2011
Dual-mode of insulin action controls GLUT4 vesicle exocytosis
Xu Y, Rubin BR, Orme CM, Karpikov A, Yu C, Bogan JS, Toomre DK. Dual-mode of insulin action controls GLUT4 vesicle exocytosis. Journal Of Cell Biology 2011, 193: 643-653. PMID: 21555461, PMCID: PMC3166865, DOI: 10.1083/jcb.201008135.Peer-Reviewed Original ResearchMeSH Keywords3T3-L1 CellsAdipocytesAnimalsBiosensing TechniquesCarrier ProteinsExocytosisGlucose Transporter Type 4Green Fluorescent ProteinsInsulinIntracellular Signaling Peptides and ProteinsKineticsMembrane FusionMiceMicroscopy, FluorescenceMicroscopy, VideoPhospholipase DRecombinant Fusion ProteinsRNA InterferenceTransfectionTransport VesiclesVesicle-Associated Membrane Protein 2ConceptsGLUT4 storage vesiclesVesicle exocytosisInsulin-stimulated control cellsGLUT4 vesicle exocytosisPlasma membrane fusionNovel regulatory siteSingle vesicle exocytosisInsulin triggersVesicle trafficExocytic rateFusion poreSurface of adipocytesMembrane fusionRegulatory sitesPhospholipase DStorage vesiclesPore expansionExocytosisControl cellsAcute perturbationVesiclesInsulin actionVesicle characteristicsAdipocytesCells
2010
Spatial control of EGF receptor activation by reversible dimerization on living cells
Chung I, Akita R, Vandlen R, Toomre D, Schlessinger J, Mellman I. Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 2010, 464: 783-787. PMID: 20208517, DOI: 10.1038/nature08827.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell Line, TumorCell PolarityCell SurvivalCHO CellsCricetinaeCricetulusDiffusionEnzyme ActivationEnzyme StabilityEpidermal Growth FactorErbB ReceptorsGene Expression RegulationGRB2 Adaptor ProteinHumansKineticsLigandsProtein MultimerizationProtein TransportSignal TransductionThermodynamicsConceptsLigand bindingEpidermal growth factor receptor moleculeType I receptor kinaseEGF receptor activationDimer formationReceptor kinaseReceptor dimerizationDimerization dynamicsReceptor dimersLiving cellsReceptor moleculesCell marginsDimer populationSpatial controlHuman carcinomasConformation changeDimerizationCell centerReceptor activationRate of dissociationCellsBindingActivationKinaseReversible dimerization
2006
Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking
Iwakiri Y, Satoh A, Chatterjee S, Toomre DK, Chalouni CM, Fulton D, Groszmann RJ, Shah VH, Sessa WC. Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 19777-19782. PMID: 17170139, PMCID: PMC1750883, DOI: 10.1073/pnas.0605907103.Peer-Reviewed Original ResearchConceptsProtein S-nitrosylationS-nitrosylationN-ethylmaleimide-sensitive factorPlasma membrane caveolaeAlters protein functionSpecific cysteine residuesSpecific posttranslational modificationsSpecific S-nitrosylationS-nitrosylation reactionsIntracellular transport processesProtein traffickingMembrane caveolaeProtein functionProtein transportPosttranslational modificationsCysteine residuesPlasma membraneTarget proteinsENOS localizationGolgi apparatusEndoplasmic reticulumGolgiDiffusible natureNOS actionGenerate nitric oxideVectorial 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
2005
Phosphatidylinositol phosphate kinase type Iγ regulates dynamics of large dense-core vesicle fusion
Gong LW, Di Paolo G, Diaz E, Cestra G, Diaz ME, Lindau M, De Camilli P, Toomre D. Phosphatidylinositol phosphate kinase type Iγ regulates dynamics of large dense-core vesicle fusion. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 5204-5209. PMID: 15793002, PMCID: PMC555604, DOI: 10.1073/pnas.0501412102.Peer-Reviewed Original ResearchConceptsDense-core vesicle fusionLarge dense-core vesicle fusionLarge dense-core vesicle (LDCV) exocytosisDense-core vesicle exocytosisFusion pore expansionDirect genetic evidenceReleasable vesicle poolType IγVesicle exocytosisGenetic evidenceVesicle primingBisphosphate synthesisVesicle fusionKinetics of secretionImportant regulatorVesicle poolPore expansionNeuroendocrine tissuesPhosphatidylinositolFusion dynamicsChromaffin cellsI gammaKey role