2014
Ablation of ErbB4 from excitatory neurons leads to reduced dendritic spine density in mouse prefrontal cortex
Cooper MA, Koleske AJ. Ablation of ErbB4 from excitatory neurons leads to reduced dendritic spine density in mouse prefrontal cortex. The Journal Of Comparative Neurology 2014, 522: 3351-3362. PMID: 24752666, PMCID: PMC4107058, DOI: 10.1002/cne.23615.Peer-Reviewed Original ResearchMeSH KeywordsAge FactorsAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Cell FractionationCells, CulturedDendritic SpinesDisks Large Homolog 4 ProteinGene Expression RegulationGreen Fluorescent ProteinsGuanylate KinasesMembrane ProteinsMiceMice, TransgenicMitogen-Activated Protein Kinase 3NestinNeuronsPrefrontal CortexReceptor, ErbB-4SynapsesTransfectionConceptsDendritic spine densitySpine densityExcitatory pyramidal cellsExcitatory neuronsPrefrontal cortexPyramidal cellsDendritic spinesErbB4 functionAblation of ErbB4Dendritic spine lossCortical neuronal culturesMouse prefrontal cortexDendritic spine developmentMonths of ageSynaptic plasma membrane preparationsSpine lossWeanling miceDorsomedial prefrontal cortexPsychiatric disordersKnockout miceMature spinesErbB4 signalingSynaptic plasticityNeuronal culturesDisease pathology
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
2004
The Abl-related gene (Arg) requires its F-actin–microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion
Miller AL, Wang Y, Mooseker MS, Koleske AJ. The Abl-related gene (Arg) requires its F-actin–microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion. Journal Of Cell Biology 2004, 165: 407-420. PMID: 15138293, PMCID: PMC2172189, DOI: 10.1083/jcb.200308055.Peer-Reviewed Original ResearchConceptsLamellipodial dynamicsCross-linking activityF-actin-binding domainFluorescent protein fusionsMT-binding domainNonreceptor tyrosine kinaseFilamentous actin bundlesWild-type fibroblastsCell polarityProtein fusionsMembrane protrusionsCell peripheryLamellipodial protrusionCell protrusionsActin bundlesMolecular mechanismsTyrosine kinaseF-actinMicrotubulesArgFibroblast adhesionABLHigh affinityFibroblastsProtrusion
1995
The RNA polymerase II holoenzyme and its implications for gene regulation
Koleske A, Young R. The RNA polymerase II holoenzyme and its implications for gene regulation. Trends In Biochemical Sciences 1995, 20: 113-116. PMID: 7709429, DOI: 10.1016/s0968-0004(00)88977-x.Peer-Reviewed Original ResearchConceptsRNA polymerase II holoenzymeTranscription initiation apparatusGeneral transcription factorsRNA polymerase holoenzymeGene regulationPol IIPolymerase holoenzymeTranscriptional regulatorsTranscription factorsB proteinGene expressionLarge complexesSRB componentsHoloenzymeRegulationRecent evidenceComplexesSuppressorRegulatorProteinExpression
1993
A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast
Thompson C, Koleske A, Chao D, Young R. A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast. Cell 1993, 73: 1361-1375. PMID: 8324825, DOI: 10.1016/0092-8674(93)90362-t.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesDNA Mutational AnalysisDNA-Binding ProteinsFungal ProteinsGene Expression RegulationMediator ComplexMolecular Sequence DataMultienzyme ComplexesRecombinant ProteinsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTranscription FactorsTranscription, GeneticConceptsTATA-binding proteinRNA polymerase II carboxy-terminal domainCarboxy-terminal domainMultisubunit complexLarge multisubunit complexFunctional preinitiation complexRNA polymerase IIEfficient transcription initiationTranscription initiation complexSRB proteinsCTD proteinsExtragenic suppressorsCTD functionPolymerase IIPreinitiation complexTranscription initiationInitiation complexComplex bindsTruncation mutationsSRB2Srb5ProteinBiochemical evidenceComplexesSRB4
1989
Phenobarbital-inducible Aldehyde Dehydrogenase in the Rat cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats
Dunn TJ, Koleske AJ, Lindahl R, Pitot HC. Phenobarbital-inducible Aldehyde Dehydrogenase in the Rat cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats. Journal Of Biological Chemistry 1989, 264: 13057-13065. PMID: 2753900, DOI: 10.1016/s0021-9258(18)51595-7.Peer-Reviewed Original ResearchConceptsComplete nucleotide sequenceSpecific gene expressionAldehyde dehydrogenaseAmino acid sequenceGlutathione S-transferase YaRat cDNA sequenceStrong conservationCDNA sequenceNucleotide sequenceMRNA speciesAcid sequenceGene expressionCytosolic isozymeMolecular massAmino acidsCytochrome P-450eMultiple pathwaysMRNAResponsive allelesMRNA levelsSequenceRegulationCytochrome P-450bDehydrogenaseP-450e