2024
Bridge-like lipid transfer protein family member 2 suppresses ciliogenesis
Parolek J, Burd C. Bridge-like lipid transfer protein family member 2 suppresses ciliogenesis. Molecular Biology Of The Cell 2024, 35: br11. PMID: 38536441, PMCID: PMC11151097, DOI: 10.1091/mbc.e24-02-0065.Peer-Reviewed Original ResearchConceptsLipid transfer proteinsFamily member 2RPE-1 cellsSuppressed ciliogenesisTubular endosomal networkMembrane contact sitesNegative regulator of ciliogenesisRegulator of ciliogenesisDrosophila melanogaster</i>Evolutionary conserved proteinMember 2Primary cilium biogenesisRPE-1Endosomal networkGenetic interactionsTubular endosomesCilium biogenesisProtein familyStructure predictionContact sitesEndoplasmic reticulumDomain-containingPreweaning lethalityNegative regulatorCiliogenesis
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
2000
Determinants of NPC1 Expression and Action: Key Promoter Regions, Posttranscriptional Control, and the Importance of a “Cysteine-Rich” Loop
Watari H, Blanchette-Mackie E, Dwyer N, Watari M, Burd C, Patel S, Pentchev P, Strauss J. Determinants of NPC1 Expression and Action: Key Promoter Regions, Posttranscriptional Control, and the Importance of a “Cysteine-Rich” Loop. Experimental Cell Research 2000, 259: 247-256. PMID: 10942596, DOI: 10.1006/excr.2000.4976.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarcinoma, HepatocellularCarrier ProteinsCHO CellsCricetinaeCysteineGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsLysosomesMembrane GlycoproteinsNiemann-Pick C1 ProteinNiemann-Pick DiseasesPlasmidsProgesteronePromoter Regions, GeneticProtein Structure, TertiaryProteinsRNA Processing, Post-TranscriptionalRNA, MessengerTransfectionTumor Cells, CulturedZincConceptsNiemann-Pick type C diseaseCholesterol trafficking defectType C diseaseC diseaseNPC1 expressionTrafficking defectsNPC1 genePromoter activityMajor transcription initiation siteBase pairsLate endosomal compartmentsTranscription initiation siteTranscription start siteI1061T mutationKey promoter regionChinese hamster cell lineProgesterone-treated cellsHamster cell linesNPC1 mRNA levelsProgesterone-induced increaseZinc-binding activityProtein synthesis inhibitorCT60 cellsThreonine residuesPosttranscriptional regulation
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 trafficking
1997
Novel 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
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