2022
Control of Synapse Structure and Function by Actin and Its Regulators
Gentile JE, Carrizales MG, Koleske AJ. Control of Synapse Structure and Function by Actin and Its Regulators. Cells 2022, 11: 603. PMID: 35203254, PMCID: PMC8869895, DOI: 10.3390/cells11040603.Peer-Reviewed Original ResearchConceptsActin poolsOrganization of proteinsSynaptic actinOrganization of actinDisease risk genesKey neuronal functionsPost-synaptic compartmentsActin regulatorsDynamic regulationActin filamentsWhole-exome sequencingRisk genesIon channelsGenetic variantsActinRegulatorNeuronal functionSynapse structureExome sequencingPostsynaptic dendritic spinesKey functionsSpecialized junctionsGenesPresynaptic axon terminalsAxon terminals
2021
Abl2:Cortactin Interactions Regulate Dendritic Spine Stability via Control of a Stable Filamentous Actin Pool
Shaw JE, Kilander MBC, Lin YC, Koleske AJ. Abl2:Cortactin Interactions Regulate Dendritic Spine Stability via Control of a Stable Filamentous Actin Pool. Journal Of Neuroscience 2021, 41: 3068-3081. PMID: 33622779, PMCID: PMC8026353, DOI: 10.1523/jneurosci.2472-20.2021.Peer-Reviewed Original ResearchConceptsDendritic spine stabilityDendritic spinesSpine stabilityTonic increaseSubset of spinesSexes of miceMost excitatory synapsesCortactin interactionsGluN2B levelsSpine densitySpine lossArg nonreceptor tyrosine kinaseKinetically distinct poolsExcitatory synapsesHippocampal neuronsSynaptic activitySpine enlargementSpineSpine sizeSpine actinActivity-dependent spine enlargementSpine shapeStructural plasticityDistinct poolsTyrosine kinase
2020
Functional interactions of ion channels with the actin cytoskeleton: does coupling to dynamic actin regulate NMDA receptors?
Shaw JE, Koleske AJ. Functional interactions of ion channels with the actin cytoskeleton: does coupling to dynamic actin regulate NMDA receptors? The Journal Of Physiology 2020, 599: 431-441. PMID: 32034761, PMCID: PMC7416480, DOI: 10.1113/jp278702.Peer-Reviewed Original ResearchConceptsActin cytoskeletonIon channelsPostsynaptic compartmentsCytoskeletal protein actinActin binding proteinsNeurotransmitter release machineryNeurotransmitter receptorsProtein actinSynaptic neurotransmitter receptorsΑ-actininMolecular mechanismsBinding proteinCytoskeletonMolecular linkageFunctional interactionRelease machineryDiverse collectionActinNMDA receptorsTraffickingChannel openingProteinVoltage-gated NaReceptorsCompartments
2018
Abl2 is recruited to ventral actin waves through cytoskeletal interactions to promote lamellipodium extension
Zhang K, Lyu W, Yu J, Koleske AJ. Abl2 is recruited to ventral actin waves through cytoskeletal interactions to promote lamellipodium extension. Molecular Biology Of The Cell 2018, 29: 2863-2873. PMID: 30256707, PMCID: PMC6249870, DOI: 10.1091/mbc.e18-01-0044.Peer-Reviewed Original ResearchConceptsCytoskeletal interactionsLamellipodium extensionTotal internal reflection fluorescence microscopyActin-rich structuresActin wavesActin-rich protrusionsN-terminal halfC-terminal halfNonreceptor tyrosine kinaseReflection fluorescence microscopyFoci colocalizeComplementation analysisLamellipodia protrusionKnockout cellsLamellipodium tipActin filament stabilizerCell shapeBind actinTyrosine kinaseCortactinABL2Fluorescence microscopyIntegrin β3High spatiotemporal resolutionPaxillinCortactin stabilization of actin requires actin-binding repeats and linker, is disrupted by specific substitutions, and is independent of nucleotide state
Scherer AN, Anand NS, Koleske AJ. Cortactin stabilization of actin requires actin-binding repeats and linker, is disrupted by specific substitutions, and is independent of nucleotide state. Journal Of Biological Chemistry 2018, 293: 13022-13032. PMID: 29929984, PMCID: PMC6109930, DOI: 10.1074/jbc.ra118.004068.Peer-Reviewed Original ResearchConceptsHematopoietic cell-specific Lyn substrate 1Nucleotide stateActin bindingActin filamentsTotal internal reflection fluorescence microscopyActin-binding proteins cortactinActin cosedimentation assaysActin-rich structuresHigh-affinity actin bindingADP-actin filamentsReflection fluorescence microscopyAdjacent linker regionActin filament bindingArp2/3 complexCortactin repeatsCellular functionsActin stabilityCosedimentation assaysActin stabilizationProtein cortactinLamellipodial protrusionGTPase regulatorFilament depolymerizationLinker regionActin depolymerization
