2020
ABL1, Overexpressed in Hepatocellular Carcinomas, Regulates Expression of NOTCH1 and Promotes Development of Liver Tumors in Mice
Wang F, Hou W, Chitsike L, Xu Y, Bettler C, Perera A, Bank T, Cotler SJ, Dhanarajan A, Denning MF, Ding X, Breslin P, Qiang W, Li J, Koleske AJ, Qiu W. ABL1, Overexpressed in Hepatocellular Carcinomas, Regulates Expression of NOTCH1 and Promotes Development of Liver Tumors in Mice. Gastroenterology 2020, 159: 289-305.e16. PMID: 32171747, PMCID: PMC7387191, DOI: 10.1053/j.gastro.2020.03.013.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarcinoma, HepatocellularCell Line, TumorDatasets as TopicDisease Models, AnimalFemaleGene Expression Regulation, NeoplasticGene Knockdown TechniquesHumansKaplan-Meier EstimateLiverLiver NeoplasmsMaleMicePhosphorylationPrognosisProto-Oncogene MasProto-Oncogene Proteins c-ablProto-Oncogene Proteins c-mycPyrimidinesReceptor, Notch1Xenograft Model Antitumor AssaysConceptsShorter survival timeLiver tumorsExpression of Notch1Hepatocellular carcinomaHuman HCC cellsHCC cellsXenograft tumorsSurvival timeExpression of MYCLiver tissueTreatment of HCCAlbumin-Cre miceNon-tumor liver tissuesABL proto-oncogene 1Nontumor liver tissuesHuman HCC specimensHuh7 HCC cellsHepatocyte-specific disruptionHCC tissue microarrayProto-oncogene 1HCC cell linesShort hairpin RNACancer Genome AtlasKnockdown of Notch1Tumor levels
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 ResearchMeSH Keywords3T3 CellsAnimalsFusion Proteins, bcr-ablGene OntologyHEK293 CellsHumansMicePhosphorylationPoint MutationProteomicsProto-Oncogene Proteins c-ablTyrosineConceptsProtein 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
2017
The vascular endothelial specific IL-4 receptor alpha–ABL1 kinase signaling axis regulates the severity of IgE-mediated anaphylactic reactions
Yamani A, Wu D, Waggoner L, Noah T, Koleske AJ, Finkelman F, Hogan SP. The vascular endothelial specific IL-4 receptor alpha–ABL1 kinase signaling axis regulates the severity of IgE-mediated anaphylactic reactions. Journal Of Allergy And Clinical Immunology 2017, 142: 1159-1172.e5. PMID: 29157947, PMCID: PMC5957775, DOI: 10.1016/j.jaci.2017.08.046.Peer-Reviewed Original ResearchConceptsIgE-mediated anaphylactic reactionsAnaphylactic reactionsFluid extravasationIL-4RαBarrier dysfunctionIL-4Food-induced anaphylactic reactionsIgE-induced anaphylaxisFood-induced anaphylaxisIgE-mediated anaphylaxisIL-4 receptor α chainIgE-mediated reactionsTreatment of miceSevere anaphylactic reactionsSeverity of anaphylaxisABL kinase inhibitor imatinibKinase inhibitor imatinibReceptor α chainVe cell linesVenous vasodilatationOral antigenHypovolemic shockInhibitor imatinibAnaphylaxisVe cellsThe Abl‐1 Kinase is Dispensable for NK Cell Inhibitory Signalling and is not Involved in Murine NK Cell Education
Ganesan S, Luu TT, Chambers BJ, Meinke S, Brodin P, Vivier E, Wetzel DM, Koleske AJ, Kadri N, Höglund P. The Abl‐1 Kinase is Dispensable for NK Cell Inhibitory Signalling and is not Involved in Murine NK Cell Education. Scandinavian Journal Of Immunology 2017, 86: 135-142. PMID: 28605050, PMCID: PMC5568956, DOI: 10.1111/sji.12574.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, LyCell DifferentiationCells, CulturedCytotoxicity, ImmunologicImmunity, InnateInterferon-gammaKiller Cells, NaturalLymphocyte ActivationMiceMice, Inbred C57BLMice, KnockoutNatural Cytotoxicity Triggering Receptor 1NK Cell Lectin-Like Receptor Subfamily CProto-Oncogene Proteins c-ablSignal TransductionConceptsNK cell educationNK cellsCell educationNatural killer cell responsivenessYAC-1 tumor cellsNK cell inhibitionNK cell functionHuman NK cellsMurine NK cellsMHC class IC-AblC-Abl expressionInhibitory Ly49Normal inhibitoryNKG2A receptorsInhibitory receptorsCell responsivenessReceptor stimulationReceptor repertoireInhibitory signalingTumor cellsITAM receptorsClass ICell inhibitionCell function
2016
Reciprocal stabilization of ABL and TAZ regulates osteoblastogenesis through transcription factor RUNX2
