2021
A KCNC1 mutation in epilepsy of infancy with focal migrating seizures produces functional channels that fail to be regulated by PKC phosphorylation
Zhang Y, Ali SR, Nabbout R, Barcia G, Kaczmarek LK. A KCNC1 mutation in epilepsy of infancy with focal migrating seizures produces functional channels that fail to be regulated by PKC phosphorylation. Journal Of Neurophysiology 2021, 126: 532-539. PMID: 34232791, PMCID: PMC8409950, DOI: 10.1152/jn.00257.2021.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCHO CellsCricetinaeCricetulusEpilepsyMutationPhosphorylationProtein Kinase CShaw Potassium ChannelsSialyltransferasesConceptsFunctional channelsProtein kinase C.Serious human diseasesPotassium channelsWild-type channelsEpilepsy of infancyChannel modulationTerminal domainIon channel mutationsPKC phosphorylationC-terminusNormal neuronal functionChannel proteinsKv3.1 potassium channelRegulatory sitesKinase C.Human diseasesChannel functionPhosphorylationIon channelsMutationsNovo variantsChannel mutationsBiophysical propertiesNeuronal function
2012
De novo gain-of-function KCNT1 channel mutations cause malignant migrating partial seizures of infancy
Barcia G, Fleming MR, Deligniere A, Gazula VR, Brown MR, Langouet M, Chen H, Kronengold J, Abhyankar A, Cilio R, Nitschke P, Kaminska A, Boddaert N, Casanova JL, Desguerre I, Munnich A, Dulac O, Kaczmarek LK, Colleaux L, Nabbout R. De novo gain-of-function KCNT1 channel mutations cause malignant migrating partial seizures of infancy. Nature Genetics 2012, 44: 1255-1259. PMID: 23086397, PMCID: PMC3687547, DOI: 10.1038/ng.2441.Peer-Reviewed Original Research
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 ResearchPKC-Induced Intracellular Trafficking of CaV2 Precedes Its Rapid Recruitment to the Plasma Membrane
Zhang Y, Helm JS, Senatore A, Spafford JD, Kaczmarek LK, Jonas EA. PKC-Induced Intracellular Trafficking of CaV2 Precedes Its Rapid Recruitment to the Plasma Membrane. Journal Of Neuroscience 2008, 28: 2601-2612. PMID: 18322103, PMCID: PMC2830008, DOI: 10.1523/jneurosci.4314-07.Peer-Reviewed Original ResearchConceptsProtein kinase CActivation of PKCPlasma membraneGrowth conesLatrunculin BIntracellular traffickingActin polymerizationIntact microtubulesIntact actinKinase CChannel insertionPKC activationIon channelsMicrotubule polymerizationRapid recruitmentOrganellesLamellipodiumSubunitsMicrotubulesActinMembraneActivationRecruitmentCone terminalsNew sites
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
2005
Association/Dissociation of a Channel–Kinase Complex Underlies State-Dependent Modulation
Magoski NS, Kaczmarek LK. Association/Dissociation of a Channel–Kinase Complex Underlies State-Dependent Modulation. Journal Of Neuroscience 2005, 25: 8037-8047. PMID: 16135761, PMCID: PMC2873328, DOI: 10.1523/jneurosci.1903-05.2005.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsAplysiaCells, CulturedConus SnailIon ChannelsMollusk VenomsNeuronal PlasticityNeuronsProtein Kinase CConceptsProtein kinase CSrc homology 3 domainCation channelsSrc tyrosine kinasePKC-dependent modulationPhorbol esterSrc-dependent regulationAplysia bag cell neuronsBag cell neuronsProtein kinaseAssociated kinaseAssociation/dissociationEgg-laying hormonePhosphotyrosine stainingTyrosine kinaseKinase CKinaseReproductive behaviorNonselective cation channelsIon channelsChannel activityUnstimulated neuronsDependent modulationCell neuronsLong-term excitabilityAcoustic environment determines phosphorylation state of the Kv3.1 potassium channel in auditory neurons
Song P, Yang Y, Barnes-Davies M, Bhattacharjee A, Hamann M, Forsythe ID, Oliver DL, Kaczmarek LK. Acoustic environment determines phosphorylation state of the Kv3.1 potassium channel in auditory neurons. Nature Neuroscience 2005, 8: 1335-1342. PMID: 16136041, DOI: 10.1038/nn1533.Peer-Reviewed Original ResearchMeSH KeywordsAcoustic StimulationAction PotentialsAnimalsAnimals, NewbornBrain StemCHO CellsCricetinaeCricetulusDose-Response Relationship, RadiationElectric StimulationEnzyme InhibitorsFunctional LateralityGene Expression RegulationImmunohistochemistryIn Vitro TechniquesIndolesMaleimidesNeuronsPatch-Clamp TechniquesPhosphorylationProtein Kinase CRatsRats, Sprague-DawleyTetradecanoylphorbol AcetateConceptsKv3.1 potassium channelAction potentialsAuditory neuronsPotassium channelsShort-duration action potentialsRat brainstem neuronsAuditory brainstem nucleiProtein kinase CHigh-frequency spikingHigh-frequency auditoryBrainstem neuronsHigh-frequency stimuliBrainstem nucleiSynaptic stimulationNeuronsInteraural differencesSound localizationIntrinsic electrical propertiesKinase C
