2021
Cerebellar Kv3.3 potassium channels activate TANK-binding kinase 1 to regulate trafficking of the cell survival protein Hax-1
Zhang Y, Varela L, Szigeti-Buck K, Williams A, Stoiljkovic M, Šestan-Peša M, Henao-Mejia J, D’Acunzo P, Levy E, Flavell RA, Horvath TL, Kaczmarek LK. Cerebellar Kv3.3 potassium channels activate TANK-binding kinase 1 to regulate trafficking of the cell survival protein Hax-1. Nature Communications 2021, 12: 1731. PMID: 33741962, PMCID: PMC7979925, DOI: 10.1038/s41467-021-22003-8.Peer-Reviewed Original ResearchConceptsTank Binding Kinase 1HAX-1Kv3.3 potassium channelMultivesicular bodiesKinase 1TANK-binding kinase 1Activation of caspasesAnti-apoptotic proteinsPotassium channelsMembrane proteinsBiochemical pathwaysCerebellar neuronsChannels bindCell deathTBK1 activityIon channelsMutant channelsCellular constituentsTraffickingKv3.3 channelsProteinNeuronal survivalMutationsChannel inactivationCaspases
2015
Membrane Ion Channels and Ion Currents
Levitan I, Kaczmarek L. Membrane Ion Channels and Ion Currents. 2015, 63-84. DOI: 10.1093/med/9780199773893.003.0004.ChaptersSingle ion channelsIon currentMovement of ionsIon channelsParticular ionPlasma membraneSpecialized membrane proteinsMembrane ion channelsIonsAction potential firingNeuronal plasma membranePatch-clamp techniqueMembrane proteinsNeurons resultsCurrentClamp techniqueAction potentialsDetailed characterizationElectrical activityMembrane currentsMembrane voltageChannelsMacroscopic membrane currentsEssential propertiesComplex patternsIon Channels Are Membrane Proteins
Levitan I, Kaczmarek L. Ion Channels Are Membrane Proteins. 2015, 85-102. DOI: 10.1093/med/9780199773893.003.0005.ChaptersMembrane-spanning segmentsHomologous domainsPrimary subunitIon channelsFunctional potassium channelsPotassium channelsVoltage-dependent ion channelsThree-dimensional structureMembrane proteinsSodium channelsMutational analysisProtein regionsVoltage-gated sodiumChannel proteinsChannel gatingProtein conformationStructural modulesChannel poreGlobal changeVoltage-dependent activationVoltage-dependent channelsSubunitsProteinOverall structureIon selectivity
2001
Ion Channels Are Membrane Proteins
B.Levitan I, Kaczmarek L. Ion Channels Are Membrane Proteins. 2001, 89-112. DOI: 10.1093/oso/9780195145236.003.0005.Peer-Reviewed Original ResearchIon channelsSingle ion channelsIon channel structureAmino acid sequenceMolecular cloning techniquesMembrane proteinsAcid sequenceSuch measurementsCloning techniquesNovel insightsProtein moleculesMacroscopic membrane currentsKey functional propertiesChannel structureFunctional propertiesPowerful combinationProteinChannelsActivity of populationsMoleculesSequenceMembrane currentsStructural approachActivityMeasurementsIon Channels, Membrane Ion Currents, and the Action Potential
B.Levitan I, Kaczmarek L. Ion Channels, Membrane Ion Currents, and the Action Potential. 2001, 113-138. DOI: 10.1093/oso/9780195145236.003.0006.Peer-Reviewed Original ResearchIon channelsPotassium channel proteinIon currentDetailed mechanistic understandingMembrane proteinsMolecular detailsActive ion channelsChannel proteinsBiological membranesMechanistic understandingSingle-channel recordingsProteinMembrane ion currentsVoltage-clamp measurementsMembraneChannel recordingsCellsMacroscopic currentsClamp measurementsCurrentElectrical phenomenaVoltage clampCurrent chapterMacroscopic membranesPotassium current
1997
Identification 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
1991
Phosphorylation 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