2019
Acylation – A New Means to Control Traffic Through the Golgi
Ernst AM, Toomre D, Bogan JS. Acylation – A New Means to Control Traffic Through the Golgi. Frontiers In Cell And Developmental Biology 2019, 7: 109. PMID: 31245373, PMCID: PMC6582194, DOI: 10.3389/fcell.2019.00109.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsDiverse protein clientsSorting of proteinsIntegral membrane proteinsProtein clientsS-acylationGolgi networkProtein adaptersMembrane proteinsAnterograde fluxLipid modificationGolgi cisternaeGolgiLipid acylationNeurodegenerative diseasesHuman physiologyProteinPotential relevanceOrganellesRecent dataRapid trafficAcylationCisternaePhysiologyCargoMechanism
2018
Seeing the long tail: A novel green fluorescent protein, SiriusGFP, for ultra long timelapse imaging
Zhong S, Rivera-Molina F, Rivetta A, Toomre D, Santos-Sacchi J, Navaratnam D. Seeing the long tail: A novel green fluorescent protein, SiriusGFP, for ultra long timelapse imaging. Journal Of Neuroscience Methods 2018, 313: 68-76. PMID: 30578868, PMCID: PMC9431725, DOI: 10.1016/j.jneumeth.2018.12.008.Peer-Reviewed Original ResearchConceptsSuper-resolution structured illumination microscopyFluorescent proteinNovel green fluorescent proteinGreen fluorescent proteinMembrane proteinsPhotostable variantsCell biologyC-terminusStructured illumination microscopyEGFPProteinConfocal imagingSIM imagingCombination of novelIllumination microscopyKey mutationsKnown mutationsOmp25High intensity excitationMutationsLight intensityCo-operative effectSustained fluorescencePhotobleachingMisfoldingS-Palmitoylation Sorts Membrane Cargo for Anterograde Transport in the Golgi
Ernst AM, Syed SA, Zaki O, Bottanelli F, Zheng H, Hacke M, Xi Z, Rivera-Molina F, Graham M, Rebane AA, Björkholm P, Baddeley D, Toomre D, Pincet F, Rothman JE. S-Palmitoylation Sorts Membrane Cargo for Anterograde Transport in the Golgi. Developmental Cell 2018, 47: 479-493.e7. PMID: 30458139, PMCID: PMC6251505, DOI: 10.1016/j.devcel.2018.10.024.Peer-Reviewed Original ResearchConceptsS-palmitoylationAnterograde cargoAnterograde signalMembrane cargoCargo selectionTransmembrane domainMembrane proteinsGolgi membranesGolgiSpecific signalsMembrane interfaceModel systemCargoProteinRate of transportAnterograde transportVesiclesCisternaeCurved regionsMembraneTransportRegionSignalsDomainFluorescence
2017
STED Imaging of Golgi Dynamics with Cer-SiR: A Two-Component, Photostable, High-Density Lipid Probe for Live Cells
Erdmann RS, Toomre D, Schepartz A. STED Imaging of Golgi Dynamics with Cer-SiR: A Two-Component, Photostable, High-Density Lipid Probe for Live Cells. Methods In Molecular Biology 2017, 1663: 65-78. PMID: 28924659, PMCID: PMC6146391, DOI: 10.1007/978-1-4939-7265-4_6.Peer-Reviewed Original ResearchConceptsLive cellsMembrane-bound proteinsLipid probesGolgi dynamicsCellular functionsGolgi structureCellular organellesGolgi apparatusCeramide lipidsSuper-resolution imagingLabeling strategySTED imagingSTED microscopyCellsPhotostable fluorophoresLipidsGolgiOrganellesTwo-componentBioorthogonal reactionsProbeProteinHigh density
2016
Sphingomyelin is sorted at the trans Golgi network into a distinct class of secretory vesicle
Deng Y, Rivera-Molina FE, Toomre DK, Burd CG. Sphingomyelin is sorted at the trans Golgi network into a distinct class of secretory vesicle. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 6677-6682. PMID: 27247384, PMCID: PMC4914164, DOI: 10.1073/pnas.1602875113.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkSynthesis of sphingomyelinGolgi networkSecretory vesiclesPlasma membraneQuantitative live-cell imagingVesicular transport carriersSorting of proteinsGlycophosphatidylinositol-anchored proteinsPore-forming toxinsLive-cell imagingInterorganelle traffickingAbundant sphingolipidIntracellular traffickingSecretory proteinsSM transportTransport carriersProteinCell imagingTraffickingDistinct classesSpecific carrierVesiclesPrincipal functionSorting
2015
The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135
