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
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
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
2007
The Tyrosine Kinase Activity of c-Src Regulates Actin Dynamics and Organization of Podosomes in Osteoclasts
Destaing O, Sanjay A, Itzstein C, Horne WC, Toomre D, De Camilli P, Baron R. The Tyrosine Kinase Activity of c-Src Regulates Actin Dynamics and Organization of Podosomes in Osteoclasts. Molecular Biology Of The Cell 2007, 19: 394-404. PMID: 17978100, PMCID: PMC2174183, DOI: 10.1091/mbc.e07-03-0227.Peer-Reviewed Original ResearchConceptsKinase activityActin cloudDynamic actin-rich structuresSrc family kinase activityDynamics of podosomesActin-rich structuresF-actin coresTyrosine kinase activityAbsence of SrcSrc mutantActin fluxActin dynamicsPodosome numbersEssential regulatorLife spanPodosomesActin polymerizationPodosome organizationF-actinPodosome structuresSrc inhibitorSrcFluorescence recoveryPodosome beltSpecific functionsLoss 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
Lymphocyte transcellular migration occurs through recruitment of endothelial ICAM-1 to caveola- and F-actin-rich domains
Millán J, Hewlett L, Glyn M, Toomre D, Clark P, Ridley AJ. Lymphocyte transcellular migration occurs through recruitment of endothelial ICAM-1 to caveola- and F-actin-rich domains. Nature Cell Biology 2006, 8: 113-123. PMID: 16429128, DOI: 10.1038/ncb1356.Peer-Reviewed Original ResearchMeSH KeywordsActinsAntibodies, MonoclonalCaveolaeCaveolin 1Cell AdhesionCell MembraneCell MovementCell Surface ExtensionsCells, CulturedEndothelial CellsE-SelectinHumansIntercellular Adhesion Molecule-1Lymphocyte ActivationLymphocytesMicroscopy, Electron, TransmissionMicroscopy, FluorescenceProtein TransportReceptor AggregationRNA, Small InterferingStress FibersT-LymphocytesTransfectionTumor Necrosis Factor-alphaVascular Cell Adhesion Molecule-1
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