2017
Kv3 Channels: Enablers of Rapid Firing, Neurotransmitter Release, and Neuronal Endurance
Kaczmarek LK, Zhang Y. Kv3 Channels: Enablers of Rapid Firing, Neurotransmitter Release, and Neuronal Endurance. Physiological Reviews 2017, 97: 1431-1468. PMID: 28904001, PMCID: PMC6151494, DOI: 10.1152/physrev.00002.2017.Peer-Reviewed Original ResearchConceptsKv3 channelsAuditory brain stem neuronsNeurotransmitter releaseBrain stem neuronsOngoing neuronal activityFire action potentialsHigh-frequency firingChannel genesStem neuronsGABAergic interneuronsMultiple protein isoformsCertain neuronsProtein-protein interactionsNeuronal activityNeuronal functionAlzheimer's diseaseNeurological disordersAction potentialsPurkinje cellsUnique expression patternKv3 familyNeuronsAbnormal regulationProtein isoformsProtein kinase
2016
Kv3.3 Channels Bind Hax-1 and Arp2/3 to Assemble a Stable Local Actin Network that Regulates Channel Gating
Zhang Y, Zhang XF, Fleming MR, Amiri A, El-Hassar L, Surguchev AA, Hyland C, Jenkins DP, Desai R, Brown MR, Gazula VR, Waters MF, Large CH, Horvath TL, Navaratnam D, Vaccarino FM, Forscher P, Kaczmarek LK. Kv3.3 Channels Bind Hax-1 and Arp2/3 to Assemble a Stable Local Actin Network that Regulates Channel Gating. Cell 2016, 165: 434-448. PMID: 26997484, PMCID: PMC4826296, DOI: 10.1016/j.cell.2016.02.009.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3Adaptor Proteins, Signal TransducingAmino Acid SequenceCell MembraneMolecular Sequence DataMutationNeuronsPluripotent Stem CellsRac GTP-Binding ProteinsShaw Potassium ChannelsSignal TransductionSpinocerebellar AtaxiasConceptsCytoplasmic C-terminusProline-rich domainPlasma membraneHAX-1Actin nucleationC-terminusCortical actin filament networkLocal actin networkStem cell-derived neuronsActin filament networkCell-derived neuronsAnti-apoptotic proteinsActin cytoskeletonKv3.3 potassium channelActin assemblyActin structuresActin networkArp2/3Channel gatingFilament networkGrowth conesCerebellar neurodegenerationKv3.3TerminusPotassium channels
2008
Amino‐termini isoforms of the Slack K+ channel, regulated by alternative promoters, differentially modulate rhythmic firing and adaptation
Brown MR, Kronengold J, Gazula V, Spilianakis CG, Flavell RA, Von Hehn CA, Bhattacharjee A, Kaczmarek LK. Amino‐termini isoforms of the Slack K+ channel, regulated by alternative promoters, differentially modulate rhythmic firing and adaptation. The Journal Of Physiology 2008, 586: 5161-5179. PMID: 18787033, PMCID: PMC2652154, DOI: 10.1113/jphysiol.2008.160861.Peer-Reviewed Original ResearchAction PotentialsAdaptation, PhysiologicalAmino Acid SequenceAnimalsBrainCloning, MolecularGene Expression RegulationMiceMice, Inbred C57BLMolecular Sequence DataNerve Tissue ProteinsNeuronsPotassium ChannelsPotassium Channels, Sodium-ActivatedPromoter Regions, GeneticProtein IsoformsRatsRNA, MessengerProtein Kinase C Modulates Inactivation of Kv3.3 Channels*
Desai R, Kronengold J, Mei J, Forman SA, Kaczmarek LK. Protein Kinase C Modulates Inactivation of Kv3.3 Channels*. Journal Of Biological Chemistry 2008, 283: 22283-22294. PMID: 18539595, PMCID: PMC2494927, DOI: 10.1074/jbc.m801663200.Peer-Reviewed Original Research
2006
Functional analysis of a novel potassium channel (KCNA1) mutation in hereditary myokymia
