2016
Stimulation of Slack K+ Channels Alters Mass at the Plasma Membrane by Triggering Dissociation of a Phosphatase-Regulatory Complex
Fleming MR, Brown MR, Kronengold J, Zhang Y, Jenkins DP, Barcia G, Nabbout R, Bausch AE, Ruth P, Lukowski R, Navaratnam DS, Kaczmarek LK. Stimulation of Slack K+ Channels Alters Mass at the Plasma Membrane by Triggering Dissociation of a Phosphatase-Regulatory Complex. Cell Reports 2016, 16: 2281-2288. PMID: 27545877, PMCID: PMC5123741, DOI: 10.1016/j.celrep.2016.07.024.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBiosensing TechniquesBithionolBridged Bicyclo Compounds, HeterocyclicCell MembraneCerebral CortexFragile X Mental Retardation ProteinGene Expression RegulationHEK293 CellsHumansIon TransportMiceMice, KnockoutMicrofilament ProteinsMutationNerve Tissue ProteinsNeuronsPatch-Clamp TechniquesPhosphorylationPotassium ChannelsPotassium Channels, Sodium-ActivatedPrimary Cell CultureProtein BindingRNA, Small InterferingSignal TransductionThiazolidinesXenopus laevisConceptsProtein phosphatase 1Plasma membraneProtein kinase C.C-terminal residuesPhactr-1Potassium channelsPhosphatase 1Terminal domainSlack channelsHuman mutationsKinase C.Sodium-activated potassium channelsPharmacological activatorsOptical biosensor assayChannel stimulationSlack currentsBiosensor assaysMembraneMutantsPhosphorylationIntellectual disabilityProteinMutationsSevere intellectual disabilityActivatorKv3.3 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
PKC-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 sitesRepetitive Firing Triggers Clustering of Kv2.1 Potassium Channels in Aplysia Neurons*
Zhang Y, McKay SE, Bewley B, Kaczmarek LK. Repetitive Firing Triggers Clustering of Kv2.1 Potassium Channels in Aplysia Neurons*. Journal Of Biological Chemistry 2008, 283: 10632-10641. PMID: 18276591, DOI: 10.1074/jbc.m800253200.Peer-Reviewed Original ResearchConceptsBag cell neuronsKv2.1 channelsPotassium channelsPlasma membraneC-terminusKv2.1 clustersKv2.1 potassium channelCell neuronsMammalian neuronsReproductive behaviorRectifier potassium channelFrequency-dependent broadeningRapid redistributionAplysia neuronsClamp recordingsAcid peptidePartial inactivationRing-like clustersPhysiological changesKv2.1Neuronal excitabilityCentral nervous systemAction potentialsGenesNervous system
2005
Actions of BAX on Mitochondrial Channel Activity and on Synaptic Transmission
Jonas EA, Hardwick JM, Kaczmarek LK. Actions of BAX on Mitochondrial Channel Activity and on Synaptic Transmission. Antioxidants & Redox Signaling 2005, 7: 1092-1100. PMID: 16115013, DOI: 10.1089/ars.2005.7.1092.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisBcl-2-Associated X ProteinBcl-X ProteinCell MembraneElectrophysiologyIntracellular MembranesLiposomesLoligoMitochondriaMultigene FamilyNeurotransmitter AgentsPatch-Clamp TechniquesPeptidesPresynaptic TerminalsProtein Structure, TertiarySynapsesSynaptic TransmissionTime FactorsConceptsMitochondrial membraneBcl-2 family proteins BaxCell deathOuter mitochondrial membraneAction of BaxMitochondrial channel activityChannel activityNormal physiological settingsAntiapoptotic Bcl-xL proteinBcl-xL proteinDeath channelMitochondrial architectureMitochondrial channelsProapoptotic fragmentsLarge conductance channelPresynaptic terminalsBcl-xL.Proapoptotic proteinsAlternative functionsProtein BaxPhysiological settingsPhysiological roleSynaptic transmissionBaxNeurotransmitter release
2000
