2008
Protein 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
Modulation of Kv3.1b Potassium Channel Phosphorylation in Auditory Neurons by Conventional and Novel Protein Kinase C Isozymes*
Song P, Kaczmarek LK. Modulation of Kv3.1b Potassium Channel Phosphorylation in Auditory Neurons by Conventional and Novel Protein Kinase C Isozymes*. Journal Of Biological Chemistry 2006, 281: 15582-15591. PMID: 16595659, DOI: 10.1074/jbc.m512866200.Peer-Reviewed Original ResearchConceptsAuditory neuronsMNTB neuronsTrapezoid bodyBrief high-frequency electrical stimulationProtein kinase CMetabotropic glutamate receptor activationHigh-frequency electrical stimulationBasal phosphorylationGlutamate receptor activationHigh-frequency stimulationFrequency electrical stimulationHigh-frequency firingMature nervous systemKv3.1 potassium channelNeuronal abilityBrainstem slicesMedial nucleusFrequency stimulationAuditory brainstemFrequency firingConventional protein kinase CPharmacological activationNervous systemElectrical stimulationPKC isozymes
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
2000
Modification of delayed rectifier potassium currents by the Kv9.1 potassium channel subunit
Richardson F, Kaczmarek L. Modification of delayed rectifier potassium currents by the Kv9.1 potassium channel subunit. Hearing Research 2000, 147: 21-30. PMID: 10962170, DOI: 10.1016/s0378-5955(00)00117-9.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAuditory PathwaysComputer SimulationDelayed Rectifier Potassium ChannelsEvoked Potentials, AuditoryFemaleHumansIn Vitro TechniquesMembrane PotentialsModels, NeurologicalNeuronsOocytesPotassium ChannelsPotassium Channels, Voltage-GatedRatsRecombinant ProteinsShab Potassium ChannelsXenopus laevisConceptsRectifier potassium currentPotassium channel subunitsChannel subunitsPotassium currentInward currentsInhibition of firingHigh-frequency stimulationVariety of neuronsPotassium channel alpha subunitChannel alpha subunitFrequency stimulationAuditory pathwayInferior colliculusSustained depolarizationAction potentialsModel neuronsFiring patternsKv9.1NeuronsPotassium channelsAmplitude of currentsKv2.1Sound stimuliRate of activationTetraethyl ammonium ions
1997
The Secretion of Classical and Peptide Cotransmitters from a Single Presynaptic Neuron Involves a Synaptobrevin-Like Molecule
Whim M, Niemann H, Kaczmarek L. The Secretion of Classical and Peptide Cotransmitters from a Single Presynaptic Neuron Involves a Synaptobrevin-Like Molecule. Journal Of Neuroscience 1997, 17: 2338-2347. PMID: 9065494, PMCID: PMC6573516, DOI: 10.1523/jneurosci.17-07-02338.1997.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAnimalsAplysiaCalciumCells, CulturedCoculture TechniquesElectric ConductivityGanglia, InvertebrateKineticsMagnesiumMembrane PotentialsMembrane ProteinsNerve Tissue ProteinsNeuronsNeurons, AfferentNeuropeptidesPatch-Clamp TechniquesPresynaptic TerminalsR-SNARE ProteinsRecombinant ProteinsSynapsesTetanus ToxinConceptsClassical transmittersSingle presynaptic neuronRelease of neuropeptidesSingle action potentialPresynaptic release sitesSecretion of peptidesNeuron B2Peptidergic synapsesSynaptic typesSensory neuronsPresynaptic neuronsTetanus toxinPeptide cotransmittersAction potentialsPresynaptic injectionSecretionNeuronsMolecular mechanismsSynapseTypes of transmittersB2CotransmitterNeuropeptidesPeptidesRelease
1996
Cloning 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
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
1991
The 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