2021
Platelet-derived growth factor receptor beta activates Abl2 via direct binding and phosphorylation
Wu K, Wu H, Lyu W, Kim Y, Furdui CM, Anderson KS, Koleske AJ. Platelet-derived growth factor receptor beta activates Abl2 via direct binding and phosphorylation. Journal Of Biological Chemistry 2021, 297: 100883. PMID: 34144039, PMCID: PMC8259415, DOI: 10.1016/j.jbc.2021.100883.Peer-Reviewed Original ResearchConceptsAbl family kinasesFamily kinasesPlatelet-derived growth factor receptor betaGrowth factor receptor betaAbl familySrc homology 2 domainSrc homology 3 domainDiverse cellular stimuliPost-translational modificationsN-terminal halfNonreceptor tyrosine kinaseMultiple novel sitesAutoinhibited conformationSrc homologyCytoskeleton organizationCytoplasmic domainCellular stimuliKinase domainGrowth factor receptorReceptor betaKinase activityMolecular mechanismsTyrosine kinaseDirect bindingKinaseAbl2: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
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 resolutionPaxillin
2016
Dendrite Maintenance
Katrancha S, Koleske A. Dendrite Maintenance. 2016, 317-355. DOI: 10.1007/978-4-431-56050-0_14.Peer-Reviewed Original ResearchDendritic spinesArbor stabilityDendrite arborsCytoplasmic nonreceptor tyrosine kinaseDendritic spine formationDendritic spine stabilityProper brain functionPsychiatric illnessSpine stabilityDifferent pathological statesSynaptic connectionsSpine formationBrain functionNormal agingNeurodegenerative diseasesMajor contributing factorSpinePathological statesReceptorsArborsEph receptorsContributing factorTyrosine kinaseCell surface adhesion receptorsMolecular mechanismsArg Deficiency Does not Influence the Course of Myelin Oligodendrocyte Glycoprotein (MOG35-55)-induced Experimental Autoimmune Encephalomyelitis
Jacobsen FA, Hulst C, Bäckström T, Koleske AJ, Andersson Å. Arg Deficiency Does not Influence the Course of Myelin Oligodendrocyte Glycoprotein (MOG35-55)-induced Experimental Autoimmune Encephalomyelitis. Journal Of Clinical & Cellular Immunology 2016, 2016: 420. PMID: 34527426, PMCID: PMC8439389, DOI: 10.4172/2155-9899.1000420.Peer-Reviewed Original ResearchExperimental autoimmune encephalomyelitisAutoimmune encephalomyelitisMyelin oligodendrocyte glycoproteinOligodendrocyte glycoproteinB cellsDevelopment of MOGB-cell traffickingDisease developmentSplenic B cellsLymphocyte phenotypesAbl kinaseImmune activationMultiple sclerosisImmunized miceRodent modelsEncephalomyelitisC57BL/6 backgroundStimulation assaysMiceArg kinaseNovel roleTyrosine kinaseMOGArg tyrosine kinasesActivation
2015
Structure of the ABL2/ARG kinase in complex with dasatinib
Ha BH, Simpson MA, Koleske AJ, Boggon TJ. Structure of the ABL2/ARG kinase in complex with dasatinib. Acta Crystallographica Section F: Structural Biology Communications 2015, 71: 443-448. PMID: 25849507, PMCID: PMC4388181, DOI: 10.1107/s2053230x15004793.Peer-Reviewed Original ResearchConceptsT-cell acute lymphoblastic leukemiaActivation loop tyrosinesABL kinase activationGlycine-rich P-loopCell morphogenesisCo-crystal structureBreakpoint cluster regionCellular functionsArg genesCatalytic domainAbl familyArg kinaseP-loopKinase activationBiological roleOpen conformationTyrosine kinaseAbl kinaseKinaseGenesKinase inhibitorsABL1 geneArgCluster regionTyrosine kinase inhibitors
