2010
Phosphorylation 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-Abl
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 degradationMaturationAssembly
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 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 ResearchMeSH Keywords3T3 CellsActinsAnimalsMiceMicroscopy, ElectronProtein BindingProtein-Tyrosine KinasesRecombinant Fusion ProteinsConceptsF-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 cooperativityArg
1998
Essential Roles for the Abl and Arg Tyrosine Kinases in Neurulation
Koleske A, Gifford A, Scott M, Nee M, Bronson R, Miczek K, Baltimore D. Essential Roles for the Abl and Arg Tyrosine Kinases in Neurulation. Neuron 1998, 21: 1259-1272. PMID: 9883720, DOI: 10.1016/s0896-6273(00)80646-7.Peer-Reviewed Original Research
1992
A novel transcription factor reveals a functional link between the RNA polymerase II CTD and TFIID
Koleske A, Buratowski S, Nonet M, Young R. A novel transcription factor reveals a functional link between the RNA polymerase II CTD and TFIID. Cell 1992, 69: 883-894. PMID: 1591782, DOI: 10.1016/0092-8674(92)90298-q.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBlotting, WesternChromatography, AffinityFungal ProteinsGenes, SuppressorMediator ComplexMolecular Sequence DataMutationRecombinant Fusion ProteinsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factor TFIIDTranscription FactorsTranscription, GeneticConceptsCarboxy-terminal domainRNA polymerase II carboxy-terminal domainNovel transcription factorTranscription initiation complexInitiation complexTranscription factorsFunctional linkConditional growth phenotypesTranscription initiation apparatusRNA polymerase IITATA-binding factorDominant suppressorsPolymerase IIGrowth phenotypeTranscription initiationGene expressionAllele specificitySRB2Truncation mutationsSame functionSimilar defectsTFIIDSuppressorEfficient establishmentMechanism of action