2018
Cortactin stabilization of actin requires actin-binding repeats and linker, is disrupted by specific substitutions, and is independent of nucleotide state
Scherer AN, Anand NS, Koleske AJ. Cortactin stabilization of actin requires actin-binding repeats and linker, is disrupted by specific substitutions, and is independent of nucleotide state. Journal Of Biological Chemistry 2018, 293: 13022-13032. PMID: 29929984, PMCID: PMC6109930, DOI: 10.1074/jbc.ra118.004068.Peer-Reviewed Original ResearchConceptsHematopoietic cell-specific Lyn substrate 1Nucleotide stateActin bindingActin filamentsTotal internal reflection fluorescence microscopyActin-binding proteins cortactinActin cosedimentation assaysActin-rich structuresHigh-affinity actin bindingADP-actin filamentsReflection fluorescence microscopyAdjacent linker regionActin filament bindingArp2/3 complexCortactin repeatsCellular functionsActin stabilityCosedimentation assaysActin stabilizationProtein cortactinLamellipodial protrusionGTPase regulatorFilament depolymerizationLinker regionActin depolymerization
2017
Neurodevelopmental disease-associated de novo mutations and rare sequence variants affect TRIO GDP/GTP exchange factor activity
Katrancha SM, Wu Y, Zhu M, Eipper BA, Koleske AJ, Mains RE. Neurodevelopmental disease-associated de novo mutations and rare sequence variants affect TRIO GDP/GTP exchange factor activity. Human Molecular Genetics 2017, 26: 4728-4740. PMID: 28973398, PMCID: PMC5886096, DOI: 10.1093/hmg/ddx355.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsDatabases, Nucleic AcidGuanine Nucleotide Exchange FactorsGuanosine DiphosphateGuanosine TriphosphateHEK293 CellsHumansMiceMice, KnockoutMutationNeurodevelopmental DisordersProtein DomainsProtein Serine-Threonine KinasesRac1 GTP-Binding ProteinRho GTP-Binding ProteinsRhoA GTP-Binding ProteinConceptsDe novo mutationsNeurodevelopmental disordersRare sequence variantsTriple functional domain proteinNovo mutationsComplex neurodevelopmental disorderBipolar disorderTherapeutic progressSequence variantsImpaired inhibitionProtein levelsDisordersMolecular pathwaysMillions of peopleIntellectual disabilityRare variantsNeurite outgrowthGenetic damageFactor activityMutationsExchange factor activityDistinct specificitiesPoor understandingRac1Activity
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 sensitivityKinase
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-AblRegulation 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
2008
Enhancement 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 structure
1995
Association of an activator with an RNA polymerase II holoenzyme.
Hengartner CJ, Thompson CM, Zhang J, Chao DM, Liao SM, Koleske AJ, Okamura S, Young RA. Association of an activator with an RNA polymerase II holoenzyme. Genes & Development 1995, 9: 897-910. PMID: 7774808, DOI: 10.1101/gad.9.8.897.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceGenes, FungalHerpes Simplex Virus Protein Vmw65Macromolecular SubstancesMediator ComplexModels, GeneticMolecular Sequence DataMutationPrecipitin TestsProtein BindingRestriction MappingRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Analysis, DNASuppression, GeneticTranscription FactorsTranscription, GeneticConceptsRNA polymerase II holoenzymeRNA polymerase IISRB proteinsPolymerase IIDomain of VP16General transcription factorsDirect interactionTranscription apparatusTranscriptional activatorMediators of activationTranscription initiationTranscription factorsImmunoprecipitation experimentsHoloenzymeGenesActivatorAffinity columnProteinSubcomplexPromoterVP16BindsInteractionHallmarkActivationA kinase–cyclin pair in the RNA polymerase II holoenzyme
Liao S, Zhang J, Jeffery D, Koleske A, Thompson C, Chao D, Viljoen M, van Vuuren H, Young R. A kinase–cyclin pair in the RNA polymerase II holoenzyme. Nature 1995, 374: 193-196. PMID: 7877695, DOI: 10.1038/374193a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCyclin-Dependent Kinase 8Cyclin-Dependent KinasesCyclinsFungal ProteinsMolecular Sequence DataMutationProtein Serine-Threonine KinasesRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTranscription FactorsTranscription, GeneticConceptsRNA polymerase II holoenzymeSRB proteinsKinase functionRNA polymerase II carboxy-terminal domainCyclin-like proteinGeneral transcription factorsRNA polymerase IISuppressors of mutationsNormal transcriptional responseCarboxy-terminal domainPolymerase IITranscriptional regulatorsTranscriptional responseGalactose inductionTranscription factorsRegulatory proteinsTranscription systemHoloenzymeRegulatory roleKinaseProteinBiochemical evidenceGenesVivoSrb11
1993
Quantitative Comparison of Initiation and Mutation Phenotypes in Hepatocytes of the Analbuminemic Rat
Dragan Y, Laufer C, Koleske A, Drinkwater N, Pilot H. Quantitative Comparison of Initiation and Mutation Phenotypes in Hepatocytes of the Analbuminemic Rat. Cancer Science 1993, 84: 175-183. PMID: 8463134, PMCID: PMC5919122, DOI: 10.1111/j.1349-7006.1993.tb02852.x.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