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 bindingKinase
2019
Regulation of MT dynamics via direct binding of an Abl family kinase
Hu Y, Lyu W, Lowery LA, Koleske AJ. Regulation of MT dynamics via direct binding of an Abl family kinase. Journal Of Cell Biology 2019, 218: 3986-3997. PMID: 31699690, PMCID: PMC6891085, DOI: 10.1083/jcb.201812144.Peer-Reviewed Original ResearchConceptsAbl family kinasesC-terminal halfFamily kinasesMT dynamicsMT growthTubulin C-terminal tailsC-terminal tailStable reexpressionEssential regulatorCell shapeBinds microtubulesMT polymerizationAbl kinaseGenetic studiesDirect bindingFunctional interactionKinaseMicrotubulesABL2ReexpressionMT behaviorBindingRegulatorProteinGrowth
2018
Analysis of Cellular Tyrosine Phosphorylation via Chemical Rescue of Conditionally Active Abl Kinase
Wang Z, Kim MS, Martinez-Ferrando I, Koleske A, Pandey A, Cole P. Analysis of Cellular Tyrosine Phosphorylation via Chemical Rescue of Conditionally Active Abl Kinase. Biochemistry 2018, 57: 1390-1398. PMID: 29341593, PMCID: PMC5906802, DOI: 10.1021/acs.biochem.7b01158.Peer-Reviewed Original ResearchConceptsProtein kinaseNonreceptor tyrosine kinases AblMass spectrometry-based quantitative proteomicsNovel putative substratesTyrosine kinase AblCellular tyrosine phosphorylationExtracellular growth factorsChemical rescue approachIntracellular signal transductionQuantitative phosphoproteomicsUnanticipated functionCellular physiologyGrowth factorPhosphorylation sitesPutative substratesDirect substrateDownstream substratesSignal transductionReceptor kinaseQuantitative proteomicsTyrosine phosphorylationActive Abl kinasesAbl kinaseChemical rescueKinase
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 aberrationsKinaseGenesIntegrin β1 Signals through Arg to Regulate Postnatal Dendritic Arborization, Synapse Density, and Behavior
Warren MS, Bradley WD, Gourley SL, Lin YC, Simpson MA, Reichardt LF, Greer CA, Taylor JR, Koleske AJ. Integrin β1 Signals through Arg to Regulate Postnatal Dendritic Arborization, Synapse Density, and Behavior. Journal Of Neuroscience 2012, 32: 2824-2834. PMID: 22357865, PMCID: PMC3313657, DOI: 10.1523/jneurosci.3942-11.2012.Peer-Reviewed Original ResearchMeSH KeywordsAlpha-FetoproteinsAnalysis of VarianceAnimalsAnimals, NewbornAvoidance LearningBasic Helix-Loop-Helix Transcription FactorsCells, CulturedCocaineDendritesEnzyme-Linked Immunosorbent AssayExploratory BehaviorGreen Fluorescent ProteinsGTPase-Activating ProteinsHippocampusImmunoprecipitationIntegrin beta1MaleMiceMice, KnockoutMutationNerve Tissue ProteinsNeuronsOrgan Culture TechniquesPost-Synaptic DensityProtein BindingRecognition, PsychologyRepressor ProteinsSignal TransductionSrc Homology DomainsSynapsesConceptsIntegrin β1Vertebrate nervous systemExtracellular matrix receptorsGenetic experimentsIntracellular tailGenetic manipulationRhoA GTPaseArg kinaseMatrix receptorsProper hippocampal functionProper developmentSynapse maintenanceDose-sensitive mannerImpaired hippocampus-dependent learningHippocampal dendritic arborsHippocampal synapse lossDendritic arbor sizeHippocampus-dependent learningΒ1ArgSelective lossGTPaseP190RhoGAPPsychomotor sensitivityKinaseLysozyme 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
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 systemCytoskeletonArg 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
2008
The 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 kinaseKinaseABLDissecting kinase signaling pathways
Boyle SN, Koleske AJ. Dissecting kinase signaling pathways. Drug Discovery Today 2007, 12: 717-724. PMID: 17826684, DOI: 10.1016/j.drudis.2007.07.019.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedAntineoplastic AgentsBenzamidesDrug Delivery SystemsHumansImatinib MesylateLapatinibNeoplasmsPhosphoproteinsPhosphorylationPiperazinesProtein Kinase InhibitorsProtein KinasesProteomicsPyrimidinesQuinazolinesSignal TransductionTrastuzumabConceptsSame protein substrateProtein Kinase SignalingKinase substratePutative substratesProtein substratesKinase signalingProtein kinaseMultiple kinasesPhysiological substratesKinaseHuman diseasesDrug targetsPhysiological relevanceSubstrate interactionsKinase inhibitorsPathwaySignalingSubstrateNeurological disordersInteractionHallmarkInhibitorsTargetA 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
Adhesion-Dependent Regulation of p190RhoGAP in the Developing Brain by the Abl-Related Gene Tyrosine Kinase
Hernández SE, Settleman J, Koleske AJ. Adhesion-Dependent Regulation of p190RhoGAP in the Developing Brain by the Abl-Related Gene Tyrosine Kinase. Current Biology 2004, 14: 691-696. PMID: 15084284, DOI: 10.1016/j.cub.2004.03.062.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsBrainCytoskeletonDNA-Binding ProteinsGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsImmunoblottingMiceMorphogenesisNeuritesNeuronsNuclear ProteinsPhosphorylationPlasmidsPrecipitin TestsProtein-Tyrosine KinasesRepressor ProteinsTransfectionTumor Cells, CulturedConceptsAdhesion-dependent regulationArg substrateNeuronal morphogenesisKinase activityGene Tyrosine KinaseActin-dependent processesWild-type extractsWild-type cellsArg kinase activityAbl kinase activityMembrane rufflingPostnatal mouse brainFamily kinasesCytoskeletal rearrangementsPhosphotyrosine contentFilopodial protrusionsCell motilityArg kinaseP190RhoGAPMouse brainTyrosine kinaseKinasePhosphorylationMorphogenesisPostnatal brainHow do Abl family kinases regulate cell shape and movement?
