2016
The Src kinases Hck, Fgr and Lyn activate Arg to facilitate IgG-mediated phagocytosis and Leishmania infection
Wetzel DM, Rhodes EL, Li S, McMahon-Pratt D, Koleske AJ. The Src kinases Hck, Fgr and Lyn activate Arg to facilitate IgG-mediated phagocytosis and Leishmania infection. Journal Of Cell Science 2016, 129: 3130-3143. PMID: 27358479, PMCID: PMC5004897, DOI: 10.1242/jcs.185595.Peer-Reviewed Original ResearchMeSH KeywordsAniline CompoundsAnimalsCytokinesDisease Models, AnimalImatinib MesylateImmunoglobulin GLeishmaniaLeishmaniasisMacrophagesMiceModels, BiologicalNitrilesParasitesPhagocytosisPhosphorylationProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-hckPyrimidinesQuinolinesRAW 264.7 CellsSignal TransductionSrc-Family KinasesConceptsAmastigote uptakeObligate intracellular parasite LeishmaniaImmunoglobulin-mediated phagocytosisIntracellular parasite LeishmaniaNovel therapeutic strategiesPersistence of infectionLeishmania infectionIgG-mediated phagocytosisTherapeutic strategiesFc receptorsSmall molecule inhibitorsArg activationDisease severityParasite burdenPrimary macrophagesMacrophagesKinase inhibitorsLeishmaniasisHuman hostDevastating diseaseInfectionParasite LeishmaniaSrc family kinasesPhagocytosisLeishmania
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
2012
Cortactin in cell migration and cancer at a glance
MacGrath SM, Koleske AJ. Cortactin in cell migration and cancer at a glance. Journal Of Cell Science 2012, 125: 1621-1626. PMID: 22566665, PMCID: PMC3346822, DOI: 10.1242/jcs.093781.Peer-Reviewed Original Research
2011
Cortactin phosphorylation regulates cell invasion through a pH-dependent pathway
Magalhaes MA, Larson DR, Mader CC, Bravo-Cordero JJ, Gil-Henn H, Oser M, Chen X, Koleske AJ, Condeelis J. Cortactin phosphorylation regulates cell invasion through a pH-dependent pathway. Journal Of Cell Biology 2011, 195: 903-920. PMID: 22105349, PMCID: PMC3257566, DOI: 10.1083/jcb.201103045.Peer-Reviewed Original ResearchMeSH KeywordsActin Depolymerizing FactorsAdaptor Proteins, Signal TransducingCation Transport ProteinsCell Line, TumorCell Surface ExtensionsCortactinHumansHydrogen-Ion ConcentrationModels, BiologicalNeoplasm InvasivenessOncogene ProteinsPhosphorylationSodium-Hydrogen Exchanger 1Sodium-Hydrogen ExchangersConceptsCortactin phosphorylationCell invasionInvadopodia maturationCortactin tyrosine phosphorylationPH-dependent regulationInvasive protrusionsPH-dependent pathwayCofilin activityCofilin regulationTyrosine phosphorylationExchanger NHE1Cofilin activationPhosphorylationInvadopodiaProteolytic activityPrecise mechanismInvasionNHE1RegulationDynamic cyclePathwayMaturationTumor cellsNck1Cofilin
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 mechanismShigellaMachineryEngulfment