2023
Correction: Trio family proteins as regulators of cell migration and morphogenesis in development and disease – mechanisms and cellular contexts
Bircher J, Koleske A. Correction: Trio family proteins as regulators of cell migration and morphogenesis in development and disease – mechanisms and cellular contexts. Journal Of Cell Science 2023, 136 PMID: 36763488, PMCID: PMC11034500, DOI: 10.1242/jcs.260984.Peer-Reviewed Original Research
2021
Regulation of the NMDA receptor by its cytoplasmic domains: (How) is the tail wagging the dog?
Ishchenko Y, Carrizales MG, Koleske AJ. Regulation of the NMDA receptor by its cytoplasmic domains: (How) is the tail wagging the dog? Neuropharmacology 2021, 195: 108634. PMID: 34097949, PMCID: PMC8410658, DOI: 10.1016/j.neuropharm.2021.108634.Peer-Reviewed Original ResearchConceptsCarboxyl-terminal domainN-methyl-D-aspartate receptorsUnique modular architectureIntracellular C-tailAmino acid sequenceDocking motifAttention deficit hyperactivity disorderKnown proteinsCytoplasmic domainC-tailTerminal domainSequence homologyAcid sequenceSynapse developmentSynaptic targetingCovalent modificationGenetic variantsGlutamate receptor subunitsAllosteric modulationImportant functionsReceptor subunitsIntellectual disabilityMetabotropic signalingSubunitsProteinTrio family proteins as regulators of cell migration and morphogenesis in development and disease – mechanisms and cellular contexts
Bircher JE, Koleske AJ. Trio family proteins as regulators of cell migration and morphogenesis in development and disease – mechanisms and cellular contexts. Journal Of Cell Science 2021, 134: jcs248393. PMID: 33568469, PMCID: PMC7888718, DOI: 10.1242/jcs.248393.Peer-Reviewed Original ResearchConceptsFamily proteinsCellular contextProtein-protein interaction domainsHuman diseasesProtein trafficking pathwaysLarge multidomain proteinCell surface receptorsTrio proteinsUNC-73Cell morphogenesisProtein traffickingTrafficking pathwaysMultidomain proteinsInteraction domainInteraction partnersKey regulatorBiological contextTissue organizationCell migrationSurface receptorsProteinTrio familiesRecent discoveryMorphogenesisRegulator
2020
Functional interactions of ion channels with the actin cytoskeleton: does coupling to dynamic actin regulate NMDA receptors?
Shaw JE, Koleske AJ. Functional interactions of ion channels with the actin cytoskeleton: does coupling to dynamic actin regulate NMDA receptors? The Journal Of Physiology 2020, 599: 431-441. PMID: 32034761, PMCID: PMC7416480, DOI: 10.1113/jp278702.Peer-Reviewed Original ResearchConceptsActin cytoskeletonIon channelsPostsynaptic compartmentsCytoskeletal protein actinActin binding proteinsNeurotransmitter release machineryNeurotransmitter receptorsProtein actinSynaptic neurotransmitter receptorsΑ-actininMolecular mechanismsBinding proteinCytoskeletonMolecular linkageFunctional interactionRelease machineryDiverse collectionActinNMDA receptorsTraffickingChannel openingProteinVoltage-gated NaReceptorsCompartments
2019
Regulation of MT dynamics via direct binding of an Abl family kinase
Hu Y, Lyu W, Lowery LA, Koleske AJ. Regulation of MT dynamics via direct binding of an Abl family kinase. Journal Of Cell Biology 2019, 218: 3986-3997. PMID: 31699690, PMCID: PMC6891085, DOI: 10.1083/jcb.201812144.Peer-Reviewed Original ResearchConceptsAbl family kinasesC-terminal halfFamily kinasesMT dynamicsMT growthTubulin C-terminal tailsC-terminal tailStable reexpressionEssential regulatorCell shapeBinds microtubulesMT polymerizationAbl kinaseGenetic studiesDirect bindingFunctional interactionKinaseMicrotubulesABL2ReexpressionMT behaviorBindingRegulatorProteinGrowth
2018
Noonan Syndrome-Associated SHP2 Dephosphorylates GluN2B to Regulate NMDA Receptor Function
Levy AD, Xiao X, Shaw JE, Devi S, Katrancha SM, Bennett AM, Greer CA, Howe JR, Machida K, Koleske AJ. Noonan Syndrome-Associated SHP2 Dephosphorylates GluN2B to Regulate NMDA Receptor Function. Cell Reports 2018, 24: 1523-1535. PMID: 30089263, PMCID: PMC6234505, DOI: 10.1016/j.celrep.2018.07.006.Peer-Reviewed Original ResearchConceptsTyrosine phosphatase SHP2Noonan syndromePhosphatase SHP2Regulatory proteinsSHP2Recombinant GluN1Nck2Receptor functionNMDA receptor functionNMDAR functionGluN2B functionMutationsNMDAR dysfunctionNeuron functionNS miceGluN1ProteinAllelesNMDA receptorsDiheteromersReceptor kineticsReduced contributionsFunctionHyperactivationMice
