2018
Transient inhibition of p53 homologs protects ovarian function from two distinct apoptotic pathways triggered by anticancer therapies
Kim SY, Nair DM, Romero M, Serna VA, Koleske AJ, Woodruff TK, Kurita T. Transient inhibition of p53 homologs protects ovarian function from two distinct apoptotic pathways triggered by anticancer therapies. Cell Death & Differentiation 2018, 26: 502-515. PMID: 29988075, PMCID: PMC6370889, DOI: 10.1038/s41418-018-0151-2.Peer-Reviewed Original ResearchConceptsDistinct apoptotic pathwaysDNA damage responseDamage-induced apoptosisTemporary repressionPhosphorylation of ATMOocyte-specific deletionActivation/phosphorylationKinase inhibitorsCDDP-induced apoptosisDamage responseMultiple kinasesMolecular basisP53 homologApoptotic pathwayNovel pathwayAbl kinase inhibitorsOvarian functionApoptosisPathwayRepressionTAp63αPhosphorylationOocytesATRImmature oocytes
2017
Brain Region and Isoform-Specific Phosphorylation Alters Kalirin SH2 Domain Interaction Sites and Calpain Sensitivity
Miller MB, Yan Y, Machida K, Kiraly DD, Levy AD, Wu YI, Lam TT, Abbott T, Koleske AJ, Eipper BA, Mains RE. Brain Region and Isoform-Specific Phosphorylation Alters Kalirin SH2 Domain Interaction Sites and Calpain Sensitivity. ACS Chemical Neuroscience 2017, 8: 1554-1569. PMID: 28418645, PMCID: PMC5517348, DOI: 10.1021/acschemneuro.7b00076.Peer-Reviewed Original ResearchConceptsLong-term potentiationCalpain sensitivityEffects of cocaineRat nucleus accumbensAdult rat nucleus accumbensRho GDP/GTP exchange factorRegion-specific effectsChronic cocaineNucleus accumbensSynaptic functionBrain regionsKALRN geneSpine morphologyPrefrontal cortexKal7CocainePotentiationFunctional significanceCalpainPhosphorylation
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
β1 integrin regulates Arg to promote invadopodial maturation and matrix degradation
Beaty BT, Sharma VP, Bravo-Cordero JJ, Simpson MA, Eddy RJ, Koleske AJ, Condeelis J. β1 integrin regulates Arg to promote invadopodial maturation and matrix degradation. Molecular Biology Of The Cell 2013, 24: 1661-1675. PMID: 23552693, PMCID: PMC3667720, DOI: 10.1091/mbc.e12-12-0908.Peer-Reviewed Original ResearchMeSH KeywordsActin Depolymerizing FactorsActinsCell Line, TumorCell MovementCortactinExtracellular MatrixGene Expression Regulation, NeoplasticHumansIntegrin beta1PhosphorylationProtein BindingProtein MultimerizationProtein-Tyrosine KinasesPseudopodiaRNA, Small InterferingSignal TransductionTyrosineConceptsΒ1 integrinBarbed end formationInvasive membrane protrusionsMatrix degradationΒ1 integrin activationMature invadopodiaInvadopodial functionMetastatic human breast cancer cellsMembrane protrusionsExtracellular matrix degradationCortactin phosphorylationTyrosine 421InvadopodiaIntegrin activationMatrix proteolysisHuman breast cancer cellsThree-dimensional matrixPrecursor maturationBreast cancer cellsMetastatic tumor cellsIntegrinsCancer cellsPhosphorylationMaturationFundamental role
2011
Cortactin phosphorylation regulates cell invasion through a pH-dependent pathway
Magalhaes MA, Larson DR, Mader CC, Bravo-Cordero JJ, Gil-Henn H, Oser M, Chen X, Koleske AJ, Condeelis J. Cortactin phosphorylation regulates cell invasion through a pH-dependent pathway. Journal Of Cell Biology 2011, 195: 903-920. PMID: 22105349, PMCID: PMC3257566, DOI: 10.1083/jcb.201103045.Peer-Reviewed Original ResearchMeSH KeywordsActin Depolymerizing FactorsAdaptor Proteins, Signal TransducingCation Transport ProteinsCell Line, TumorCell Surface ExtensionsCortactinHumansHydrogen-Ion ConcentrationModels, BiologicalNeoplasm InvasivenessOncogene ProteinsPhosphorylationSodium-Hydrogen Exchanger 1Sodium-Hydrogen ExchangersConceptsCortactin phosphorylationCell invasionInvadopodia maturationCortactin tyrosine phosphorylationPH-dependent regulationInvasive protrusionsPH-dependent pathwayCofilin activityCofilin regulationTyrosine phosphorylationExchanger NHE1Cofilin activationPhosphorylationInvadopodiaProteolytic activityPrecise mechanismInvasionNHE1RegulationDynamic cyclePathwayMaturationTumor cellsNck1CofilinAn EGFR–Src–Arg–Cortactin Pathway Mediates Functional Maturation of Invadopodia and Breast Cancer Cell Invasion
Mader CC, Oser M, Magalhaes MA, Bravo-Cordero JJ, Condeelis J, Koleske AJ, Gil-Henn H. An EGFR–Src–Arg–Cortactin Pathway Mediates Functional Maturation of Invadopodia and Breast Cancer Cell Invasion. Cancer Research 2011, 71: 1730-1741. PMID: 21257711, PMCID: PMC3057139, DOI: 10.1158/0008-5472.can-10-1432.Peer-Reviewed Original ResearchConceptsBreast cancer cell invasionActin polymerizationCancer cell invasionInvadopodium maturationCell invasionCortactin phosphorylationEGFR-SrcExtracellular matrixTumor cell invasionInvadopodia functionV-SrcProtein cortactinEpidermal growth factorKnockdown cellsInvadopodiaFunctional maturationMaster switchSrc overexpressionCandidate therapeutic targetInvasive carcinoma cellsECM degradationNovel mechanismPhosphorylationNovel mediatorArg activation
