2019
Labeling Strategies Matter for Super-Resolution Microscopy: A Comparison between HaloTags and SNAP-tags
Erdmann RS, Baguley SW, Richens JH, Wissner RF, Xi Z, Allgeyer ES, Zhong S, Thompson AD, Lowe N, Butler R, Bewersdorf J, Rothman JE, St Johnston D, Schepartz A, Toomre D. Labeling Strategies Matter for Super-Resolution Microscopy: A Comparison between HaloTags and SNAP-tags. Cell Chemical Biology 2019, 26: 584-592.e6. PMID: 30745239, PMCID: PMC6474801, DOI: 10.1016/j.chembiol.2019.01.003.Peer-Reviewed Original Research
2017
Novel ecto-tagged integrins reveal their trafficking in live cells
Huet-Calderwood C, Rivera-Molina F, Iwamoto DV, Kromann EB, Toomre D, Calderwood DA. Novel ecto-tagged integrins reveal their trafficking in live cells. Nature Communications 2017, 8: 570. PMID: 28924207, PMCID: PMC5603536, DOI: 10.1038/s41467-017-00646-w.Peer-Reviewed Original ResearchConceptsIntegrin functionΒ1 integrinLive cellsCell surface adhesion receptorsHeterodimeric cell-surface adhesion receptorsIntegrin endocytosisMulticellular organismsNovel powerful toolFocal adhesionsKnockout fibroblastsIntegrin activationAdhesion receptorsExtracellular loopIntegrinsTraffickingMajor mysteriesCellsTagsAdhesionHaloTagEndocytosisPowerful toolExocytosisOrganismsVesicles
2012
Optogenetic control of phosphoinositide metabolism
Idevall-Hagren O, Dickson EJ, Hille B, Toomre DK, De Camilli P. Optogenetic control of phosphoinositide metabolism. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: e2316-e2323. PMID: 22847441, PMCID: PMC3435206, DOI: 10.1073/pnas.1211305109.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmino Acid MotifsAnimalsArabidopsis ProteinsBinding SitesCell MembraneChlorocebus aethiopsCOS CellsCryptochromesEndocytosisHumansKCNQ2 Potassium ChannelKCNQ3 Potassium ChannelLightMembrane PotentialsPC12 CellsPhosphatidylinositol 3-KinasesPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositolsPhosphoric Monoester HydrolasesPhosphorylationRatsRecombinant Fusion ProteinsSignal TransductionConceptsCryptochrome 2Membrane rufflingCellular functionsEndocytic clathrin-coated pitsMembrane-targeting motifClathrin-coated pitsLight-induced dimerizationMammalian cellsReversible dephosphorylationPlasma membraneDownstream effectorsPlant proteinsBlue light illuminationPI3KCellular assaysRegion domainsOptogenetic controlPhosphoinositideCell membraneCIBNPhosphoinositide metabolismDephosphorylationCompensatory accumulationRufflingLipid components
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 activationDual-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
2008
Both daughter cells traffic and exocytose membrane at the cleavage furrow during mammalian cytokinesis
Goss JW, Toomre DK. Both daughter cells traffic and exocytose membrane at the cleavage furrow during mammalian cytokinesis. Journal Of Cell Biology 2008, 181: 1047-1054. PMID: 18573914, PMCID: PMC2442215, DOI: 10.1083/jcb.200712137.Peer-Reviewed Original ResearchConceptsDaughter cellsTotal internal reflection fluorescence microscopy imagingCleavage furrowAdvanced live-cell imaging techniquesConfocal time-lapse imagingLive-cell imaging techniquesCell imaging techniquesReserve vesicle poolTime-lapse imagingMidbody abscissionMammalian cytokinesisFluorescence microscopy imagingFluorescent proteinPhotobleaching experimentsCytokinesisVesicle poolLysosomal compartmentIndividual vesiclesSingle vesiclesVesiclesGolgiFurrow regionMidbodyMembraneFurrow
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
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
2003
Nanometer targeting of microtubules to focal adhesions
Krylyshkina O, Anderson KI, Kaverina I, Upmann I, Manstein DJ, Small JV, Toomre DK. Nanometer targeting of microtubules to focal adhesions. Journal Of Cell Biology 2003, 161: 853-859. PMID: 12782685, PMCID: PMC2172972, DOI: 10.1083/jcb.200301102.Peer-Reviewed Original ResearchConceptsTotal internal reflection fluorescence microscopyAdhesion complexesIntact microtubule cytoskeletonReflection fluorescence microscopyGFP-CLIP-170Substrate adhesionFocal adhesionsMicrotubule cytoskeletonCell movementCell peripheryCommon cytoskeletal elementsMicrotubule tipsAdhesion fociCytoskeletal elementsPolymerizing microtubulesTip complexGFP-tubulinMicrotubule endsFluorescence microscopyMicrotubulesMultiple microtubulesSite targetingCentral roleComplexesTargeting
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