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
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 cellsNck1Cofilin
2007
Dissecting 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 disordersInteractionHallmarkInhibitorsTarget
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