2012
Regulation of Neuronal Excitability by Interaction of Fragile X Mental Retardation Protein with Slack Potassium Channels
Zhang Y, Brown MR, Hyland C, Chen Y, Kronengold J, Fleming MR, Kohn AB, Moroz LL, Kaczmarek LK. Regulation of Neuronal Excitability by Interaction of Fragile X Mental Retardation Protein with Slack Potassium Channels. Journal Of Neuroscience 2012, 32: 15318-15327. PMID: 23115170, PMCID: PMC3518385, DOI: 10.1523/jneurosci.2162-12.2012.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnisomycinAplysiaCHO CellsCloning, MolecularCricetinaeCricetulusElectrophysiological PhenomenaFragile X Mental Retardation ProteinImmunohistochemistryImmunoprecipitationNeuronsPatch-Clamp TechniquesPotassium ChannelsProtein Synthesis InhibitorsRNA InterferenceRNA, Small InterferingSodiumSynapsesConceptsNeuronal excitabilitySlack potassium channelsTetrodotoxin-sensitive componentCurrent-clamp recordingsSlack channelsMental retardation proteinBag cell neuronsSustained componentIntracellular injectionNeuronal firingInhibitory periodSynaptic stimulationPotassium currentCell neuronsAction potentialsOutward currentsPotassium channelsProlonged changesNeuronsAplysia bag cell neuronsProtein synthesis inhibitor anisomycinExcitabilityFragile X Mental Retardation ProteinCommon formIntellectual disability
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, Messenger
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 DistributionXenopus
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
1999
Cell Type‐Specific Expression of the Kv3.1 Gene Is Mediated by a Negative Element in the 5′ Untranslated Region of the Kv3.1 Promoter
Gan L, Hahn S, Kaczmarek L. Cell Type‐Specific Expression of the Kv3.1 Gene Is Mediated by a Negative Element in the 5′ Untranslated Region of the Kv3.1 Promoter. Journal Of Neurochemistry 1999, 73: 1350-1362. PMID: 10501178, DOI: 10.1046/j.1471-4159.1999.0731350.x.Peer-Reviewed Original ResearchMeSH Keywords3T3 Cells5' Untranslated RegionsAnimalsBase SequenceBeta-GalactosidaseBrainCell LineCHO CellsCloning, MolecularCricetinaeGene Expression RegulationGliomaHumansMiceMice, TransgenicMolecular Sequence DataNeuropeptidesOrgan SpecificityPC12 CellsPotassium ChannelsPotassium Channels, Voltage-GatedPromoter Regions, GeneticRatsRecombinant Fusion ProteinsRegulatory Sequences, Nucleic AcidRNA, MessengerShaw Potassium ChannelsTranscription, GeneticTransfectionConceptsType-specific expressionUntranslated regionCell type-specific enhancersCell type-specific expressionCell linesTissue-specific expressionThymidine kinase promoterCell-type specificityTransient transfection assaysKv3.1 potassium channel genePotassium channel genesKv3.1 geneDifferent tissue originsRegulatory fragmentDeletion analysisRegulatory regionsTranscriptional mechanismsTransgenic miceTransfection assaysKinase promoterFunctional analysisChannel genesType specificityPromoterGenes
1998
When, where, and how much? Expression of the Kv3.1 potassium channel in high‐frequency firing neurons
Gan L, Kaczmarek L. When, where, and how much? Expression of the Kv3.1 potassium channel in high‐frequency firing neurons. Developmental Neurobiology 1998, 37: 69-79. PMID: 9777733, DOI: 10.1002/(sici)1097-4695(199810)37:1<69::aid-neu6>3.0.co;2-6.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsAuditory brain stem neuronsVoltage-dependent potassium currentsBrain stem neuronsHigh-frequency firing neuronsKv3.1 potassium channelStem neuronsKv3.1 potassium channel geneLong-term regulationSynaptic inputsPotassium currentPotassium channel genesNeuronsPotassium channelsKv3.1 geneKv3.1 subunitsFiring neuronsHigh frequencyChannel genesCurrent knowledgeChannels altersTranscriptional mechanismsCell-type specificityExpressionGene transcriptionExtrinsic factors
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 function