2014
Abl2/Abl-related Gene Stabilizes Actin Filaments, Stimulates Actin Branching by Actin-related Protein 2/3 Complex, and Promotes Actin Filament Severing by Cofilin*
Courtemanche N, Gifford SM, Simpson MA, Pollard TD, Koleske AJ. Abl2/Abl-related Gene Stabilizes Actin Filaments, Stimulates Actin Branching by Actin-related Protein 2/3 Complex, and Promotes Actin Filament Severing by Cofilin*. Journal Of Biological Chemistry 2014, 290: 4038-4046. PMID: 25540195, PMCID: PMC4326814, DOI: 10.1074/jbc.m114.608117.Peer-Reviewed Original ResearchAbelson phosphorylation of CLASP2 modulates its association with microtubules and actin
Engel U, Zhan Y, Long JB, Boyle SN, Ballif BA, Dorey K, Gygi SP, Koleske AJ, VanVactor D. Abelson phosphorylation of CLASP2 modulates its association with microtubules and actin. Cytoskeleton 2014, 71: 195-209. PMID: 24520051, PMCID: PMC4054870, DOI: 10.1002/cm.21164.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAmino Acid SequenceAnimalsCell AdhesionChlorocebus aethiopsCOS CellsGrowth ConesHEK293 CellsHumansMicrotubule-Associated ProteinsMicrotubulesMolecular Sequence DataPhosphorylationPhosphotyrosinePlatelet-Derived Growth FactorProtein BindingProto-Oncogene Proteins c-ablSignal TransductionSubcellular FractionsSubstrate SpecificityXenopusConceptsAbelson non-receptor tyrosine kinasesNon-receptor tyrosine kinaseBona fide substrateF-actin structuresVertebrate cellsFide substrateProtein CLASPInteraction domainPDGF stimulationCLASP2Tyrosine residuesF-actinTyrosine kinaseNeural developmentAbl phosphorylationMicrotubulesPhosphorylationGrowth conesCytoskeletonABLFunctional relationshipDrosophilaMultiple stagesKinaseNeurulation
2010
The Abl and Arg non‐receptor tyrosine kinases regulate different zones of stress fiber, focal adhesion, and contractile network localization in spreading fibroblasts
Peacock JG, Couch BA, Koleske AJ. The Abl and Arg non‐receptor tyrosine kinases regulate different zones of stress fiber, focal adhesion, and contractile network localization in spreading fibroblasts. Cytoskeleton 2010, 67: 666-675. PMID: 20737438, PMCID: PMC2955401, DOI: 10.1002/cm.20479.Peer-Reviewed Original ResearchConceptsCell peripheryPhosphorylated myosin light chainFocal adhesionsActomyosin contractilitySpatial regulationFocal adhesion dynamicsNon-receptor tyrosine kinaseAbl functionAdhesion dynamicsMutant cellsAbl familyFA formationStress fibersEdge protrusionMyosin light chainF-actinTyrosine kinaseRhoA activityInhibitory complexWT cellsArg functionAdhesive structuresCell migrationAdhesion elementsP120
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
2004
The Abl-related gene (Arg) requires its F-actin–microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion
Miller AL, Wang Y, Mooseker MS, Koleske AJ. The Abl-related gene (Arg) requires its F-actin–microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion. Journal Of Cell Biology 2004, 165: 407-420. PMID: 15138293, PMCID: PMC2172189, DOI: 10.1083/jcb.200308055.Peer-Reviewed Original ResearchConceptsLamellipodial dynamicsCross-linking activityF-actin-binding domainFluorescent protein fusionsMT-binding domainNonreceptor tyrosine kinaseFilamentous actin bundlesWild-type fibroblastsCell polarityProtein fusionsMembrane protrusionsCell peripheryLamellipodial protrusionCell protrusionsActin bundlesMolecular mechanismsTyrosine kinaseF-actinMicrotubulesArgFibroblast adhesionABLHigh affinityFibroblastsProtrusionAbl-dependent tyrosine phosphorylation of Sos-1 mediates growth-factor-induced Rac activation
Sini P, Cannas A, Koleske AJ, Di Fiore PP, Scita G. Abl-dependent tyrosine phosphorylation of Sos-1 mediates growth-factor-induced Rac activation. Nature Cell Biology 2004, 6: 268-274. PMID: 15039778, DOI: 10.1038/ncb1096.Peer-Reviewed Original ResearchConceptsGuanine nucleotide exchange factorsSos-1Rac activationTyrosine phosphorylationFunction of RacNon-receptor tyrosine kinase AblActin cytoskeleton remodellingNucleotide exchange factorsRac-GEF activityTyrosine kinase AblActivation of RTKsActivity of RacReceptor tyrosine kinasesCytoskeleton remodellingActin remodellingSignal transductionMolecular connectionMolecular mechanismsTyrosine kinaseBcr-Abl oncoproteinRacPharmacological interferencePhosphorylationGrowth factorABL signals