2014
Abelson 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
2013
Arg kinase signaling in dendrite and synapse stabilization pathways: Memory, cocaine sensitivity, and stress
Kerrisk ME, Koleske AJ. Arg kinase signaling in dendrite and synapse stabilization pathways: Memory, cocaine sensitivity, and stress. The International Journal Of Biochemistry & Cell Biology 2013, 45: 2496-2500. PMID: 23916785, PMCID: PMC3797846, DOI: 10.1016/j.biocel.2013.07.018.Peer-Reviewed Original ResearchConceptsNeuronal actin cytoskeletonPhosphorylation of substratesNonreceptor tyrosine kinaseArg nonreceptor tyrosine kinaseActin cytoskeletonPostnatal mouse brainDendritic spinesArg kinaseMolecular mechanismsF-actinTyrosine kinaseSignaling pathwaysPostnatal day 21Synapse stabilityIntegrin α3β1KinaseNeurodegenerative diseasesNeuronal remodelingTherapeutic approachesCocaine sensitivityStabilization pathwayDay 21Arbor sizeMouse brainArg
2012
Arg/Abl2 promotes invasion and attenuates proliferation of breast cancer in vivo
Gil-Henn H, Patsialou A, Wang Y, Warren MS, Condeelis JS, Koleske AJ. Arg/Abl2 promotes invasion and attenuates proliferation of breast cancer in vivo. Oncogene 2012, 32: 2622-2630. PMID: 22777352, PMCID: PMC3473103, DOI: 10.1038/onc.2012.284.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBreast NeoplasmsCell Line, TumorCell ProliferationErbB ReceptorsFemaleGene Knockdown TechniquesHumansLung NeoplasmsMAP Kinase Signaling SystemMiceMice, SCIDNeoplasm InvasivenessNeoplasm MetastasisNeoplasm TransplantationProto-Oncogene Proteins c-ablSrc-Family KinasesTransplantation, HeterologousConceptsTumor cell invasionBreast cancer cellsTyrosine kinaseCancer cellsCell invasionNon-receptor tyrosine kinaseRas-MAPK signalingRas-MAPK pathwayGene expression patternsSrc tyrosine kinaseInvasion-associated genesUncontrolled cell divisionProliferation-associated genesMetastatic cancer cellsCell divisionExpression patternsEGF receptorTumor cell proliferationPromotes InvasionMouse xenograft modelCell proliferationMultistep processGenetic aberrationsKinaseGenesLysozyme contamination facilitates crystallization of a heterotrimeric cortactin–Arg–lysozyme complex
Liu W, MacGrath SM, Koleske AJ, Boggon TJ. Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin–Arg–lysozyme complex. Acta Crystallographica Section F: Structural Biology Communications 2012, 68: 154-158. PMID: 22297987, PMCID: PMC3274391, DOI: 10.1107/s1744309111056132.Peer-Reviewed Original ResearchConceptsCrystal structure determinationNonreceptor tyrosine kinaseArg nonreceptor tyrosine kinaseHeterotrimeric complexSH3 domainMacromolecular crystallographersCrystallography approachStructure determinationTyrosine kinaseCocrystal structureMolecular replacementTrace amountsLysozyme complexStructure solutionProteinCortactinComplexesCrystallizationCrystallographersCocrystalsKinaseMotifAutomatic model buildingSequenceArg
2011
Cell adhesion signaling pathways: First responders to cocaine exposure?