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 potentialsNeuronsInsulinCloning and Characterization of the Promoter for a Potassium Channel Expressed in High Frequency Firing Neurons (∗)
Gan L, Perney T, Kaczmarek L. Cloning and Characterization of the Promoter for a Potassium Channel Expressed in High Frequency Firing Neurons (∗). Journal Of Biological Chemistry 1996, 271: 5859-5865. PMID: 8621457, DOI: 10.1074/jbc.271.10.5859.Peer-Reviewed Original Research3T3 Cells8-Bromo Cyclic Adenosine MonophosphateAnimalsBase SequenceBinding SitesBucladesineCell DifferentiationChloramphenicol O-AcetyltransferaseCloning, MolecularCyclic AMPDNA PrimersDNA, ComplementaryFibroblastsGene ExpressionGenomic LibraryIonomycinKineticsMiceMolecular Sequence DataNeuronsNeuropeptidesPC12 CellsPlasmidsPodophyllinPodophyllotoxinPotassium ChannelsPotassium Channels, Voltage-GatedPromoter Regions, GeneticRatsRecombinant ProteinsRegulatory Sequences, Nucleic AcidRestriction MappingSequence DeletionShaw Potassium ChannelsTransfection
1994
A shab potassium channel contributes to action potential broadening in peptidergic neurons
Quattrocki E, Marshall J, Kaczmarek L. A shab potassium channel contributes to action potential broadening in peptidergic neurons. Neuron 1994, 12: 73-86. PMID: 8292361, DOI: 10.1016/0896-6273(94)90153-8.Peer-Reviewed Original ResearchMeSH KeywordsAction PotentialsAmino Acid SequenceAnimalsAplysiaBase SequenceCloning, MolecularDNA, ComplementaryFemaleInvertebrate HormonesKineticsMathematicsModels, TheoreticalMolecular Sequence DataNeuronsOocytesPolymerase Chain ReactionPotassiumPotassium ChannelsShab Potassium ChannelsTetraethylammoniumTetraethylammonium CompoundsTranscription, GeneticXenopus laevis
1991
Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator.
Marshall J, Martin K, Picciotto M, Hockfield S, Nairn A, Kaczmarek L. Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator. Journal Of Biological Chemistry 1991, 266: 22749-22754. PMID: 1718999, DOI: 10.1016/s0021-9258(18)54631-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCell MembraneCloning, MolecularCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNADogfishHumansImmunoenzyme TechniquesMembrane ProteinsMolecular Sequence DataMolecular WeightProtein KinasesRectumSebaceous GlandsSequence Homology, Nucleic AcidSubstrate SpecificityConceptsCystic fibrosis transmembrane conductance regulatorHuman cystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorDogfish proteinRectal glandConductance regulatorPutative substrate sitesCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseMajor phosphorylation siteCyclic AMP-dependent protein phosphorylationApical plasma membraneAmino acid sequenceStudy of regulationPhosphorylation sitesProtein phosphorylationCDNA clonesProtein kinaseSimilar molecular massCFTR sequencePlasma membraneAcid sequenceImmunolocalization studiesMolecular massThe molecular biology of K+ channels
Perney T, Kaczmarek L. The molecular biology of K+ channels. Current Opinion In Cell Biology 1991, 3: 663-670. PMID: 1772658, DOI: 10.1016/0955-0674(91)90039-2.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus Statements
1990
Cloning and expression of cDNA and genomic clones encoding three delayed rectifier potassium channels in rat brain
Swanson R, Marshall J, Smith J, Williams J, Boyle M, Folander K, Luneau C, Antanavage J, Oliva C, Buhrow S, Bennet C, Stein R, Kaczmarek L. Cloning and expression of cDNA and genomic clones encoding three delayed rectifier potassium channels in rat brain. Neuron 1990, 4: 929-939. PMID: 2361015, DOI: 10.1016/0896-6273(90)90146-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCloning, MolecularDNAFemaleMembrane ProteinsMolecular Sequence DataOligonucleotide ProbesOocytesOrgan SpecificityPotassium ChannelsProtein BiosynthesisRatsRats, Inbred StrainsRestriction MappingRNA, MessengerSequence Homology, Nucleic AcidTranscription, GeneticXenopus