10.1074/jbc.m105665200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceEndosomesGreen Fluorescent ProteinsIntracellular MembranesLigasesLuminescent ProteinsMolecular Sequence DataPhosphatidylinositol 3-KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesVacuolesConceptsPI3K productsVacuolar membraneFYVE domainUbiquitin ligaseK productRING-type ubiquitin ligaseUbiquitin ligase activityFYVE fingerFinger motifEukaryotic cellsYeast SaccharomycesCellular proteinsRING domainLigase activityDeletional analysisFusion proteinStructural domainsHistidine residuesPrimary structurePI3KFluorescence microscopyProteinLigaseBindsMembrane
1999
Molecular 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 ResearchMeSH KeywordsBiological TransportCell MembraneGTP-Binding ProteinsGuanine Nucleotide Dissociation InhibitorsMutagenesisMutationProtein BindingSaccharomyces cerevisiaeConceptsRecycling 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
Novel pathways, membrane coats and PI kinase regulation in yeast lysosomal trafficking
Burd C, Babst M, Emr S. Novel pathways, membrane coats and PI kinase regulation in yeast lysosomal trafficking. Seminars In Cell And Developmental Biology 1998, 9: 527-533. PMID: 9835640, DOI: 10.1006/scdb.1998.0255.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAlkaline PhosphataseBiological TransportCarboxypeptidasesCarrier ProteinsCathepsin ACell MembraneCoated Pits, Cell-MembraneFungal ProteinsIntracellular MembranesLysosomesMembrane ProteinsModels, BiologicalMonomeric Clathrin Assembly ProteinsPhosphatidylinositol 3-KinasesSaccharomyces cerevisiaeVacuolesConceptsSorting pathwaysVesicle docking/fusionAdaptor protein-3 complexProtein sorting signalsDocking/fusionPhosphorylation-dependent ubiquitinationVesicle coat proteinsYeast Saccharomyces cerevisiaeMembrane fusion reactionGolgi recyclingEndocytic cargoFYVE domainSorting signalsKinase regulationEukaryotic cellsImportant mechanistic insightsMembrane transport reactionsRecycling pathwaySaccharomyces cerevisiaeBiosynthetic pathwayCoat proteinRecognition motifMembrane coatMolecular mechanismsLysosomal traffickingAcidic Di-leucine Motif Essential for AP-3–dependent Sorting and Restriction of the Functional Specificity of the Vam3p Vacuolar t-SNARE
Darsow T, Burd C, Emr S. Acidic Di-leucine Motif Essential for AP-3–dependent Sorting and Restriction of the Functional Specificity of the Vam3p Vacuolar t-SNARE. Journal Of Cell Biology 1998, 142: 913-922. PMID: 9722605, PMCID: PMC2132875, DOI: 10.1083/jcb.142.4.913.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAlkaline PhosphataseBiological TransportCarboxypeptidasesCathepsin AEndosomesFungal ProteinsLeucineMembrane ProteinsMonomeric Clathrin Assembly ProteinsMutationNerve Tissue ProteinsPhosphoproteinsQa-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsVesicle-Associated Membrane Protein 3Vesicular Transport ProteinsConceptsPre-vacuolar endosomesVacuolar proteinCarboxypeptidase Y pathwayDi-leucine sequenceOrganelle-specific functionsT-SNARE proteinsAP-3 functionAlkaline phosphatase pathwayYeast Saccharomyces cerevisiaeTransport of proteinsSNAP receptor (SNARE) proteinsT-SNAREsGenetic screenCPY pathwayLeucine signalDelivery of cargoPhosphatase pathwaysRegulated transportMammalian systemsPep12pVam3pSaccharomyces cerevisiaeAccessory proteinsAcid sequenceALP pathwayPhosphatidylinositol(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-GolgiNovel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component
Cowles C, Snyder W, Burd C, Emr S. Novel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component. The EMBO Journal 1997, 16: 2769-2782. PMID: 9184222, PMCID: PMC1169886, DOI: 10.1093/emboj/16.10.2769.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAmino Acid SequenceBiological TransportCarboxypeptidasesCarrier ProteinsCathepsin ACell CompartmentationFungal ProteinsGolgi ApparatusMembrane ProteinsModels, BiologicalMolecular Sequence DataNuclear ProteinsQa-SNARE ProteinsRecombinant Fusion ProteinsRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesVesicular Transport ProteinsConceptsVacuolar protein sorting (vps) mutantsSoluble vacuolar hydrolasesVacuolar membrane proteinSoluble vacuolar proteinsDomain-swapping experimentsNon-permissive conditionsNon-permissive temperatureCytoplasmic tail domainVacuolar deliveryT-SNAREsNovel GolgiTransport intermediatesSorting signalsVacuolar hydrolasesVesicle recognitionVacuolar proteinDouble mutantAmino acid portionVacuolar localizationMembrane proteinsTail domainDelivery pathwayPlasma membraneSelective packagingAlkaline phosphatase
1996
A Yeast Protein Related to a Mammalian Ras-Binding Protein, Vps9p, Is Required for Localization of Vacuolar Proteins
Burd C, Mustol P, Schu P, Emr S. A Yeast Protein Related to a Mammalian Ras-Binding Protein, Vps9p, Is Required for Localization of Vacuolar Proteins. Molecular And Cellular Biology 1996, 16: 2369-2377. PMID: 8628304, PMCID: PMC231225, DOI: 10.1128/mcb.16.5.2369.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAmino Acid SequenceAnimalsCarrier ProteinsCloning, MolecularFungal ProteinsGenes, FungalGenetic Complementation TestGuanine Nucleotide Exchange FactorsHumansMammalsMolecular Sequence DataMutagenesisPolymerase Chain ReactionRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTemperatureVacuolesVesicular Transport ProteinsConceptsVacuolar protein sortingProtein sortingVacuolar proteinVPS pathwayVacuolar protein sorting (VPS) genesTemperature-sensitive growth defectTemperature-conditional alleleVacuolar protein precursorsFamily of proteinsSecretion of proteinsRab GTPaseRA-binding proteinsTransport vesiclesYeast proteinsHomology domainYeast SaccharomycesGrowth defectHuman proteinsVps9pDNA sequencesGene productsCytosolic proteinsNonpermissive temperatureCarboxypeptidase YIntracellular transport
1994
The mRNA Poly(A)-Binding Protein: Localization, Abundance, and RNA-Binding Specificity
Görlach M, Burd C, Dreyfuss G. The mRNA Poly(A)-Binding Protein: Localization, Abundance, and RNA-Binding Specificity. Experimental Cell Research 1994, 211: 400-407. PMID: 7908267, DOI: 10.1006/excr.1994.1104.Peer-Reviewed Original ResearchConceptsHuman PABPRNA binding specificityQuantitative immunoblotting experimentsMost eukaryotic mRNAsRNA-binding propertiesTranslation of mRNAsConfocal immunofluorescence microscopySelection/amplificationEukaryotic mRNAsOligonucleotide poolRNA sequencesRich sequencesCellular localizationBinding proteinHeLa cellsImmunofluorescence microscopyImmunoblotting experimentsLow turnover rateLow affinityPABPProteinAbundanceMRNAIntracellular concentrationTurnover rate
1991
The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities.
Burd C, Matunis E, Dreyfuss G. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Molecular And Cellular Biology 1991, 11: 3419-3424. PMID: 1675426, PMCID: PMC361068, DOI: 10.1128/mcb.11.7.3419.Peer-Reviewed Original Research