2010
Kv1.3 is the exclusive voltage‐gated K+ channel of platelets and megakaryocytes: roles in membrane potential, Ca2+ signalling and platelet count
McCloskey C, Jones S, Amisten S, Snowden RT, Kaczmarek LK, Erlinge D, Goodall AH, Forsythe ID, Mahaut‐Smith M. Kv1.3 is the exclusive voltage‐gated K+ channel of platelets and megakaryocytes: roles in membrane potential, Ca2+ signalling and platelet count. The Journal Of Physiology 2010, 588: 1399-1406. PMID: 20308249, PMCID: PMC2876798, DOI: 10.1113/jphysiol.2010.188136.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlood PlateletsCalcium SignalingCell SizeDNA, ComplementaryHumansIn Vitro TechniquesKv1.3 Potassium ChannelMegakaryocytesMembrane PotentialsMiceMice, Inbred C57BLPatch-Clamp TechniquesPlatelet CountReverse Transcriptase Polymerase Chain ReactionScorpion VenomsSecond Messenger SystemsConceptsLarge ionic conductanceMembrane potentialHuman plateletsKv alphaMegakaryocyte developmentAncillary subunitsQuantitative RT-PCRMolecular levelKv channelsRole of Kv1.3MegakaryocytesKv1.3RT-PCRWild-type miceKv currentsSubunitsSignalingMiceApoptosisMargatoxinPlatelet activationRoleIonic conductancesPlateletsActivation
2008
Na+-mediated coupling between AMPA receptors and KNa channels shapes synaptic transmission
Nanou E, Kyriakatos A, Bhattacharjee A, Kaczmarek LK, Paratcha G, Manira A. Na+-mediated coupling between AMPA receptors and KNa channels shapes synaptic transmission. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 20941-20946. PMID: 19095801, PMCID: PMC2634910, DOI: 10.1073/pnas.0806403106.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
2003
The 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
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
1999
Prolonged Activation of Mitochondrial Conductances During Synaptic Transmission
Jonas E, Buchanan J, Kaczmarek L. Prolonged Activation of Mitochondrial Conductances During Synaptic Transmission. Science 1999, 286: 1347-1350. PMID: 10558987, DOI: 10.1126/science.286.5443.1347.Peer-Reviewed Original ResearchMeSH KeywordsAction PotentialsAnimalsCalciumCalcium ChannelsDecapodiformesElectric ConductivityElectric StimulationIntracellular MembranesIon ChannelsIon TransportMicroscopy, ElectronMitochondriaPatch-Clamp TechniquesPorinsPresynaptic TerminalsSynaptic TransmissionTime FactorsVoltage-Dependent Anion ChannelsConceptsChannel activityIon channel activityMitochondrial membraneOnly organellesIntracellular organellesIntact cellsIon channelsMitochondriaOrganellesLarge conductanceTens of secondsPresynaptic terminalsIon transportSynaptic transmissionSynaptic stimulationConductanceElectron microscopyPatch-clamp techniqueMembraneActivityCellsActivationSquidStimulation
1998
Expression of a foreign G-protein coupled receptor modulates the excitability of the peptidergic bag cell neurons of Aplysia
Whim M, Kaczmarek L. Expression of a foreign G-protein coupled receptor modulates the excitability of the peptidergic bag cell neurons of Aplysia. Neuroscience Letters 1998, 258: 143-146. PMID: 9885951, DOI: 10.1016/s0304-3940(98)00850-7.Peer-Reviewed Original ResearchConceptsBag cell neuronsCell neuronsMetabotropic glutamate receptorsG proteinsPeptidergic bag cell neuronsAfferent stimulationSpontaneous firingAfferent inputGlutamate receptorsSecond messenger pathwaysPharmacological activationReceptor activationAfterdischargesNeuronsMessenger pathwaysReceptorsActivationAdditional pathwaysExpressionExcitabilityPathwaySustained period
1985
Enhancement of calcium current in Aplysia neurones by phorbol ester and protein kinase C
DeRiemer SA, Strong JA, Albert KA, Greengard P, Kaczmarek LK. Enhancement of calcium current in Aplysia neurones by phorbol ester and protein kinase C. Nature 1985, 313: 313-316. PMID: 2578617, DOI: 10.1038/313313a0.Peer-Reviewed Original ResearchConceptsProtein kinase CKinase CProtein kinase presentEndogenous protein kinase CKinase presentProtein kinase1Molecular mechanismsCellular componentsPhorbol ester TPAIon channelsPhorbol esterMammalian brainTumor-promoting phorbol ester TPAMollusc AplysiaPhysiological propertiesEnzymeNeuronal excitabilityDirect evidenceKinase1PhosphorylationProteinHigh concentrationsActivationAplysia