Matsumoto Y, La Rose J, Kent OA, Wagner MJ, Narimatsu M, Levy AD, Omar MH, Tong J, Krieger JR, Riggs E, Storozhuk Y, Pasquale J, Ventura M, Yeganeh B, Post M, Moran MF, Grynpas MD, Wrana JL, Superti-Furga G, Koleske AJ, Pendergast AM, Rottapel R. Reciprocal stabilization of ABL and TAZ regulates osteoblastogenesis through transcription factor RUNX2. Journal Of Clinical Investigation 2016, 126: 4482-4496. PMID: 27797343, PMCID: PMC5127668, DOI: 10.1172/jci87802.Peer-Reviewed Original ResearchConceptsLineage-specifying transcription factorsReciprocal stabilizationAdaptor protein 3BP2TAZ nuclear localizationTranscription factor complexTyrosine kinase AblTranscription factor Runx2Transcriptional coactivator TAZLineage-specific maturationMetazoan organismsCellular identityOsteoblast expansionTranscriptional positive feedbackTranscription factorsSkeletal formationFactor complexNuclear localizationOwn expressionPositive feedback loopGenetic dataOsteoblast lineageMaturation programOsteoblast differentiationDevelopmental networksTAZ
2014
Two Amino Acid Residues Confer Different Binding Affinities of Abelson Family Kinase Src Homology 2 Domains for Phosphorylated Cortactin*
Gifford SM, Liu W, Mader CC, Halo TL, Machida K, Boggon TJ, Koleske AJ. Two Amino Acid Residues Confer Different Binding Affinities of Abelson Family Kinase Src Homology 2 Domains for Phosphorylated Cortactin*. Journal Of Biological Chemistry 2014, 289: 19704-19713. PMID: 24891505, PMCID: PMC4094080, DOI: 10.1074/jbc.m114.556480.Peer-Reviewed Original ResearchConceptsAbl SH2 domainSH2 domainAbl family kinasesFamily kinasesSrc homology 2 domainCell edge protrusionAbl SH2Similar N-terminal sequencesImportant non-redundant rolesWild-type levelsAmino acid sequenceAmino acid positionsN-terminal sequenceNon-redundant roleCell morphogenesisArg substrateCellular functionsSpecific phosphotyrosineCell peripheryAcid sequenceSerine 187Edge protrusionTarget proteinsType levelsDifferent binding affinitiesAbelson 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
WAVE2 Regulates Epithelial Morphology and Cadherin Isoform Switching through Regulation of Twist and Abl
Bryce NS, Reynolds AB, Koleske AJ, Weaver AM. WAVE2 Regulates Epithelial Morphology and Cadherin Isoform Switching through Regulation of Twist and Abl. PLOS ONE 2013, 8: e64533. PMID: 23691243, PMCID: PMC3654908, DOI: 10.1371/journal.pone.0064533.Peer-Reviewed Original ResearchConceptsEpithelial morphogenesisAbl kinaseActin cytoskeletal rearrangementCell-cell junctionsE-cadherinRegulation of TwistTotal cell lysatesAbl kinase activityEpithelial morphologyTranscription factor Twist1N-cadherin proteinTwist1 expressionWAVE2 complexABL substratesCellular signalingInhibition of AblCadherin isoformsCytoskeletal rearrangementsTyrosine phosphorylationEpithelial-mesenchymal transitionKinase activityMorphological phenotypesFilament localizationCadherin expressionWAVE2
2012
A Peptide Photoaffinity Probe Specific for the Active Conformation of the Abl Tyrosine Kinase
Deng Y, Couch BA, Koleske AJ, Turk BE. A Peptide Photoaffinity Probe Specific for the Active Conformation of the Abl Tyrosine Kinase. ChemBioChem 2012, 13: 2510-2512. PMID: 23081945, PMCID: PMC3595066, DOI: 10.1002/cbic.201200560.Peer-Reviewed Original ResearchMet acts through Abl to regulate p53 transcriptional outcomes and cell survival in the developing liver
Furlan A, Lamballe F, Stagni V, Hussain A, Richelme S, Prodosmo A, Moumen A, Brun C, del Barco Barrantes I, Arthur JS, Koleske AJ, Nebreda AR, Barilà D, Maina F. Met acts through Abl to regulate p53 transcriptional outcomes and cell survival in the developing liver. Journal Of Hepatology 2012, 57: 1292-1298. PMID: 22889954, PMCID: PMC3571726, DOI: 10.1016/j.jhep.2012.07.044.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell SurvivalCyclin-Dependent Kinase Inhibitor p21HepatocytesLiverMiceP38 Mitogen-Activated Protein KinasesPhosphorylationProto-Oncogene Proteins c-ablProto-Oncogene Proteins c-bcl-2Proto-Oncogene Proteins c-mdm2Proto-Oncogene Proteins c-metTranscription, GeneticTumor Suppressor Protein p53ConceptsHepatocyte survivalRT-PCR arrayHGF/METEmbryonic liverCell survivalP53 transcriptional responseP53 axisP53-dependent cell deathEmbryonic hepatocytesMdm2 upregulationAbstractTextPathway modulationLiverP53 pathwaySurvivalMetSSurvival propertiesTranscriptional responseSurvival genesDeathAIMSCell deathP53 phosphorylationPresent studyP38MAPKThe Abl and Arg Kinases Mediate Distinct Modes of Phagocytosis and Are Required for Maximal Leishmania Infection