Chen H, von Hehn C, Kaczmarek LK, Ment LR, Pober BR, Hisama FM. Functional analysis of a novel potassium channel (KCNA1) mutation in hereditary myokymia. Neurogenetics 2006, 8: 131-135. PMID: 17136396, PMCID: PMC1820748, DOI: 10.1007/s10048-006-0071-z.Peer-Reviewed Original ResearchConceptsEpisodic ataxiaAdditional clinical featuresAbsence of epilepsyPotassium channel mutationsVoltage-gated potassium channelsPotassium channel gene KCNA1Febrile illnessCerebral palsyClinical featuresExtensor plantarsNonconservative missense mutationElectrophysiological studiesVermiform movementsKv1.1 subunitsLoss of functionMotor delayMyokymiaAutosomal dominant traitPotassium channelsChannel mutationsNovel c.AtaxiaMutation analysisMissense mutationsMutant cRNA
2004
The Appearance of a Protein Kinase A-regulated Splice Isoform of slo Is Associated with the Maturation of Neurons That Control Reproductive Behavior*
Zhang Y, Joiner WJ, Bhattacharjee A, Rassendren F, Magoski NS, Kaczmarek LK. The Appearance of a Protein Kinase A-regulated Splice Isoform of slo Is Associated with the Maturation of Neurons That Control Reproductive Behavior*. Journal Of Biological Chemistry 2004, 279: 52324-52330. PMID: 15375169, DOI: 10.1074/jbc.m408543200.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsAplysiaCell DifferentiationCHO CellsCricetinaeCyclic AMP-Dependent Protein KinasesDNA, ComplementaryIn Vitro TechniquesLarge-Conductance Calcium-Activated Potassium ChannelsMolecular Sequence DataNeuronsPatch-Clamp TechniquesPotassium Channels, Calcium-ActivatedProtein IsoformsRecombinant ProteinsReproductionConceptsBag cell neuronsReproductive behaviorSlo geneConsensus phosphorylation sitesCell cDNA libraryProtein kinase ACell neuronsChinese hamster ovary cellsPhosphorylation sitesCatalytic subunitHamster ovary cellsAlternative transcriptsCDNA librarySplice isoformsKinase ABK channel activityMaturation of neuronsPKA inhibitorVoltage-dependent channelsOvary cellsBrief synaptic stimulationChannel activityMature neuronsIsoformsPKA
2003
Slick (Slo2.1), a Rapidly-Gating Sodium-Activated Potassium Channel Inhibited by ATP
Bhattacharjee A, Joiner WJ, Wu M, Yang Y, Sigworth FJ, Kaczmarek LK. Slick (Slo2.1), a Rapidly-Gating Sodium-Activated Potassium Channel Inhibited by ATP. Journal Of Neuroscience 2003, 23: 11681-11691. PMID: 14684870, PMCID: PMC6740956, DOI: 10.1523/jneurosci.23-37-11681.2003.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceAnimalsCells, CulturedChloridesCHO CellsCloning, MolecularCricetinaeElectric ConductivityHumansIon Channel GatingKineticsMolecular Sequence DataPotassium ChannelsPotassium Channels, Sodium-ActivatedRatsSequence AlignmentSodiumTissue DistributionXenopusThe Sodium-Activated Potassium Channel Is Encoded by a Member of the Slo Gene Family
Yuan A, Santi CM, Wei A, Wang Z, Pollak K, Nonet M, Kaczmarek L, Crowder CM, Salkoff L. The Sodium-Activated Potassium Channel Is Encoded by a Member of the Slo Gene Family. Neuron 2003, 37: 765-773. PMID: 12628167, DOI: 10.1016/s0896-6273(03)00096-5.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCaenorhabditis elegansCells, CulturedFemaleLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMolecular Sequence DataMultigene FamilyMutationNerve Tissue ProteinsOocytesPotassium ChannelsPotassium Channels, Calcium-ActivatedPotassium Channels, Sodium-ActivatedSequence Homology, Amino AcidSodiumXenopus
2002
Localization of the Slack potassium channel in the rat central nervous system
