2017
Kv3 Channels: Enablers of Rapid Firing, Neurotransmitter Release, and Neuronal Endurance
Kaczmarek LK, Zhang Y. Kv3 Channels: Enablers of Rapid Firing, Neurotransmitter Release, and Neuronal Endurance. Physiological Reviews 2017, 97: 1431-1468. PMID: 28904001, PMCID: PMC6151494, DOI: 10.1152/physrev.00002.2017.Peer-Reviewed Original ResearchConceptsKv3 channelsAuditory brain stem neuronsNeurotransmitter releaseBrain stem neuronsOngoing neuronal activityFire action potentialsHigh-frequency firingChannel genesStem neuronsGABAergic interneuronsMultiple protein isoformsCertain neuronsProtein-protein interactionsNeuronal activityNeuronal functionAlzheimer's diseaseNeurological disordersAction potentialsPurkinje cellsUnique expression patternKv3 familyNeuronsAbnormal regulationProtein isoformsProtein kinase
2015
Receptors and Transduction Mechanisms II: Indirectly Coupled Receptor/Ion Channel Systems
Levitan I, Kaczmarek L. Receptors and Transduction Mechanisms II: Indirectly Coupled Receptor/Ion Channel Systems. 2015, 263-294. DOI: 10.1093/med/9780199773893.003.0012.ChaptersProtein phosphorylationSecond messenger-dependent protein kinasesReceptor-channel couplingIon channel proteinsAppropriate biological responseExtracellular signalsDirect phosphorylationSpecific membrane receptorsProtein kinaseRegulatory componentsChannel proteinsSecond messenger systemsMembrane receptorsTransduction mechanismsIon channelsPhosphorylationBiological responsesMessenger systemsIon channel systemsDiversityTarget cellsSignal recognitionNeuronal excitabilityCellsKinase
2006
Non-conducting functions of voltage-gated ion channels
Kaczmarek LK. Non-conducting functions of voltage-gated ion channels. Nature Reviews Neuroscience 2006, 7: 761-771. PMID: 16988652, DOI: 10.1038/nrn1988.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseΒ-subunitProtein kinaseIntrinsic protein kinase activityTRP familyΑ-subunitNon-conducting functionCell-cell adhesionTranscription factor activityDependent protein kinase IIProtein kinase activityLarge extracellular domainCell proliferationSynaptic release machineryTranscription factor CREBProtein kinase IIVoltage-gated ion channelsKey PointsIn additionMAPK/ERKIntrinsic enzyme activityNon-selective cation channelsCell adhesion moleculeReductase functionC-terminusKinase activity
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 ResearchConceptsProtein 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 excitability
2002
Protein 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
1998
Modulation 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 ResearchConceptsProtein 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 studiesATP
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
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 mass
1989
Inhibitors of protein kinase C prevent enhancement of calcium current and action potentials in peptidergic neurons of Aplysia
Conn P, Strong J, Kaczmarek L. Inhibitors of protein kinase C prevent enhancement of calcium current and action potentials in peptidergic neurons of Aplysia. Journal Of Neuroscience 1989, 9: 480-487. PMID: 2918372, PMCID: PMC6569798, DOI: 10.1523/jneurosci.09-02-00480.1989.Peer-Reviewed Original Research
1987
Stimulation of protein kinase C recruits covert calcium channels in Aplysia bag cell neurons
Strong J, Fox A, Tsien R, Kaczmarek L. Stimulation of protein kinase C recruits covert calcium channels in Aplysia bag cell neurons. Nature 1987, 325: 714-717. PMID: 2434853, DOI: 10.1038/325714a0.Peer-Reviewed Original ResearchConceptsProtein kinase CBag cell neuronsKinase CProtein kinaseCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseAplysia bag cell neuronsCell neuronsCalcium channelsSingle-channel levelExcitable cellsKinaseUntreated cellsUnitary conductanceCalcium currentPeptidergic bag cell neuronsVoltage-activated calcium channelsCardiac muscleDifferent unitary conductancesCellsDifferent mechanismsVoltage-activated calcium currentsChannel levelSecond classNeurons