Hernández SE, Krishnaswami M, Miller AL, Koleske AJ. How do Abl family kinases regulate cell shape and movement? Trends In Cell Biology 2004, 14: 36-44. PMID: 14729179, DOI: 10.1016/j.tcb.2003.11.003.Peer-Reviewed Original ResearchConceptsAbl family kinasesFamily kinasesAdhesion receptorsC-terminal halfCytoskeletal regulatory proteinsNonreceptor tyrosine kinaseCell morphogenesisCytoskeletal dynamicsRecent biochemicalCytoskeletal rearrangementsCytoskeletal structuresCytoskeletal componentsRegulatory proteinsCell shapeGenetic analysisTyrosine kinaseKinaseCell surfaceARG proteinRelay signalsProteinLeukemia cellsDrosophilaCrystallographic analysisMorphogenesis
2003
Regulation of neuronal morphogenesis and synaptic function by Abl family kinases
Moresco E, Koleske AJ. Regulation of neuronal morphogenesis and synaptic function by Abl family kinases. Current Opinion In Neurobiology 2003, 13: 535-544. PMID: 14630215, DOI: 10.1016/j.conb.2003.08.002.Peer-Reviewed Original ResearchAbl Family Nonreceptor Tyrosine Kinases Modulate Short-Term Synaptic Plasticity
Moresco EM, Scheetz AJ, Bornmann WG, Koleske AJ, Fitzsimonds RM. Abl Family Nonreceptor Tyrosine Kinases Modulate Short-Term Synaptic Plasticity. Journal Of Neurophysiology 2003, 89: 1678-1687. PMID: 12626632, DOI: 10.1152/jn.00892.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBenzamidesEnzyme InhibitorsHippocampusImatinib MesylateLong-Term PotentiationLong-Term Synaptic DepressionMiceMice, Mutant StrainsMicroscopy, ImmunoelectronNeuronal PlasticityOrgan Culture TechniquesPiperazinesProbabilityProtein-Tyrosine KinasesProto-Oncogene Proteins c-ablPyrimidinesSynapsesSynaptic TransmissionConceptsActin cytoskeletal dynamicsAbl family kinasesNonreceptor tyrosine kinasePaired-pulse facilitationCell morphogenesisMouse hippocampal area CA1Wild-type slicesActin cytoskeletonCytoskeletal dynamicsLong-term depressionLong-term potentiationFamily kinasesAdult mouse brainNonreceptor tyrosineTyrosine kinaseWild-type controlsFunctional interactionPostsynaptic compartmentsPosttetanic potentiationImmunoelectron microscopyMature neuronsImportant functionsKinaseBasal synaptic transmissionABL
2001
The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin
Wang Y, Miller A, Mooseker M, Koleske A. The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 14865-14870. PMID: 11752434, PMCID: PMC64950, DOI: 10.1073/pnas.251249298.Peer-Reviewed Original ResearchConceptsF-actin-binding domainActin-rich structuresAbl family kinasesNonreceptor tyrosine kinaseF-actinActin cytoskeletonFamily kinasesFluorescent protein fusion proteinTyrosine kinaseActin-bundling activityProtein fusion proteinActin cytoskeletal structuresCellular morphogenesisSwiss 3T3 fibroblastsBundling activityDeletion mutantsCytoskeletal structuresC-terminusFusion proteinFunctional interactionKinaseActin moleculesCytoskeletonPositive cooperativityArg