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 disabilityActivator
2014
Human Slack Potassium Channel Mutations Increase Positive Cooperativity between Individual Channels
Kim GE, Kronengold J, Barcia G, Quraishi IH, Martin HC, Blair E, Taylor JC, Dulac O, Colleaux L, Nabbout R, Kaczmarek LK. Human Slack Potassium Channel Mutations Increase Positive Cooperativity between Individual Channels. Cell Reports 2014, 9: 1661-1672. PMID: 25482562, PMCID: PMC4294418, DOI: 10.1016/j.celrep.2014.11.015.Peer-Reviewed Original Research
2009
The N-Terminal Domain of Slack Determines the Formation and Trafficking of Slick/Slack Heteromeric Sodium-Activated Potassium Channels
Chen H, Kronengold J, Yan Y, Gazula VR, Brown MR, Ma L, Ferreira G, Yang Y, Bhattacharjee A, Sigworth FJ, Salkoff L, Kaczmarek LK. The N-Terminal Domain of Slack Determines the Formation and Trafficking of Slick/Slack Heteromeric Sodium-Activated Potassium Channels. Journal Of Neuroscience 2009, 29: 5654-5665. PMID: 19403831, PMCID: PMC3688047, DOI: 10.1523/jneurosci.5978-08.2009.Peer-Reviewed Original ResearchConceptsTerminal domainN-terminal domainAlternative splice variantsPotassium channelsSubcellular localizationPlasma membraneMolecular explanationHeteromer formationSplice variantsHeteromeric channelsDistinct rolesSingle-channel levelSubunitsUnitary conductanceCentral neuronsSlack channelsImmunocytochemical studyFiring patternsDomainLocalizationNeuronsGenesTraffickingChannel levelHomomers
2006
Opposite Regulation of Slick and Slack K+ Channels by Neuromodulators
Santi CM, Ferreira G, Yang B, Gazula VR, Butler A, Wei A, Kaczmarek LK, Salkoff L. Opposite Regulation of Slick and Slack K+ Channels by Neuromodulators. Journal Of Neuroscience 2006, 26: 5059-5068. PMID: 16687497, PMCID: PMC6674240, DOI: 10.1523/jneurosci.3372-05.2006.Peer-Reviewed Original ResearchConceptsSlo2 channelsHippocampal brain sectionsCultured hippocampal neuronsProtein kinase CWhole-cell currentsPKC activator PMANeuronal excitabilityHippocampal neuronsBrain sectionsBasal levelsImmunocytochemical techniquesGalphaq proteinElectrical activitySlo2.1Activator PMAReceptorsChannel gene familyWidespread expressionChannel activityExcitabilityNeuromodulatorsIntracellular concentrationPotential of cellsBrainXenopus oocytes
2003
Functional Specialization of Male and Female Vocal Motoneurons
Yamaguchi A, Kaczmarek LK, Kelley DB. Functional Specialization of Male and Female Vocal Motoneurons. Journal Of Neuroscience 2003, 23: 11568-11576. PMID: 14684859, PMCID: PMC6740944, DOI: 10.1523/jneurosci.23-37-11568.2003.Peer-Reviewed Original Research
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
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
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
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