2003
Modulation of the Kv3.1b Potassium Channel Isoform Adjusts the Fidelity of the Firing Pattern of Auditory Neurons
Macica CM, von Hehn CA, Wang LY, Ho CS, Yokoyama S, Joho RH, Kaczmarek LK. Modulation of the Kv3.1b Potassium Channel Isoform Adjusts the Fidelity of the Firing Pattern of Auditory Neurons. Journal Of Neuroscience 2003, 23: 1133-1141. PMID: 12598601, PMCID: PMC6742259, DOI: 10.1523/jneurosci.23-04-01133.2003.Peer-Reviewed Original ResearchMeSH KeywordsAction PotentialsAnimalsBrain StemCells, CulturedCHO CellsCricetinaeElectric ConductivityEvoked Potentials, AuditoryKineticsMiceMice, KnockoutNeuronsNeuropeptidesPatch-Clamp TechniquesPhosphorylationPotassium ChannelsPotassium Channels, Voltage-GatedProtein IsoformsProtein Kinase CSerineShaw Potassium ChannelsTetradecanoylphorbol AcetateConceptsTrapezoid bodyMedial nucleusAuditory neuronsHigh-frequency stimulationWild-type neuronsKv3.1 potassium channelHigh-threshold componentPotassium channel isoformsGreat temporal precisionPartial decreaseProtein kinase C activationAction potentialsLocation of soundsMice resultsFiring patternsNeuronsSensory stimulationPotassium channelsChannel isoformsKinase C activationKv3.1Kv3.1 geneStimulationHigh frequencyProtein kinase C
2002
Prolonged Activation of Ca2+-Activated K+Current Contributes to the Long-Lasting Refractory Period ofAplysia Bag Cell Neurons
Zhang Y, Magoski NS, Kaczmarek LK. Prolonged Activation of Ca2+-Activated K+Current Contributes to the Long-Lasting Refractory Period ofAplysia Bag Cell Neurons. Journal Of Neuroscience 2002, 22: 10134-10141. PMID: 12451114, PMCID: PMC6758731, DOI: 10.1523/jneurosci.22-23-10134.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAplysiaCalciumCells, CulturedElectric StimulationEnzyme ActivatorsEnzyme InhibitorsLarge-Conductance Calcium-Activated Potassium ChannelsNeural InhibitionNeuronsPatch-Clamp TechniquesPhloretinPotassiumPotassium Channel BlockersPotassium Channels, Calcium-ActivatedProtein Kinase CRefractory Period, ElectrophysiologicalSphingosineTetradecanoylphorbol AcetateConceptsBag cell neuronsCell neuronsRefractory periodBK currentsProtein kinase COnset of afterdischargeBK channel activityApplication of phloretinBK channel activatorsProlonged refractory periodAbility of stimulationRole of Ca2Blocker paxillinePharmacological characteristicsChannel activatorIntracellular Ca2Prolonged increaseOutward currentsInhibitor of PKCAfterdischargesNeuronsAdditional stimulationProlonged activationActivator of PKCChannel activityProtein 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
Casein Kinase 2 Determines the Voltage Dependence of the Kv3.1 Channel in Auditory Neurons and Transfected Cells
Macica C, Kaczmarek L. Casein Kinase 2 Determines the Voltage Dependence of the Kv3.1 Channel in Auditory Neurons and Transfected Cells. Journal Of Neuroscience 2001, 21: 1160-1168. PMID: 11160386, PMCID: PMC6762230, DOI: 10.1523/jneurosci.21-04-01160.2001.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAnimalsAuditory PathwaysBinding SitesBrain StemCasein Kinase IICDC2-CDC28 KinasesCHO CellsCricetinaeCyclin-Dependent Kinase 2Cyclin-Dependent KinasesElectric StimulationEnzyme InhibitorsIn Vitro TechniquesMembrane PotentialsNeuronsNeuropeptidesPatch-Clamp TechniquesPhosphorylationPotassium ChannelsPotassium Channels, Voltage-GatedPrecipitin TestsProtein Kinase CProtein Serine-Threonine KinasesRatsShaw Potassium ChannelsTetradecanoylphorbol AcetateTransfectionConceptsCasein kinase 2Kinase 2Casein kinase IIProtein kinase CKv3.1 channelsChinese hamster ovary cellsHamster ovary cellsConstitutive phosphorylationPhosphatase treatmentKinase IIKinase CTransfected CellsVoltage-dependent activationOvary cellsWhole-cell conductancePhosphorylationPotassium channelsRectifier channelsBiophysical characteristicsInactivationKv3.1 potassium channelVoltage dependenceActivationKv3.1Patch-clamp recordings
1998
Protein Kinase C Regulates a Vesicular Class of Calcium Channels in the Bag Cell Neurons of Aplysia
White B, Nick T, Carew T, Kaczmarek L. Protein Kinase C Regulates a Vesicular Class of Calcium Channels in the Bag Cell Neurons of Aplysia. Journal Of Neurophysiology 1998, 80: 2514-2520. PMID: 9819259, DOI: 10.1152/jn.1998.80.5.2514.Peer-Reviewed Original ResearchModulation of a calcium-sensitive nonspecific cation channel by closely associated protein kinase and phosphatase activities