Gourley SL, Taylor JR, Koleske AJ. Cell adhesion signaling pathways: First responders to cocaine exposure? Communicative & Integrative Biology 2011, 4: 30-3. PMID: 21509173, PMCID: PMC3073265, DOI: 10.4161/cib.4.1.14083.Peer-Reviewed Original ResearchCocaine exposureDendritic spinesDendritic spine structureChronic drug exposureCertain brain regionsExpression/functionDrug exposurePsychomotor sensitizationPsychostimulant exposureBrain regionsFirst respondersNeuronal shapeSpine structureHuman brainRespondersExposureSpineTyrosine kinaseRecent findingsNonreceptor tyrosine kinaseCell adhesion receptorsAdhesion receptorsDevelopmental periodAdhesion factorsCell adhesion factorsCell adhesion signaling pathways
Gourley S, Taylor J, Koleske A. Cell adhesion signaling pathways. Communicative & Integrative Biology 2011, 4: 30-33. DOI: 10.4161/cib.14083.Peer-Reviewed Original ResearchDendritic spinesDendritic spine structureChronic drug exposureCertain brain regionsExpression/functionDrug exposureCocaine exposurePsychomotor sensitizationPsychostimulant exposureBrain regionsNeuronal shapeSpine structureHuman brainExposureSpineTyrosine kinaseRecent findingsNonreceptor tyrosine kinaseCell adhesion receptorsAdhesion receptorsDevelopmental periodAdhesion factorsCell adhesion factorsFirst respondersCytoskeletal effectors
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 elementsP120Synaptic Clustering of PSD-95 Is Regulated by c-Abl through Tyrosine Phosphorylation
de Arce K, Varela-Nallar L, Farias O, Cifuentes A, Bull P, Couch BA, Koleske AJ, Inestrosa NC, Alvarez AR. Synaptic Clustering of PSD-95 Is Regulated by c-Abl through Tyrosine Phosphorylation. Journal Of Neuroscience 2010, 30: 3728-3738. PMID: 20220006, PMCID: PMC2872795, DOI: 10.1523/jneurosci.2024-09.2010.Peer-Reviewed Original ResearchConceptsPSD-95Protein postsynaptic density protein 95Postsynaptic density protein 95PSD-95 clusteringHippocampal neuron culturesFirst postnatal weekC-AblC-Abl levelsPresynaptic markersTyrosine phosphorylationRat hippocampusPostnatal weekPostsynaptic sitesSynaptic clusteringNeuron culturesSynaptic functionC-Abl kinase activityReduced synapsesSynapse formationPostsynaptic compartmentsBrain synapsesGenetic inhibitionSynapsesTyrosine kinaseC-Abl tyrosine kinaseRegulation of Actin Polymerization and Adhesion-Dependent Cell Edge Protrusion by the Abl-Related Gene (Arg) Tyrosine Kinase and N-WASp
Miller MM, Lapetina S, MacGrath SM, Sfakianos MK, Pollard TD, Koleske AJ. Regulation of Actin Polymerization and Adhesion-Dependent Cell Edge Protrusion by the Abl-Related Gene (Arg) Tyrosine Kinase and N-WASp. Biochemistry 2010, 49: 2227-2234. PMID: 20146487, PMCID: PMC2836179, DOI: 10.1021/bi901721u.Peer-Reviewed Original ResearchConceptsCell edge protrusionN-WASPActin polymerizationEdge protrusionN-WASP-dependent actin polymerizationGene Tyrosine KinaseFluorescent protein fusionsNovel binding partnerExtracellular cuesProtein fusionsSH2 domainExtracellular stimuliActin cytoskeletonSH3 domainBinding partnerCellular protrusionsPoint mutantsAffinity purificationTyrosine kinasePhysical interactionSH3PhosphorylationArgABLPotential link
2009
Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts
Bradley WD, Koleske AJ. Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts. Journal Of Cell Science 2009, 122: 3441-3454. PMID: 19759284, PMCID: PMC2746129, DOI: 10.1242/jcs.039859.Peer-Reviewed Original ResearchConceptsAbl family kinasesNon-receptor tyrosine kinaseWAVE family proteinsCell-specific proteinsActivation of cortactinExtracellular cuesEpithelial morphogenesisAdhesion dynamicsCytoskeletal rearrangementsEssential regulatorPhysiological contextCell motilityActin polymerizationCytoskeletal changesPhysiological processesTyrosine kinaseGenetic studiesKinaseMorphogenesisCell contractilityCell migrationProteinComplex processImmune systemCytoskeletonN-Myristoylated c-Abl Tyrosine Kinase Localizes to the Endoplasmic Reticulum upon Binding to an Allosteric Inhibitor*