2010
Specific tyrosine phosphorylation sites on cortactin regulate Nck1-dependent actin polymerization in invadopodia
Oser M, Mader CC, Gil-Henn H, Magalhaes M, Bravo-Cordero JJ, Koleske AJ, Condeelis J. Specific tyrosine phosphorylation sites on cortactin regulate Nck1-dependent actin polymerization in invadopodia. Journal Of Cell Science 2010, 123: 3662-3673. PMID: 20971703, PMCID: PMC3037016, DOI: 10.1242/jcs.068163.Peer-Reviewed Original ResearchConceptsTyrosine phosphorylation sitesTumor cell invasionActin polymerizationPhosphorylation sitesCell invasionTyrosine 421Actin barbed endsPhosphorylation of tyrosineRegulatory switchSH2 domainMembrane protrusionsInvadopodiaCrucial residuesCortactinBarbed endsDirect bindingInvasive carcinoma cellsPhosphorylationNck1Carcinoma cellsFRET interactionsInvasionCellsPhosphotyrosineSitesRegulation 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
Cortactin regulates cofilin and N-WASp activities to control the stages of invadopodium assembly and maturation
Oser M, Yamaguchi H, Mader CC, Bravo-Cordero JJ, Arias M, Chen X, DesMarais V, van Rheenen J, Koleske AJ, Condeelis J. Cortactin regulates cofilin and N-WASp activities to control the stages of invadopodium assembly and maturation. Journal Of Cell Biology 2009, 186: 571-587. PMID: 19704022, PMCID: PMC2733743, DOI: 10.1083/jcb.200812176.Peer-Reviewed Original ResearchMeSH KeywordsActin Depolymerizing FactorsActin-Related Protein 2-3 ComplexActinsAdaptor Proteins, Signal TransducingAnimalsCell Line, TumorCortactinEpidermal Growth FactorExtracellular MatrixHumansMammary Neoplasms, AnimalMatrix Metalloproteinase 14Neoplasm InvasivenessOncogene Protein pp60(v-src)Oncogene ProteinsPhosphorylationProtein Structure, TertiaryRatsRecombinant Fusion ProteinsRNA, Small InterferingTyrosineWiskott-Aldrich Syndrome Protein, NeuronalConceptsInvadopodium assemblyActin polymerizationCortactin phosphorylationArp2/3 complex-dependent actin polymerizationArp2/3-dependent actin polymerizationComplex-dependent actin polymerizationBarbed end formationN-WASP activityCarcinoma cellsMembrane protrusionsEnd formationSevering activityInvadopodiaMaster switchActin filamentsBarbed endsCortactinInvasive carcinoma cellsMetastatic carcinoma cellsNovel mechanismPhosphorylationCofilinMatrix degradationMaturationAssemblyArg 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
2007
A 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
2006
Integrin Signaling through Arg Activates p190RhoGAP by Promoting Its Binding to p120RasGAP and Recruitment to the Membrane
Bradley WD, Hernández SE, Settleman J, Koleske AJ. Integrin Signaling through Arg Activates p190RhoGAP by Promoting Its Binding to p120RasGAP and Recruitment to the Membrane. Molecular Biology Of The Cell 2006, 17: 4827-4836. PMID: 16971514, PMCID: PMC1635390, DOI: 10.1091/mbc.e06-02-0132.Peer-Reviewed Original ResearchConceptsCell peripheryP120 bindingGene Tyrosine KinaseRho family GTPases RhoAActin stress fibersIntegrin-mediated adhesionWild-type fibroblastsP190 phosphorylationFocal adhesionsGTPases RhoARho activityStress fibersEssential effectorTyrosine kinaseAdhesive environmentCell attachmentP190P120P190RhoGAPP120RasGAPPhosphorylationComplex formationBindingRecruitmentRho
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 brainAbl-dependent tyrosine phosphorylation of Sos-1 mediates growth-factor-induced Rac activation
Sini P, Cannas A, Koleske AJ, Di Fiore PP, Scita G. Abl-dependent tyrosine phosphorylation of Sos-1 mediates growth-factor-induced Rac activation. Nature Cell Biology 2004, 6: 268-274. PMID: 15039778, DOI: 10.1038/ncb1096.Peer-Reviewed Original ResearchConceptsGuanine nucleotide exchange factorsSos-1Rac activationTyrosine phosphorylationFunction of RacNon-receptor tyrosine kinase AblActin cytoskeleton remodellingNucleotide exchange factorsRac-GEF activityTyrosine kinase AblActivation of RTKsActivity of RacReceptor tyrosine kinasesCytoskeleton remodellingActin remodellingSignal transductionMolecular connectionMolecular mechanismsTyrosine kinaseBcr-Abl oncoproteinRacPharmacological interferencePhosphorylationGrowth factorABL signals
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 family
2001
The 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