1986
Chapter 7 The role of protein kinases in the control of prolonged changes in neuronal excitability
Kaczmarek L, Strong J, Kauer J. Chapter 7 The role of protein kinases in the control of prolonged changes in neuronal excitability. Progress In Brain Research 1986, 69: 77-90. PMID: 3328878, DOI: 10.1016/s0079-6123(08)61050-x.Chapters
1985
Calcium/phosphatidylserine/diacylglycerol-dependent protein phosphorylation in the Aplysia nervous system
DeRiemer SA, Greengard P, Kaczmarek LK. Calcium/phosphatidylserine/diacylglycerol-dependent protein phosphorylation in the Aplysia nervous system. Journal Of Neuroscience 1985, 5: 2672-2676. PMID: 4045549, PMCID: PMC6565129, DOI: 10.1523/jneurosci.05-10-02672.1985.Peer-Reviewed Original ResearchConceptsProtein kinase CProtein kinase activityAplysia nervous systemBag cell neuronsKinase CProtein phosphorylationKinase activityDiacylglycerol-dependent protein kinaseEndogenous substrate proteinsEndogenous enzymesCytosolic fractionTumor-promoting phorbol diestersCell neuronsSubstrate proteinsCell clustersBag cell clustersProtein kinaseDalton proteinMammalian tissuesSpecific substratesNervous systemPhosphorylationBovine brainMammalian brainPolymixin B sulfateInhibitors of calcium-dependent enzymes prevent the onset of afterdischarge in the peptidergic bag cell neurons of Aplysia
DeRiemer S, Schweitzer B, Kaczmarek L. Inhibitors of calcium-dependent enzymes prevent the onset of afterdischarge in the peptidergic bag cell neurons of Aplysia. Brain Research 1985, 340: 175-180. PMID: 4027644, DOI: 10.1016/0006-8993(85)90790-5.Peer-Reviewed Original ResearchConceptsBag cell neuronsCalcium-dependent enzymesCell neuronsNeuroactive peptidesAttenuation of secretionOnset of afterdischargeBrief electrical stimulationPeptidergic bag cell neuronsAbility of stimulationEffect of TFPEffects of agentsNeuronal excitabilitySynaptic transmissionAfterdischargesNeurosecretory neuronsElectrical stimulationEndogenous burstingNeuronsSecretionCalmodulin-dependent enzymesProtein kinaseAplysiaStimulationOnsetAgents
1984
Calcium/calmodulin-dependent protein phosphorylation in the nervous system of Aplysia
DeRiemer SA, Kaczmarek LK, Lai Y, McGuinness TL, Greengard P. Calcium/calmodulin-dependent protein phosphorylation in the nervous system of Aplysia. Journal Of Neuroscience 1984, 4: 1618-1625. PMID: 6726349, PMCID: PMC6564979, DOI: 10.1523/jneurosci.04-06-01618.1984.Peer-Reviewed Original ResearchConceptsCaM-dependent protein kinaseCaM-dependent protein phosphorylationProtein phosphorylationBag cell neuronsCalcium/calmodulin-dependent protein phosphorylationProtein kinaseAplysia CNSCalmodulin-dependent protein phosphorylationSynapsin IAplysia nervous systemMammalian nervous systemCalmodulin kinase IISubstrate proteinsControl of phosphorylationPhosphorylation stateNervous system proteinsKinase IICell neuronsSubcellular distributionMajor substrateSystem proteinsCell proteinsPhosphorylationNeuronal proteinsCell-free preparations
1980
Microinjection of catalytic subunit of cyclic AMP-dependent protein kinase enhances calcium action potentials of bag cell neurons in cell culture
Kaczmarek LK, Jennings KR, Strumwasser F, Nairn AC, Walter U, Wilson FD, Greengard P. Microinjection of catalytic subunit of cyclic AMP-dependent protein kinase enhances calcium action potentials of bag cell neurons in cell culture. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 7487-7491. PMID: 6261262, PMCID: PMC350530, DOI: 10.1073/pnas.77.12.7487.Peer-Reviewed Original ResearchConceptsCalcium action potentialsBag cell neuronsAction potentialsCell neuronsInput resistanceCalcium antagonistsControl injectionsIntracellular injectionAbdominal ganglionPotassium channelsProtein kinaseNeuronsPrimary culturesInjected cellsInjectionIntracellular microinjectionMembrane potentialSubthreshold oscillationsAMP-dependent protein kinaseMicroinjectionCell culturesCyclic AMP-dependent protein kinaseSpike enhancementCatalytic subunitExtracellular medium