Exocytotic Insertion of Calcium Channels Constrains Compensatory Endocytosis to Sites of Exocytosis
Smith R, Baibakov B, Ikebuchi Y, White B, Lambert N, Kaczmarek L, Vogel S. Exocytotic Insertion of Calcium Channels Constrains Compensatory Endocytosis to Sites of Exocytosis. Journal Of Cell Biology 2000, 148: 755-768. PMID: 10684256, PMCID: PMC2169375, DOI: 10.1083/jcb.148.4.755.Peer-Reviewed Original Research
1999
Shaw‐like potassium currents in the auditory rhombencephalon throughout embryogenesis
Hendriks R, Morest D, Kaczmarek L. Shaw‐like potassium currents in the auditory rhombencephalon throughout embryogenesis. Journal Of Neuroscience Research 1999, 58: 791-804. PMID: 10583910, DOI: 10.1002/(sici)1097-4547(19991215)58:6<791::aid-jnr6>3.0.co;2-3.Peer-Reviewed Original ResearchConceptsPotassium currentNucleus magnocellularisOutward currentsWhole-cell patch recordingsInitial transient componentTransient outward currentsEarly neuronal developmentEarly neuronal differentiationHigh activation thresholdFirst synapsesAuditory nucleiPatch recordingsPotassium channel genesSynaptic functionCharacteristic response propertiesSynapses formNeuronal developmentNeuronal differentiationActivation thresholdDevelopmental appearanceTetraethylammoniumMagnocellularisEarly ageChannel genesNeuroblasts
1998
Activation of Kv3.1 channels in neuronal spine-like structures may induce local potassium ion depletion
Wang L, Gan L, Perney T, Schwartz I, Kaczmarek L. Activation of Kv3.1 channels in neuronal spine-like structures may induce local potassium ion depletion. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 1882-1887. PMID: 9465111, PMCID: PMC19207, DOI: 10.1073/pnas.95.4.1882.Peer-Reviewed Original ResearchConceptsSpine-like structuresIon channelsMembrane structureMembrane compartmentsVesicle compartmentKv3.1 channelsBulk cytoplasmElectron immunomicroscopyCHO cellsPostsynaptic membraneVesiclesMembrane patchesSpine-like protrusionsNeuronal membrane structurePotassium channel Kv3.1Channel Kv3.1CellsComplete inactivationInactivationCompartmentsRapid depletionCentral nervous systemSlow refillingSynaptic stimulationNeuronal structures
1997
Giga-Ohm Seals on Intracellular Membranes: A Technique for Studying Intracellular Ion Channels in Intact Cells
Jonas E, Knox R, Kaczmarek L. Giga-Ohm Seals on Intracellular Membranes: A Technique for Studying Intracellular Ion Channels in Intact Cells. Neuron 1997, 19: 7-13. PMID: 9247259, DOI: 10.1016/s0896-6273(00)80343-8.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MembraneCells, CulturedCHO CellsCricetinaeIon ChannelsPatch-Clamp TechniquesConceptsGiga-ohm sealsIntracellular membranesIntact cellsIntracellular ion channelsMembrane ion channel activityIon channel activityConventional patch clampingOrganelle membranesPlasma membraneInternal organellesInternal membranesInternal organelles membraneCell typesIon channelsChannel activityConfocal imagingInositol trisphosphateLipophilic fluorescent dyeMembranePatch clampingConcentric electrode arrangementPatch-clamp techniqueCellsIntact neuronsOrganellesProperties 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 organsMessenger
1996
Regulation of potassium channels by protein kinases
Jonas E, Kaczmarek L. Regulation of potassium channels by protein kinases. Current Opinion In Neurobiology 1996, 6: 318-323. PMID: 8794088, DOI: 10.1016/s0959-4388(96)80114-0.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus Statements
1995
Elimination of potassium channel expression by antisense oligonucleotides in a pituitary cell line.