Choi Y, Seeliger MA, Panjarian SB, Kim H, Deng X, Sim T, Couch B, Koleske AJ, Smithgall TE, Gray NS. N-Myristoylated c-Abl Tyrosine Kinase Localizes to the Endoplasmic Reticulum upon Binding to an Allosteric Inhibitor*. Journal Of Biological Chemistry 2009, 284: 29005-29014. PMID: 19679652, PMCID: PMC2781447, DOI: 10.1074/jbc.m109.026633.Peer-Reviewed Original Research
2008
Enhancement of ABL Kinase Catalytic Efficiency by a Direct Binding Regulator Is Independent of Other Regulatory Mechanisms*
Cao X, Tanis KQ, Koleske AJ, Colicelli J. Enhancement of ABL Kinase Catalytic Efficiency by a Direct Binding Regulator Is Independent of Other Regulatory Mechanisms*. Journal Of Biological Chemistry 2008, 283: 31401-31407. PMID: 18796434, PMCID: PMC2581583, DOI: 10.1074/jbc.m804002200.Peer-Reviewed Original ResearchConceptsSH2 domainKinase activityTyrosine kinaseAbl family tyrosine kinasesKinase activation mechanismRelief of autoinhibitionUnique protein structureFamily tyrosine kinasesCatalytic site mutationsPhosphorylation of CrkInhibitor-resistant mutantsAbl kinase activityTyrosine kinase activitySH3-SH2ABL tyrosine kinase activityABL2 kinaseABL substratesRegulatory domainPhosphorylation mechanismDownstream effectorsDomain coreInactive conformationAbl SH3Regulatory mechanismsProtein structureThe c-Abl tyrosine kinase regulates actin remodeling at the immune synapse
Huang Y, Comiskey EO, Dupree RS, Li S, Koleske AJ, Burkhardt JK. The c-Abl tyrosine kinase regulates actin remodeling at the immune synapse. Blood 2008, 112: 111-119. PMID: 18305217, PMCID: PMC2435682, DOI: 10.1182/blood-2007-10-118232.Peer-Reviewed Original ResearchMeSH KeywordsActinsAdaptor Proteins, Signal TransducingAnimalsCells, CulturedHumansInterleukin-2Jurkat CellsLymphocyte ActivationMiceMice, KnockoutPhosphorylationProtein BindingProteinsProto-Oncogene Proteins c-ablPseudopodiaReceptors, Antigen, T-CellSignal TransductionT-LymphocytesTranscription, GeneticWiskott-Aldrich Syndrome Protein FamilyConceptsC-AblImmune synapseActin responseC-Abl nonreceptor tyrosine kinaseT cell activationTyrosine kinaseC-Abl tyrosine kinaseC-Abl bindsActin regulatory proteinsNonreceptor tyrosine kinaseChemokine-induced T cell migrationT cell receptor engagementSH2 domainActin dynamicsActin reorganizationTyrosine phosphorylationRegulatory proteinsActin polymerizationDownstream eventsNormal localizationConditional knockout miceCoordinate actionReceptor engagementKinaseLamellipodial spreading
2007
Use of a Chemical Genetic Technique To Identify Myosin IIB as a Substrate of the Abl-Related Gene (Arg) Tyrosine Kinase
Boyle SN, Koleske AJ. Use of a Chemical Genetic Technique To Identify Myosin IIB as a Substrate of the Abl-Related Gene (Arg) Tyrosine Kinase. Biochemistry 2007, 46: 11614-11620. PMID: 17892306, DOI: 10.1021/bi701119s.Peer-Reviewed Original ResearchConceptsPutative substratesMyosin IIBGene Tyrosine KinaseUnnatural ATP analoguesProtein substrate specificityPhosphotyrosine-containing proteinsSer/ThrAbl/ArgChemical-genetic techniqueCell morphogenesisKinase substrateDirect substrateFamily kinasesTyrosine phosphorylationSubstrate specificityGenetic techniquesNucleotide specificityMolecular mechanismsTyrosine kinaseK-252aUnexpected high levelATP analogGene kinaseKinaseABL