Bhattacharjee A, Gan L, Kaczmarek LK. Localization of the Slack potassium channel in the rat central nervous system. The Journal Of Comparative Neurology 2002, 454: 241-254. PMID: 12442315, DOI: 10.1002/cne.10439.Peer-Reviewed Original ResearchConceptsRat central nervous systemSlack potassium channelsChannel subunitsRat brain slicesCentral nervous systemRat brain membranesOnly cortical regionDeep cerebellar nucleiGiant presynaptic terminalSlo subunitWestern blot analysisSubstantia nigraTrigeminal systemImmunohistochemical studyMedial nucleusOculomotor nucleusReticular formationBrain slicesFrontal cortexOlfactory bulbPresynaptic terminalsRed nucleusNervous systemCerebellar nucleiBrain membranesProtein Kinase Modulation of a Neuronal Cation Channel Requires Protein–Protein Interactions Mediated by an Src homology 3 Domain
Magoski NS, Wilson GF, Kaczmarek LK. Protein Kinase Modulation of a Neuronal Cation Channel Requires Protein–Protein Interactions Mediated by an Src homology 3 Domain. Journal Of Neuroscience 2002, 22: 1-9. PMID: 11756482, PMCID: PMC6757624, DOI: 10.1523/jneurosci.22-01-00001.2002.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceAnimalsAplysiaCationsCells, CulturedIon Channel GatingIon ChannelsMacromolecular SubstancesMembrane PotentialsMolecular Sequence DataMultiprotein ComplexesNeuronsPatch-Clamp TechniquesPeptidesPhosphorylationProtein BindingProtein Kinase CSrc Homology DomainsConceptsProtein-protein interactionsSrc homology 3 domainProtein kinase CSH3 domainSH3 domain-mediated interactionsDomain-mediated interactionsIon channelsSrc SH3 domainProtein kinase modulationMultiprotein complexesPDZ domainAdaptor proteinProtein kinaseKinase modulationIon channel modulationKinase CMotif peptideCation channel activationKinaseChannel open probabilityCation channelsMembrane depolarizationChannel activationChannel modulationProtein
2001
Aplysia Ror Forms Clusters on the Surface of Identified Neuroendocrine Cells
McKay S, Hislop J, Scott D, Bulloch A, Kaczmarek L, Carew T, Sossin W. Aplysia Ror Forms Clusters on the Surface of Identified Neuroendocrine Cells. Molecular And Cellular Neuroscience 2001, 17: 821-841. PMID: 11358481, DOI: 10.1006/mcne.2001.0977.Peer-Reviewed Original ResearchMeSH KeywordsAge FactorsAmino Acid SequenceAnimalsAntibody SpecificityAplysiaBase SequenceCaenorhabditis elegans ProteinsCell CompartmentationCells, CulturedCloning, MolecularGanglia, InvertebrateImmunohistochemistryMolecular Sequence DataNeuronsNeurosecretory SystemsReceptor Protein-Tyrosine KinasesReceptor Tyrosine Kinase-like Orphan ReceptorsReceptors, Cell SurfaceRNA, MessengerConceptsBag cell neuronsNeuroendocrine bag cell neuronsROR receptorsCultured bag cell neuronsRegulation of growthReceptor tyrosine kinasesMarine mollusk Aplysia californicaPeripheral neuronal processesMollusk Aplysia californicaCellular polarityFunctional domainsTyrosine kinaseIntracellular organellesCell surfaceProteinNeuroendocrine cellsKinaseAplysia californicaRelease sitesNeuronal processesOrganellesNeuronal populationsForm clustersGanglionic neuropilReceptors
2000
Cloning and localization of the hyperpolarization-activated cyclic nucleotide-gated channel family in rat brain
Monteggia L, Eisch A, Tang M, Kaczmarek L, Nestler E. Cloning and localization of the hyperpolarization-activated cyclic nucleotide-gated channel family in rat brain. Brain Research 2000, 81: 129-139. PMID: 11000485, DOI: 10.1016/s0169-328x(00)00155-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCloning, MolecularCyclic Nucleotide-Gated Cation ChannelsHumansHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsIn Situ HybridizationIon ChannelsMaleMembrane PotentialsModels, MolecularMolecular Sequence DataMultigene FamilyMuscle ProteinsNerve Tissue ProteinsOrgan SpecificityPotassium ChannelsProtein Structure, SecondaryRatsRats, Sprague-DawleyRNA, MessengerSequence AlignmentSequence Homology, Amino AcidTranscription, GeneticConceptsRat brainLower brain stem nucleiNeuronal pacemaker activityPrincipal relay nucleiBrain stem nucleiVentral cochlear nucleusAdult rat brainFacial motor nucleusCerebral cortexMotor nucleusStem nucleiTrapezoid bodyCochlear nucleusMamillary bodiesMedial habenulaRelay nucleiHCN1 expressionHCN1-4Olfactory bulbPontine nucleiAdult brainRhythmic firingPacemaker activitySupraoptic nucleusHCN4 expression
