2017
Differential requirement for N‐ethylmaleimide‐sensitive factor in endosomal trafficking of transferrin receptor from anterograde trafficking of vesicular stomatitis virus glycoprotein G
Fan J, Zhou X, Wang Y, Kuang C, Sun Y, Liu X, Toomre D, Xu Y. Differential requirement for N‐ethylmaleimide‐sensitive factor in endosomal trafficking of transferrin receptor from anterograde trafficking of vesicular stomatitis virus glycoprotein G. FEBS Letters 2017, 591: 273-281. PMID: 27995606, DOI: 10.1002/1873-3468.12532.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoprotein GGolgi structureDifferential requirementN-ethylmaleimide-sensitive factorConstitutive trafficking pathwayTrafficking pathwaysGlycoprotein GTransferrin endocytosisEndosomal traffickingAnterograde traffickingGolgi fragmentationMammalian cellsVesicular transportDifferent vesiclesHeLa cellsReceptor exocytosisTraffickingTransferrin receptorFusion factorKnockdownCell viabilityCentral rolePathwayCrucial roleCells
2011
Splice isoform estrogen receptors as integral transmembrane proteins
Kim KH, Toomre D, Bender JR. Splice isoform estrogen receptors as integral transmembrane proteins. Molecular Biology Of The Cell 2011, 22: 4415-4423. PMID: 21937726, PMCID: PMC3216666, DOI: 10.1091/mbc.e11-05-0416.Peer-Reviewed Original ResearchConceptsSplice isoformsTotal internal reflection fluorescence microscopySteroid hormone receptorsIntegral transmembrane proteinN-terminal ectodomainReflection fluorescence microscopyHormone receptorsTransmembrane proteinPlasma membraneProtein structureHuman endothelial cellsLigand engagementPotential novel therapeutic targetER46Fluorescence microscopyNovel therapeutic targetEcliptic pHluorinActivation signalsEndothelial nitric oxide synthase activationEstrogen receptor αENOS activationReceptor αIsoformsTherapeutic targetNitric oxide synthase activation
2007
A Role of the Lowe Syndrome Protein OCRL in Early Steps of the Endocytic Pathway
Erdmann KS, Mao Y, McCrea HJ, Zoncu R, Lee S, Paradise S, Modregger J, Biemesderfer D, Toomre D, De Camilli P. A Role of the Lowe Syndrome Protein OCRL in Early Steps of the Endocytic Pathway. Developmental Cell 2007, 13: 377-390. PMID: 17765681, PMCID: PMC2025683, DOI: 10.1016/j.devcel.2007.08.004.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCarrier ProteinsCell LineChlorocebus aethiopsClathrin-Coated VesiclesCOS CellsCrystallography, X-RayEndocytosisEndosomesGlutathione TransferaseGreen Fluorescent ProteinsHumansKidneyModels, BiologicalModels, MolecularMolecular Sequence DataMutationPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositolsPhosphoric Monoester HydrolasesPhosphorylationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsSequence Homology, Amino AcidTime FactorsConceptsEndocytic pathwayLike domainEndocytic clathrin-coated pitsLowe syndrome protein OCRLRole of OCRLEarly endocytic pathwayClathrin-coated pitsPeripheral early endosomesPhosphatase domainMembrane traffickingEarly endosomesGrowth factor receptorProtein networkClathrin boxOCRLDisease mutationsCell surfaceEarly stepsLowe syndromeFactor receptorRenal Fanconi syndromeDisease mechanismsMembrane interfaceAPPL1Predominant localization
2006
The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor
Murata T, Delprato A, Ingmundson A, Toomre DK, Lambright DG, Roy CR. The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor. Nature Cell Biology 2006, 8: 971-977. PMID: 16906144, DOI: 10.1038/ncb1463.Peer-Reviewed Original ResearchConceptsGuanine nucleotide exchange factorsNucleotide exchange factorsType IV secretion apparatusIntracellular pathogen Legionella pneumophilaHost cellsEndoplasmic reticulum-derived vesiclesDot/IcmPathogen Legionella pneumophilaL. pneumophila mutantsRab1 recruitmentSubstrate proteinsRab familyExchange factorGTPase Rab1Secretion apparatusVesicular transportBacterial proteinsGolgi apparatusVisual screenEndoplasmic reticulumRab1Membrane transportSpecific membersDrrAIntracellular pathogens
2002
Selective Delivery of Secretory Cargo in Golgi‐Derived Carriers of Nonepithelial Cells
Rustom A, Bajohrs M, Kaether C, Keller P, Toomre D, Corbeil D, Gerdes H. Selective Delivery of Secretory Cargo in Golgi‐Derived Carriers of Nonepithelial Cells. Traffic 2002, 3: 279-288. PMID: 11929609, DOI: 10.1034/j.1600-0854.2002.030405.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsBiological TransportCell LineChlorocebus aethiopsChromograninsDogsDrug Delivery SystemsElectroporationEpithelial CellsGene DeletionGolgi ApparatusGreen Fluorescent ProteinsHumansImmunohistochemistryLuminescent ProteinsMicroscopy, ElectronMicroscopy, FluorescenceMutationPlasmidsRecombinant Fusion ProteinsRecombinant ProteinsTransfectionVero Cells