2021
Measuring Cell-Edge Protrusion Dynamics during Spreading using Live-Cell Microscopy.
Lukic N, Saha T, Lapetina S, Gendler M, Lehmann G, Koleske AJ, Gil-Henn H. Measuring Cell-Edge Protrusion Dynamics during Spreading using Live-Cell Microscopy. Journal Of Visualized Experiments 2021 PMID: 34779432, PMCID: PMC8672187, DOI: 10.3791/63157.Peer-Reviewed Original ResearchConceptsCell edge protrusionCell migrationProtrusion dynamicsKey actin regulatorsLive-cell microscopyMulticellular organismsActin regulatorsCoordinated regulationEmbryonic developmentMembrane dynamicsEssential eventRegeneration of tissuesCancer metastasisTissue invasionPathological disordersRufflesProtrusionMigrationOrganismsRegulatorHomeostasisRegulationInvasionDysregulationDynamics
2017
Long‐Term Live‐Cell STED Nanoscopy of Primary and Cultured Cells with the Plasma Membrane HIDE Probe DiI‐SiR
Thompson AD, Omar MH, Rivera‐Molina F, Xi Z, Koleske AJ, Toomre DK, Schepartz A. Long‐Term Live‐Cell STED Nanoscopy of Primary and Cultured Cells with the Plasma Membrane HIDE Probe DiI‐SiR. Angewandte Chemie International Edition 2017, 56: 10408-10412. PMID: 28679029, PMCID: PMC5576494, DOI: 10.1002/anie.201704783.Peer-Reviewed Original Research
2013
Integrin α3 Is Required for Late Postnatal Stability of Dendrite Arbors, Dendritic Spines and Synapses, and Mouse Behavior
Kerrisk ME, Greer CA, Koleske AJ. Integrin α3 Is Required for Late Postnatal Stability of Dendrite Arbors, Dendritic Spines and Synapses, and Mouse Behavior. Journal Of Neuroscience 2013, 33: 6742-6752. PMID: 23595732, PMCID: PMC3711182, DOI: 10.1523/jneurosci.0528-13.2013.Peer-Reviewed Original ResearchMeSH KeywordsAge FactorsAlpha-FetoproteinsAnalysis of VarianceAnimalsAnimals, NewbornBasic Helix-Loop-Helix Transcription FactorsCell MembraneDendritesDendritic SpinesDisks Large Homolog 4 ProteinFemaleGene Expression Regulation, DevelopmentalGreen Fluorescent ProteinsGuanylate KinasesHippocampusImmunoprecipitationIntegrin alpha3LysineMaleMembrane ProteinsMemory DisordersMiceMice, Inbred C57BLMice, TransgenicModels, BiologicalNerve Tissue ProteinsNeuronsPhosphopyruvate HydrataseRecognition, PsychologyRhoA GTP-Binding ProteinSynapsesConceptsDendritic spinesIntegrin α3Adult rodent forebrainHippocampal-dependent behaviorsPostnatal day 21Excitatory forebrain neuronsMouse behaviorProper hippocampal functionLong-term potentiationArbor stabilityArg nonreceptor tyrosine kinaseRodent forebrainForebrain neuronsSynapse densitySynapse stabilityDendrite arborsDay 21Arbor sizeHippocampal dendritesHippocampal functionMutant miceSynapse maintenanceBrain functionNeurodegenerative diseasesKey mediator
2009
Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion
Lapetina S, Mader CC, Machida K, Mayer BJ, Koleske AJ. Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion. Journal Of Cell Biology 2009, 185: 503-519. PMID: 19414610, PMCID: PMC2700396, DOI: 10.1083/jcb.200809085.Peer-Reviewed Original ResearchConceptsCell edge protrusionEdge protrusionActin polymerization machineryAdhesion-dependent phosphorylationCell-matrix adhesionPro-rich motifMutation of residuesPolymerization machinerySH2 domainDomain bindsC-terminusCortactinMolecular mechanismsGene kinaseSimilar defectsAdditional binding sitesCatalytic eventsBinding sitesArgInteractsFibroblast adhesionProtrusionNck1KinasePhosphorylation
2007
A Critical Role for Cortactin Phosphorylation by Abl-Family Kinases in PDGF-Induced Dorsal-Wave Formation