Wetzel DM, McMahon-Pratt D, Koleske AJ. The Abl and Arg Kinases Mediate Distinct Modes of Phagocytosis and Are Required for Maximal Leishmania Infection. Molecular And Cellular Biology 2012, 32: 3176-3186. PMID: 22665498, PMCID: PMC3434515, DOI: 10.1128/mcb.00086-12.Peer-Reviewed Original ResearchConceptsComplement receptor 3Leishmania infectionIgG-coated beadsMurine cutaneous leishmaniasisPotential therapeutic targetLeishmania uptakeVisceral diseaseObligate intracellular parasitesCutaneous leishmaniasisTherapeutic targetFc receptorsAmastigote uptakeTreatment resultsReceptor 3Small lesionsInfection severityLeishmania amazonensisKinase inhibitorsIntracellular parasitesBead phagocytosisPhagocytosisReceptorsC3biInfectionLeishmaniasisArg/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 aberrationsKinaseGenes
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 ResearchMeSH Keywords3T3 CellsActin CytoskeletonActomyosinAnimalsCell AdhesionCytoskeletonFibroblastsFocal AdhesionsMiceMyosin Light ChainsProtein-Tyrosine KinasesProto-Oncogene Proteins c-ablStress FibersConceptsCell 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 elementsP120Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function
Ko HS, Lee Y, Shin JH, Karuppagounder SS, Gadad BS, Koleske AJ, Pletnikova O, Troncoso JC, Dawson VL, Dawson TM. Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 16691-16696. PMID: 20823226, PMCID: PMC2944759, DOI: 10.1073/pnas.1006083107.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCell DeathCell LineDopamineGene Knockout TechniquesHumansIn Vitro TechniquesMiceMice, KnockoutMolecular Sequence DataMutationNeuronsParkinson DiseasePC12 CellsPhosphorylationProto-Oncogene Proteins c-ablRatsRecombinant Fusion ProteinsStress, PhysiologicalUbiquitinationUbiquitin-Protein LigasesConceptsParkinson's diseaseTreatment of PDSTI-571Postmortem PD brainsSporadic Parkinson's diseaseC-AblProtective functionNonreceptor tyrosine kinase c-AblMPTP intoxicationUbiquitin E3 ligase activityNeuroprotective approachesPD brainsSubstantia nigraDopaminergic neurotoxinProtective effectProtein type 2Subsequent neurotoxicityNervous systemType 2Parkin inactivationAutosomal recessive Parkinson's diseaseConditional knockoutKinase inhibitorsRecessive Parkinson's diseaseTyrosine kinase c-AblSynaptic 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 kinase
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 ResearchMeSH KeywordsAnimalsCell MovementCytoskeletonHumansMorphogenesisMultigene FamilyProtein Structure, TertiaryProto-Oncogene Proteins c-ablSignal TransductionConceptsAbl 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
T cell survival and function requires the c-Abl tyrosine kinase
Silberman I, Sionov RV, Zuckerman V, Haupt S, Goldberg Z, Strasser A, Ben-Sasson ZS, Baniyash M, Koleske AJ, Haupt Y. T cell survival and function requires the c-Abl tyrosine kinase. Cell Cycle 2008, 7: 3847-3857. PMID: 19098427, PMCID: PMC3407662, DOI: 10.4161/cc.7.24.7267.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtrophyCell DeathDisease SusceptibilityInterleukin-2LymphopeniaMiceMice, KnockoutMitogensNeoplasm TransplantationProto-Oncogene Proteins c-ablT-LymphocytesConceptsT cellsThymic atrophyT cell numbersAnti-tumor antibodiesAdult T-cellT cell functionT cell survivalDeficient T cellsTumor cell killingLck-Cre transgeneSyngeneic tumorsCell-autonomous roleEarly deathImmune systemIncreased susceptibilityMiceImpaired abilityCell functionAtrophyCell killingCell numberSurvivalOxidative stress stimuliCell survivalRole of AblEnhancement 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