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
2010
Regulation 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
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
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 affinityFibroblastsProtrusion
2003
Two Distinct Phosphorylation Pathways Have Additive Effects on Abl Family Kinase Activation
Tanis KQ, Veach D, Duewel HS, Bornmann WG, Koleske AJ. Two Distinct Phosphorylation Pathways Have Additive Effects on Abl Family Kinase Activation. Molecular And Cellular Biology 2003, 23: 3884-3896. PMID: 12748290, PMCID: PMC155218, DOI: 10.1128/mcb.23.11.3884-3896.2003.Peer-Reviewed Original ResearchConceptsSrc nonreceptor tyrosine kinaseAdditive effectTyrosine kinaseArg nonreceptor tyrosine kinaseKinase activationNonreceptor tyrosine kinaseKinase activityCell surface receptorsSurface receptorsStimuli resultsStimulationFivefold stimulationActivationTwofold stimulationABLPhosphorylationPhosphorylation pathwayPathwaySrc family kinase HckSrc familyAbl 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