Boyle SN, Michaud GA, Schweitzer B, Predki PF, Koleske AJ. A Critical Role for Cortactin Phosphorylation by Abl-Family Kinases in PDGF-Induced Dorsal-Wave Formation. Current Biology 2007, 17: 445-451. PMID: 17306540, DOI: 10.1016/j.cub.2007.01.057.Peer-Reviewed Original ResearchConceptsAbl family kinasesCortactin phosphorylationActin regulatory protein cortactinTyrosine kinaseAbl family tyrosine kinasesSrc family kinasesNonreceptor tyrosine kinaseHuman protein microarrayCell morphogenesisActin reorganizationCytoskeletal rearrangementsProtein cortactinGrowth factor receptorLamellipodial protrusionCytoskeletal structuresCell motilityProper regulationPDGF treatmentTyrosine residuesCortactinKinaseNovel substrateDownstream actionsPhosphorylationProtein microarrays
2006
Shigella IpgB1 promotes bacterial entry through the ELMO–Dock180 machinery
Handa Y, Suzuki M, Ohya K, Iwai H, Ishijima N, Koleske AJ, Fukui Y, Sasakawa C. Shigella IpgB1 promotes bacterial entry through the ELMO–Dock180 machinery. Nature Cell Biology 2006, 9: 121-128. PMID: 17173036, DOI: 10.1038/ncb1526.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBacterial AdhesionCell LineCell MembraneDogsHeLa CellsHumansImmunoprecipitationMiceModels, BiologicalNIH 3T3 CellsProtein TransportRac GTP-Binding ProteinsRac1 GTP-Binding ProteinRNA InterferenceShigellaSignal TransductionTransduction, GeneticTransfectionConceptsMembrane rufflesCell motility proteinsRole of RhoGEpithelial cellsType III secretionWild-type cellsMembrane associationMotility proteinsPulldown assaysBinding partnerDock180 pathwayBacterial entryRufflesRac1 activityIpgB1EffectorsPivotal roleCellsELMODock180RhoGSpecial mechanismShigellaMachineryEngulfmentIntegrin Signaling through Arg Activates p190RhoGAP by Promoting Its Binding to p120RasGAP and Recruitment to the Membrane
Bradley WD, Hernández SE, Settleman J, Koleske AJ. Integrin Signaling through Arg Activates p190RhoGAP by Promoting Its Binding to p120RasGAP and Recruitment to the Membrane. Molecular Biology Of The Cell 2006, 17: 4827-4836. PMID: 16971514, PMCID: PMC1635390, DOI: 10.1091/mbc.e06-02-0132.Peer-Reviewed Original ResearchConceptsCell peripheryP120 bindingGene Tyrosine KinaseRho family GTPases RhoAActin stress fibersIntegrin-mediated adhesionWild-type fibroblastsP190 phosphorylationFocal adhesionsGTPases RhoARho activityStress fibersEssential effectorTyrosine kinaseAdhesive environmentCell attachmentP190P120P190RhoGAPP120RasGAPPhosphorylationComplex formationBindingRecruitmentRho
1995
Reduction of caveolin and caveolae in oncogenically transformed cells.
Koleske AJ, Baltimore D, Lisanti MP. Reduction of caveolin and caveolae in oncogenically transformed cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 1381-1385. PMID: 7877987, PMCID: PMC42523, DOI: 10.1073/pnas.92.5.1381.Peer-Reviewed Original ResearchConceptsPlasma membraneTransduction of signalsNIH 3T3 cellsSize of coloniesOncogenic transformationCaveolaeProtein coatCaveolinDemonstrated roleContact inhibitionCellular levelSoft agarElectron microscopy revealsCell linesCritical roleMicroscopy revealsCellsMembranePotocytosisTransductionFunctional alterationsOncogeneInvaginationColoniesRoleCaveolae, transmembrane signalling and cellular transformation
Lisanti M, Tang Z, Scherer P, Kübler E, Koleske A, Sargiacomo M. Caveolae, transmembrane signalling and cellular transformation. Molecular Membrane Biology 1995, 12: 121-124. PMID: 7767370, DOI: 10.3109/09687689509038506.Peer-Reviewed Original ResearchConceptsCaveolin-rich membrane domainsV-Src substrateCaveolar marker proteinCaveolar functionSmall moleculesMembrane domainsCellular transformationPlasma membraneCaveolaeMarker proteinsCultured cellsCapillary endothelial cellsProteinEndothelial cellsCellsMembraneCaveolinTransmembraneCytoplasmGPITranslocationElectron micrographsMoleculesWide varietyTranscytosis