1998
Formation of intermediate-conductance calcium-activated potassium channels by interaction of Slack and Slo subunits
Joiner W, Tang M, Wang L, Dworetzky S, Boissard C, Gan L, Gribkoff V, Kaczmarek L. Formation of intermediate-conductance calcium-activated potassium channels by interaction of Slack and Slo subunits. Nature Neuroscience 1998, 1: 462-469. PMID: 10196543, DOI: 10.1038/2176.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsElectric ConductivityIntermediate-Conductance Calcium-Activated Potassium ChannelsIsomerismLarge-Conductance Calcium-Activated Potassium ChannelsMolecular Sequence DataNerve Tissue ProteinsPotassium ChannelsPotassium Channels, Calcium-ActivatedPotassium Channels, Sodium-ActivatedConceptsCalcium-activated potassium channelsIntracellular calciumNervous systemIntermediate-conductance calcium-activated potassium channelsPotassium channelsLarge-conductance calcium-activated potassium channelsControl of excitabilitySlo subunitIntermediate conductance channelPotassium channel genesPharmacological propertiesIntermediate conductanceCytoplasmic calciumChannel subunitsSlo channelsSlack channelsChannel genesSingle-channel conductanceUnitary conductanceCalciumExcitabilitySLOSecretion
1997
hSK4, a member of a novel subfamily of calcium-activated potassium channels
Joiner W, Wang L, Tang M, Kaczmarek L. hSK4, a member of a novel subfamily of calcium-activated potassium channels. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 11013-11018. PMID: 9380751, PMCID: PMC23566, DOI: 10.1073/pnas.94.20.11013.Peer-Reviewed Original ResearchConceptsCalcium-activated potassium channelsSK channelsSmall-conductance calcium-activated potassium channelsPotassium channelsHSK4Novel subfamilyAdult animalsPredominant expressionLeucine zipper-like domainChinese hamster ovary cellsNonexcitable tissuesHamster ovary cellsChannel polypeptideOvary cellsLow homologyC-terminusHigh affinityUnknown functionLocalization of a high threshold potassium channel in the rat cochlear nucleus
Perney T, Kaczmarek L. Localization of a high threshold potassium channel in the rat cochlear nucleus. The Journal Of Comparative Neurology 1997, 386: 178-202. PMID: 9295146, DOI: 10.1002/(sici)1096-9861(19970922)386:2<178::aid-cne2>3.0.co;2-z.Peer-Reviewed Original ResearchConceptsCochlear nucleusBushy cellsKv3.1 mRNAKv3.1 channelsPotassium channelsDorsal cochlear nucleusRat cochlear nucleusVentral cochlear nucleusLarge synaptic potentialsTypes of neuronsProximal dendritesSynaptic potentialsAxon terminalsStained neuronsUnmyelinated axonsAuditory neuronsNeuronal firingOctopus cellsMultipolar cellsGiant cellsKv3.1 proteinNeuronsKv3.1Situ hybridizationImmunolabelingProperties and regulation of the minK potassium channel protein