2017
The repeat region of cortactin is intrinsically disordered in solution
Li X, Tao Y, Murphy JW, Scherer AN, Lam TT, Marshall AG, Koleske AJ, Boggon TJ. The repeat region of cortactin is intrinsically disordered in solution. Scientific Reports 2017, 7: 16696. PMID: 29196701, PMCID: PMC5711941, DOI: 10.1038/s41598-017-16959-1.Peer-Reviewed Original ResearchConceptsCortactin repeatsRepeat regionActin filamentsHydrogen-deuterium exchange mass spectrometryAdjacent helical regionsMulti-domain proteinsExchange mass spectrometryExtensive biophysical analysisCircular dichroismHydrophobic core regionSmall-angle X-ray scatteringBiophysical analysisHelical regionCortactinRepeatsSimilar copiesUnfolded peptidesProteinMotifSize exclusion chromatographyMass spectrometryFilamentsExclusion chromatographyX-ray scatteringRegion
2013
Metabotropic Glutamate Receptor 5 Is a Coreceptor for Alzheimer Aβ Oligomer Bound to Cellular Prion Protein
Um J, Kaufman A, Kostylev M, Heiss J, Stagi M, Takahashi H, Kerrisk M, Vortmeyer A, Wisniewski T, Koleske A, Gunther E, Nygaard H, Strittmatter S. Metabotropic Glutamate Receptor 5 Is a Coreceptor for Alzheimer Aβ Oligomer Bound to Cellular Prion Protein. Neuron 2013, 80: 531. DOI: 10.1016/j.neuron.2013.10.001.Peer-Reviewed Original Research
2012
Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin–Arg–lysozyme complex
Liu W, MacGrath SM, Koleske AJ, Boggon TJ. Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin–Arg–lysozyme complex. Acta Crystallographica Section F: Structural Biology Communications 2012, 68: 154-158. PMID: 22297987, PMCID: PMC3274391, DOI: 10.1107/s1744309111056132.Peer-Reviewed Original ResearchConceptsCrystal structure determinationNonreceptor tyrosine kinaseArg nonreceptor tyrosine kinaseHeterotrimeric complexSH3 domainMacromolecular crystallographersCrystallography approachStructure determinationTyrosine kinaseCocrystal structureMolecular replacementTrace amountsLysozyme complexStructure solutionProteinCortactinComplexesCrystallizationCrystallographersCocrystalsKinaseMotifAutomatic model buildingSequenceArg
2010
Mechanisms of Synapse and Dendrite Maintenance and Their Disruption in Psychiatric and Neurodegenerative Disorders
Lin YC, Koleske AJ. Mechanisms of Synapse and Dendrite Maintenance and Their Disruption in Psychiatric and Neurodegenerative Disorders. Annual Review Of Neuroscience 2010, 33: 349-378. PMID: 20367247, PMCID: PMC3063389, DOI: 10.1146/annurev-neuro-060909-153204.Peer-Reviewed Original Research
2009
Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts
Bradley WD, Koleske AJ. Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts. Journal Of Cell Science 2009, 122: 3441-3454. PMID: 19759284, PMCID: PMC2746129, DOI: 10.1242/jcs.039859.Peer-Reviewed Original ResearchConceptsAbl family kinasesNon-receptor tyrosine kinaseWAVE family proteinsCell-specific proteinsActivation of cortactinExtracellular cuesEpithelial morphogenesisAdhesion dynamicsCytoskeletal rearrangementsEssential regulatorPhysiological contextCell motilityActin polymerizationCytoskeletal changesPhysiological processesTyrosine kinaseGenetic studiesKinaseMorphogenesisCell contractilityCell migrationProteinComplex processImmune systemCytoskeleton
2004
The Arg Non-receptor Tyrosine Kinase Modifies F-actin Structure
Galkin VE, Orlova A, Koleske AJ, Egelman EH. The Arg Non-receptor Tyrosine Kinase Modifies F-actin Structure. Journal Of Molecular Biology 2004, 346: 565-575. PMID: 15670605, DOI: 10.1016/j.jmb.2004.11.078.Peer-Reviewed Original ResearchConceptsSubdomain 1Domain bindsActin filamentsF-actinSingle particle image analysisActin-bundling activityNon-receptor tyrosine kinaseCalponin homology domainActin-binding domainF-actin structuresActin subdomain 1Homology domainAbl familyCH domainCell motilityAdjacent protomersTyrosine kinaseParticle image analysisActin protomersConformational changesCooperative bindingARG proteinProtomersArgProteinHow do Abl family kinases regulate cell shape and movement?