Chung S, Saal D, Kaczmarek L. Elimination of potassium channel expression by antisense oligonucleotides in a pituitary cell line. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 5955-5959. PMID: 7597060, PMCID: PMC41620, DOI: 10.1073/pnas.92.13.5955.Peer-Reviewed Original ResearchAnimalsBase SequenceCell MembraneClone CellsDexamethasoneEgtazic AcidGene ExpressionKv1.4 Potassium ChannelKv1.5 Potassium ChannelMembrane PotentialsMolecular Sequence DataOligonucleotides, AntisensePatch-Clamp TechniquesPituitary GlandPotassium Channel BlockersPotassium ChannelsPotassium Channels, Voltage-GatedRatsRNA, MessengerTetraethylammoniumTetraethylammonium CompoundsThionucleotides
1994
The minK potassium channel exists in functional and nonfunctional forms when expressed in the plasma membrane of Xenopus oocytes
Blumenthal E, Kaczmarek L. The minK potassium channel exists in functional and nonfunctional forms when expressed in the plasma membrane of Xenopus oocytes. Journal Of Neuroscience 1994, 14: 3097-3105. PMID: 7514215, PMCID: PMC6577436, DOI: 10.1523/jneurosci.14-05-03097.1994.Peer-Reviewed Original ResearchConceptsN-terminal domainMinK proteinPlasma membraneInjected mRNAXenopus oocytesMinK potassium channelsFunctional potassium channelsPotassium channelsAmino acid epitopeProtein sequencesLevels of proteinMink genesLive oocytesIntracellular cAMP levelsKinetics of activationProteinOocytesMinK mRNANonfunctional formMRNASurface expressionRNAMinK currentsMRNA levelsCAMP levelsAutoactive 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
1993
Inward rectification of the minK potassium channel
Blumenthal E, Kaczmarek L. Inward rectification of the minK potassium channel. The Journal Of Membrane Biology 1993, 136: 23-29. PMID: 8271270, DOI: 10.1007/bf00241486.Peer-Reviewed Original Research
1992
Modulation by cAMP of a slowly activating potassium channel expressed in Xenopus oocytes
Blumenthal E, Kaczmarek L. Modulation by cAMP of a slowly activating potassium channel expressed in Xenopus oocytes. Journal Of Neuroscience 1992, 12: 290-296. PMID: 1370322, PMCID: PMC6575684, DOI: 10.1523/jneurosci.12-01-00290.1992.Peer-Reviewed Original ResearchMeSH Keywords8-Bromo Cyclic Adenosine MonophosphateAmino Acid SequenceAnimalsCell MembraneCyclic AMPFemaleGene ExpressionHumansMembrane PotentialsMembrane ProteinsMolecular Sequence DataMutagenesis, Site-DirectedOocytesPhosphorylationPotassium ChannelsPotassium Channels, Voltage-GatedProgesteroneProtein Kinase InhibitorsProtein KinasesRatsRNATransfectionXenopus laevisConceptsMinK proteinCAMP-dependent protein kinasePotential phosphorylation sitesXenopus oocytesCAMP levelsPhosphorylation sitesProtein kinasePlasma membraneKinase activityChannel proteinsIntracellular cAMP levelsProtein inhibitorProteinKinasePotassium channelsOocytesVoltage-dependent potassium currentsIsK
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 massPhosphorylation of membrane‐associated proteins by phorbol esters in isolated bag cell neurons of Aplysia
Azhderian E, Kaczmarek L. Phosphorylation of membrane‐associated proteins by phorbol esters in isolated bag cell neurons of Aplysia. Developmental Neurobiology 1991, 22: 105-115. PMID: 2030336, DOI: 10.1002/neu.480220202.Peer-Reviewed Original ResearchConceptsProtein kinase CBag cell neuronsKinase CPlasma membrane-containing fractionsProtein kinase C inhibitor H7Membrane-associated proteinsPhorbol esterExtent of phosphorylationMembrane-containing fractionsCell neuronsMembrane proteinsProtein phosphorylationNew speciesPhosphorylation statePlasma membraneTetradecanoyl phorbol 13Inhibitor H7Inactive phorbol esterIntact cellsPhosphate incorporationProtein extractsPhosphoproteinExtracellular mediumPhosphorylationProtein
1984
A voltage-clamp analysis of currents underlying cyclic AMP-induced membrane modulation in isolated peptidergic neurons of Aplysia
Kaczmarek L, Strumwasser F. A voltage-clamp analysis of currents underlying cyclic AMP-induced membrane modulation in isolated peptidergic neurons of Aplysia. Journal Of Neurophysiology 1984, 52: 340-349. PMID: 6090605, DOI: 10.1152/jn.1984.52.2.340.Peer-Reviewed Original ResearchConceptsBag cell neuronsCell neuronsCyclic AMP analoguePotassium currentOutward currentsNormal ionic mediumOnset of afterdischargePhosphodiesterase-resistant cAMP analoguePeak inward currentsAMP analogueBag cell clustersDelayed potassium currentMinority of cellsSpontaneous dischargeCalcium currentPeptidergic neuronsVoltage-clamp analysisCell culturesTwo-electrode voltage clampInward currentsSodium currentNegative slope resistanceA-currentMarked reductionNeurons