2016
Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells
Rauch L, Hennings K, Trasak C, Röder A, Schröder B, Koch-Nolte F, Rivera-Molina F, Toomre D, Aepfelbacher M. Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells. Journal Of Cell Science 2016, 129: 2937-2949. PMID: 27311480, PMCID: PMC5004874, DOI: 10.1242/jcs.186213.Peer-Reviewed Original ResearchConceptsEndocytic vesiclesActin polymerizationEndothelial cell invasionExocyst complexPhagocytic cupsPhagocytic cup-like structuresCell invasionPhagocytic cup closureArp2/3 complexN-WASPCup closureCup-like structuresCdc42GAPCdc42Human endothelial cellsCell functionVesiclesAnalogous mechanismInvasionEndothelial cellsExocystComplexesEndosomes
2012
The Legionella pneumophila Effector DrrA Is Sufficient to Stimulate SNARE-Dependent Membrane Fusion
Arasaki K, Toomre DK, Roy CR. The Legionella pneumophila Effector DrrA Is Sufficient to Stimulate SNARE-Dependent Membrane Fusion. Cell Host & Microbe 2012, 11: 46-57. PMID: 22264512, PMCID: PMC3266541, DOI: 10.1016/j.chom.2011.11.009.Peer-Reviewed Original ResearchConceptsMembrane transport pathwaysEndoplasmic reticulumSyntaxin proteinsFusion of ERMembrane fusionSNARE-dependent membrane fusionBacterial pathogen Legionella pneumophilaPathogen-containing vacuolesSNARE protein Sec22bIntracellular bacterial pathogen Legionella pneumophilaPathogen Legionella pneumophilaFusion of vesiclesRab1 activationNoncanonical pairingTransport pathwaysRab1 GTPasePlasma membraneVesicle fusionOrganellesDrrASec22bVesiclesLegionella pneumophilaProteinVacuoles
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 pathogensVectorial insertion of apical and basolateral membrane proteins in polarized epithelial cells revealed by quantitative 3D live cell imaging
Hua W, Sheff D, Toomre D, Mellman I. Vectorial insertion of apical and basolateral membrane proteins in polarized epithelial cells revealed by quantitative 3D live cell imaging. Journal Of Cell Biology 2006, 172: 1035-1044. PMID: 16567501, PMCID: PMC2063761, DOI: 10.1083/jcb.200512012.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCell LineCell MembraneCell PolarityDogsEndocytosisEpithelial CellsGlycoproteinsGlycosylphosphatidylinositolsGreen Fluorescent ProteinsKineticsLaser Scanning CytometryLuminescent ProteinsMembrane GlycoproteinsMembrane ProteinsNeural Cell Adhesion MoleculesProtein TransportRecombinant Fusion ProteinsTemperatureTrans-Golgi NetworkTransfectionTransport VesiclesViral Envelope ProteinsConceptsBasolateral membrane proteinsLive-cell imagingMembrane proteinsThree-dimensional live cell imagingGlycosylphosphatidylinositol-anchored proteinsVesicular stomatitis virus glycoproteinApical surfaceMadin-Darby canine kidney cellsCell imagingFilter-grown Madin-Darby canine kidney (MDCK) cellsEpithelial cellsBasolateral proteinsCanine kidney cellsTransport intermediatesVesicle dockingSecretory pathwayPlasma membraneVectorial insertionMembrane componentsJunctional complexesProteinRespective membranesKidney cellsVirus glycoproteinPathway
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