Hernández SE, Krishnaswami M, Miller AL, Koleske AJ. How do Abl family kinases regulate cell shape and movement? Trends In Cell Biology 2004, 14: 36-44. PMID: 14729179, DOI: 10.1016/j.tcb.2003.11.003.Peer-Reviewed Original ResearchConceptsAbl family kinasesFamily kinasesAdhesion receptorsC-terminal halfCytoskeletal regulatory proteinsNonreceptor tyrosine kinaseCell morphogenesisCytoskeletal dynamicsRecent biochemicalCytoskeletal rearrangementsCytoskeletal structuresCytoskeletal componentsRegulatory proteinsCell shapeGenetic analysisTyrosine kinaseKinaseCell surfaceARG proteinRelay signalsProteinLeukemia cellsDrosophilaCrystallographic analysisMorphogenesis
2003
Phospholipids Can Switch the GTPase Substrate Preference of a GTPase-activating Protein*
Ligeti E, Dagher MC, Hernandez SE, Koleske AJ, Settleman J. Phospholipids Can Switch the GTPase Substrate Preference of a GTPase-activating Protein*. Journal Of Biological Chemistry 2003, 279: 5055-5058. PMID: 14699145, DOI: 10.1074/jbc.c300547200.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsSmall GTPasesSubstrate preferencePotent GTPase-activating proteinMajor cellular inhibitorActivity of GTPasesNovel regulatory mechanismLikely physiological roleRacGAP activityIntrinsic GTPRhoGAP activityP190 RhoGAPCellular inhibitorRac GTPasesGTPasesRegulatory mechanismsPhysiological roleProteinPhospholipidsFatty acidsRhoGAPGTPP190ActivityRhoDo Filopodia Enable the Growth Cone to Find Its Way?
Koleske AJ. Do Filopodia Enable the Growth Cone to Find Its Way? Science Signaling 2003, 2003: pe20. PMID: 12759482, DOI: 10.1126/stke.2003.183.pe20.Peer-Reviewed Original ResearchConceptsEna/VASP proteinsVASP proteinsEna/VASP family proteinsGrowth conesActin filament elongationNeuronal growth conesGrowth cone filopodiaCaenorhabditis elegansFamily proteinsFilament elongationAxon guidanceSensory organsFilopodiaGuidance cuesNonneuronal cellsProteinDrosophilaElegansLamellipodiaNervous system
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
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 columnProteinSubcomplexPromoterVP16BindsInteractionHallmarkActivationThe 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 evidenceComplexesSuppressorRegulatorProteinExpressionA 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 evidenceGenesVivoSrb11Caveolae, transmembrane signalling and cellular transformation
Lisanti M, Tang Z, Scherer P, Kübler E, Koleske A, Sargiacomo M. Caveolae, transmembrane signalling and cellular transformation. Molecular Membrane Biology 1995, 12: 121-124. PMID: 7767370, DOI: 10.3109/09687689509038506.Peer-Reviewed Original ResearchConceptsCaveolin-rich membrane domainsV-Src substrateCaveolar marker proteinCaveolar functionSmall moleculesMembrane domainsCellular transformationPlasma membraneCaveolaeMarker proteinsCultured cellsCapillary endothelial cellsProteinEndothelial cellsCellsMembraneCaveolinTransmembraneCytoplasmGPITranslocationElectron micrographsMoleculesWide varietyTranscytosis