Wilson G, Magoski N, Kaczmarek L. Modulation of a calcium-sensitive nonspecific cation channel by closely associated protein kinase and phosphatase activities. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 10938-10943. PMID: 9724808, PMCID: PMC27999, DOI: 10.1073/pnas.95.18.10938.Peer-Reviewed Original ResearchMeSH KeywordsAdenine NucleotidesAnimalsAplysiaIon ChannelsMethylationPhosphoprotein PhosphatasesProtein Kinase CProtein Phosphatase 1RabbitsConceptsProtein kinaseCation channelsProtein phosphatase 1Protein tyrosine phosphataseNonspecific cation channelProtein kinase C inhibitorPresence of H7Nonhydrolyzable ATP analogKinase C inhibitorRegulatory complexPhosphatase 1Bag cell neuronsTyrosine phosphataseExcised patchesOpen probabilityCytoplasmic sideMolecular switchATP analogC inhibitorPhosphatase activityKinaseChannel closureSpontaneous action potentialsPatch-clamp studiesATPThe Expression of Two Splice Variants of the Kv3.1 Potassium Channel Gene Is Regulated by Different Signaling Pathways
Liu S, Kaczmarek L. The Expression of Two Splice Variants of the Kv3.1 Potassium Channel Gene Is Regulated by Different Signaling Pathways. Journal Of Neuroscience 1998, 18: 2881-2890. PMID: 9526005, PMCID: PMC6792597, DOI: 10.1523/jneurosci.18-08-02881.1998.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsCerebellumFibroblast Growth FactorsGene Expression Regulation, DevelopmentalMembrane PotentialsNerve Growth FactorsNeuropeptidesPotassium ChannelsPotassium Channels, Voltage-GatedProtein Kinase CRatsRats, Sprague-DawleyRNA, MessengerSecond Messenger SystemsShaw Potassium ChannelsSignal TransductionTranscription, GeneticConceptsDifferent signaling pathwaysKv3.1 potassium channel genePotassium channel genesBasic fibroblast growth factorChannel genesSignaling pathwaysNuclear protein kinase C activityMRNA levelsDifferent channel proteinsProtein kinase C inhibitorProtein kinase C activityKinase C inhibitorKinase C activityAlternative splicingNuclear RNAChannel proteinsMolecular mechanismsFibroblast growth factorDifferential regulationDevelopmental stagesSplice variantsC inhibitorPKC activityC activityGenes
1997
Properties 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
1995
Electrophysiological and pharmacological characterization of a mammalian Shaw channel expressed in NIH 3T3 fibroblasts
Kanemasa T, Gan L, Perney T, Wang L, Kaczmarek L. Electrophysiological and pharmacological characterization of a mammalian Shaw channel expressed in NIH 3T3 fibroblasts. Journal Of Neurophysiology 1995, 74: 207-217. PMID: 7472324, DOI: 10.1152/jn.1995.74.1.207.Peer-Reviewed Original Research
1994
Transient changes in intracellular calcium associated with a prolonged increase in excitability in neurons of Aplysia californica
Fisher T, Levy S, Kaczmarek L. Transient changes in intracellular calcium associated with a prolonged increase in excitability in neurons of Aplysia californica. Journal Of Neurophysiology 1994, 71: 1254-1257. PMID: 8201416, DOI: 10.1152/jn.1994.71.3.1254.Peer-Reviewed Original ResearchConceptsIntracellular calcium levelsBag cell neuronsCalcium levelsSpontaneous firingCell neuronsIntracellular calciumAction potentialsTransient elevationBasal intracellular calcium levelsLong-duration action potentialsBasal calcium levelsFree calcium ion concentrationTriggers calcium releaseCalcium-sensitive microelectrodesAplysia californicaIndividual action potentialsAfferent stimulationAfferent inputAfterdischargesProlonged increaseCalcium releaseCalcium ion concentrationNeuronsBiphasic patternPrimary cultures
1992
Inhibition of peptide release from invertebrate neurons by the protein kinase inhibitor H-7
Loechner K, Mattessich-Arrandale J, Azhderian E, Kaczmarek L. Inhibition of peptide release from invertebrate neurons by the protein kinase inhibitor H-7. Brain Research 1992, 581: 315-318. PMID: 1393536, DOI: 10.1016/0006-8993(92)90724-n.Peer-Reviewed Original ResearchRecruitment of Ca2+ channels by protein kinase C during rapid formation of putative neuropeptide release sites in isolated Aplysia neurons
Knox R, Quattrocki E, Connor J, Kaczmarek L. Recruitment of Ca2+ channels by protein kinase C during rapid formation of putative neuropeptide release sites in isolated Aplysia neurons. Neuron 1992, 8: 883-889. PMID: 1316764, DOI: 10.1016/0896-6273(92)90202-o.Peer-Reviewed Original Research