Kaczmarek L, Blumenthal E. Properties and regulation of the minK potassium channel protein. Physiological Reviews 1997, 77: 627-641. PMID: 9234960, DOI: 10.1152/physrev.1997.77.3.627.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsMinK proteinSingle transmembrane segmentPotassium channel proteinChannel-forming subunitTransmembrane segmentsMink genesChannel proteinsSecond messengerAmino acidsKvLQT1 channelsXenopus oocytesProteinNative currentsEpithelial cellsMinK mRNAIon selectivityVoltage-dependent potassium currentsResultant channelPotassium currentStrong candidateCellsGenesSubunitsVestibular organsMessengerIdentification of a Vesicular Pool of Calcium Channels in the Bag Cell Neurons of Aplysia californica
White B, Kaczmarek L. Identification of a Vesicular Pool of Calcium Channels in the Bag Cell Neurons of Aplysia californica. Journal Of Neuroscience 1997, 17: 1582-1595. PMID: 9030618, PMCID: PMC6573390, DOI: 10.1523/jneurosci.17-05-01582.1997.Peer-Reviewed Original ResearchConceptsBag cell neuronsCalcium channel alpha1 subunitAplysia nervous systemProtein kinase CCell neuronsAplysia californicaBag cell clustersCalcium channelsChannel alpha1 subunitCell clustersVesicular channelsMembrane proteinsReverse-transcribed RNAVesicular localizationPlasma membraneEgg-laying hormoneMolecular mechanismsSubcellular distributionKinase CLysoTracker RedDense-core vesiclesAcidic organellesGrowth conesCalcium channel subtypesCalcium current modulation
1996
Insulin receptor in Aplysia neurons: characterization, molecular cloning, and modulation of ion currents
Jonas E, Knox R, Kaczmarek L, Schwartz J, Solomon D. Insulin receptor in Aplysia neurons: characterization, molecular cloning, and modulation of ion currents. Journal Of Neuroscience 1996, 16: 1645-1658. PMID: 8774433, PMCID: PMC6578688, DOI: 10.1523/jneurosci.16-05-01645.1996.Peer-Reviewed Original ResearchMeSH KeywordsAction PotentialsAmino Acid SequenceAnimalsAplysiaBase SequenceCalcium ChannelsCloning, MolecularDNA, ComplementaryElectrophysiologyImmunohistochemistryInsulinIon ChannelsMolecular ProbesMolecular Sequence DataNeuronsPotassium ChannelsProtein-Tyrosine KinasesReceptor, InsulinTissue DistributionConceptsBag cell neuronsInsulin receptorInsulin-like peptidesImmunocytochemical staining showCell neuronsTyrosine kinase receptorsVertebrate insulinsMolecular cloningHerbimycin ATyrosine residuesTyrosine kinaseKinase receptorsInsulin-like growth factor-1Factor 1Staining showsVoltage-clamped neuronsVoltage-dependent Ca2Growth factor-1Aplysia californicaAplysia neuronsNervous systemReceptorsAction potentialsNeuronsInsulin
1995
A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem
Ketchum K, Joiner W, Sellers A, Kaczmarek L, Goldstein S. A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem. Nature 1995, 376: 690-695. PMID: 7651518, DOI: 10.1038/376690a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCells, CulturedDNA PrimersDrosophilaMolecular Sequence DataOocytesPatch-Clamp TechniquesPotassiumPotassium ChannelsProtein ConformationRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSodiumXenopus laevisConceptsP domainPotassium channel proteinCaenorhabditis elegansCommon structural motifChannel proteinsPore domainCellular membranesPrimary structureExcised membrane patchesSignature sequencesFlow of ionsAmino acidsXenopus laevisSelective currentMembrane potentialStructural motifsMembrane patchesPotassium channelsExternal divalent cationsDivalent cationsFunctional propertiesElegansVoltage-dependent mannerGenomeDomain
1994
Autoactive peptides act at three distinct receptors to depolarize the bag cell neurons of Aplysia
Loechner K, Kaczmarek L. Autoactive peptides act at three distinct receptors to depolarize the bag cell neurons of Aplysia. Journal Of Neurophysiology 1994, 71: 195-203. PMID: 8158229, DOI: 10.1152/jn.1994.71.1.195.Peer-Reviewed Original Research