Stoops EH, Hull M, Olesen C, Mistry K, Harder JL, Rivera-Molina F, Toomre D, Caplan MJ. The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135. Journal Of Cell Biology 2015, 211: 287-294. PMID: 26504168, PMCID: PMC4621837, DOI: 10.1083/jcb.201502045.Peer-Reviewed Original ResearchConceptsPrimary ciliaSurface proteinsTrans-Golgi networkPolarized epithelial cellsApical surface proteinsSNAP-tag systemBasolateral plasma membraneCell surface proteinsEpithelial cellsApical proteinsPericiliary regionGolgi networkPolarized traffickingCarrier vesiclesProtein deliveryPlasma membraneApical membraneProteinGp135Basolateral membraneCiliaMembraneHot spotsCellsTrafficking
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
2008
Analyzing Protein-Protein Spatial-Temporal Dependencies from Image Sequences Using Fuzzy Temporal Random Sets
Daz M, Ayala G, Len T, Zoncu R, Toomre D. Analyzing Protein-Protein Spatial-Temporal Dependencies from Image Sequences Using Fuzzy Temporal Random Sets. Journal Of Computational Biology 2008, 15: 1221-1236. PMID: 18973437, DOI: 10.1089/cmb.2008.0055.Peer-Reviewed Original ResearchConceptsTotal internal reflection fluorescence microscopyFluorescent-tagged proteinsReflection fluorescence microscopyEndocytic proteinsBiological questionsPlasma membraneDifferent proteinsFluorescence microscopyProteinSequenceK-functionArea of fluorescenceEndocytosisFree tuning parametersGFPBiologistsColocalizationHigh spatial-temporal resolutionMembraneSpatial-temporal resolutionPoisson cluster modelCellsFluorescenceRepair of injured plasma membrane by rapid Ca2+-dependent endocytosis
Idone V, Tam C, Goss JW, Toomre D, Pypaert M, Andrews NW. Repair of injured plasma membrane by rapid Ca2+-dependent endocytosis. Journal Of Cell Biology 2008, 180: 905-914. PMID: 18316410, PMCID: PMC2265401, DOI: 10.1083/jcb.200708010.Peer-Reviewed Original ResearchConceptsPlasma membraneStreptolysin OPore-forming proteinsPlasma membrane lesionsBacterial toxin streptolysin OEnhancement of endocytosisDependent endocytosisToxin streptolysin OImportant new insightsMembrane resealingLysosomal organellesEndocytosisMicrobial toxinsNovel pathwayExocytosisRepair processMembrane lesionsProteinNew insightsMembraneRapid Ca2ResealingRapid repair processCellsImmune system
2007
Loss of endocytic clathrin-coated pits upon acute depletion of phosphatidylinositol 4,5-bisphosphate
Zoncu R, Perera RM, Sebastian R, Nakatsu F, Chen H, Balla T, Ayala G, Toomre D, De Camilli PV. Loss of endocytic clathrin-coated pits upon acute depletion of phosphatidylinositol 4,5-bisphosphate. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 3793-3798. PMID: 17360432, PMCID: PMC1805489, DOI: 10.1073/pnas.0611733104.Peer-Reviewed Original ResearchConceptsClathrin-coated pitsPlasma membraneRegulatory complexEndocytic clathrin-coated pitsClathrin coat dynamicsTotal internal reflection fluorescence microscopyFluorescent fusion proteinsActin regulatory proteinsEndocytic clathrin adaptorsReflection fluorescence microscopyEndocytic adaptorsClathrin spotsClathrin adaptorsActin regulationInducible recruitmentClathrin punctaAccessory factorsFusion proteinCell surfaceFluorescence microscopyP20 subunitAcute depletionDramatic lossAdaptorProtein
2006
Vectorial 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 ProteinsTemperatureTransfectionTrans-Golgi NetworkTransport 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
2005
The Abl/Arg substrate ArgBP2/nArgBP2 coordinates the function of multiple regulatory mechanisms converging on the actin cytoskeleton
Cestra G, Toomre D, Chang S, De Camilli P. The Abl/Arg substrate ArgBP2/nArgBP2 coordinates the function of multiple regulatory mechanisms converging on the actin cytoskeleton. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 1731-1736. PMID: 15659545, PMCID: PMC547834, DOI: 10.1073/pnas.0409376102.Peer-Reviewed Original ResearchConceptsActin cytoskeletonCOOH-terminal SH3 domainFocal adhesion proteinsBrain-specific splice variantCell adhesion sitesMultiple regulatory mechanismsUbiquitin ligase CblNH2-terminal regionArg tyrosine kinasesActin rufflesWAVE isoformsAdaptor proteinScaffold proteinSH3 domainTyrosine phosphorylationRegulatory proteinsAdhesion proteinsStress fibersRegulatory mechanismsTyrosine kinaseCytoskeletonDomain domainSplice variantsNeuronal synapsesProtein