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
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
Integrin 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
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
2009
Arg 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
2004
The Arg Non-receptor Tyrosine Kinase Modifies F-actin Structure
Galkin VE, Orlova A, Koleske AJ, Egelman EH. The Arg Non-receptor Tyrosine Kinase Modifies F-actin Structure. Journal Of Molecular Biology 2004, 346: 565-575. PMID: 15670605, DOI: 10.1016/j.jmb.2004.11.078.Peer-Reviewed Original ResearchConceptsSubdomain 1Domain bindsActin filamentsF-actinSingle particle image analysisActin-bundling activityNon-receptor tyrosine kinaseCalponin homology domainActin-binding domainF-actin structuresActin subdomain 1Homology domainAbl familyCH domainCell motilityAdjacent protomersTyrosine kinaseParticle image analysisActin protomersConformational changesCooperative bindingARG proteinProtomersArgProteinThe 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
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 cooperativityArgThe ARG Tyrosine Kinase Interacts with Siva-1 in the Apoptotic Response to Oxidative Stress*
Cao C, Ren X, Kharbanda S, Koleske A, Prasad K, Kufe D. The ARG Tyrosine Kinase Interacts with Siva-1 in the Apoptotic Response to Oxidative Stress*. Journal Of Biological Chemistry 2001, 276: 11465-11468. PMID: 11278261, DOI: 10.1074/jbc.c100050200.Peer-Reviewed Original Research