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
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
2001
Aplysia Ror Forms Clusters on the Surface of Identified Neuroendocrine Cells
McKay S, Hislop J, Scott D, Bulloch A, Kaczmarek L, Carew T, Sossin W. Aplysia Ror Forms Clusters on the Surface of Identified Neuroendocrine Cells. Molecular And Cellular Neuroscience 2001, 17: 821-841. PMID: 11358481, DOI: 10.1006/mcne.2001.0977.Peer-Reviewed Original ResearchMeSH KeywordsAge FactorsAmino Acid SequenceAnimalsAntibody SpecificityAplysiaBase SequenceCaenorhabditis elegans ProteinsCell CompartmentationCells, CulturedCloning, MolecularGanglia, InvertebrateImmunohistochemistryMolecular Sequence DataNeuronsNeurosecretory SystemsReceptor Protein-Tyrosine KinasesReceptor Tyrosine Kinase-like Orphan ReceptorsReceptors, Cell SurfaceRNA, MessengerConceptsBag cell neuronsNeuroendocrine bag cell neuronsROR receptorsCultured bag cell neuronsRegulation of growthReceptor tyrosine kinasesMarine mollusk Aplysia californicaPeripheral neuronal processesMollusk Aplysia californicaCellular polarityFunctional domainsTyrosine kinaseIntracellular organellesCell surfaceProteinNeuroendocrine cellsKinaseAplysia californicaRelease sitesNeuronal processesOrganellesNeuronal populationsForm clustersGanglionic neuropilReceptors
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
1993
Mode-switching of a voltage-gated cation channel is mediated by a protein kinase A-regulated tyrosine phosphatase
Wilson G, Kaczmarek L. Mode-switching of a voltage-gated cation channel is mediated by a protein kinase A-regulated tyrosine phosphatase. Nature 1993, 366: 433-438. PMID: 8247151, DOI: 10.1038/366433a0.Peer-Reviewed Original ResearchConceptsVoltage-gated cation channelsTyrosine phosphataseProtein kinase A. MoreoverProtein kinase ACation channelsAplysia bag cell neuronsBag cell neuronsKinase ATyrosine kinasePatch-clamp studiesPhosphataseGating modesCell neuronsA. MoreoverNeuronal excitabilityNervous system tissueKinaseCentral nervous system tissueEnzyme
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
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
Phorbol Esters, Protein Phosphorylation and the Regulation of Neuronal Ion Channels
Kaczmarek L. Phorbol Esters, Protein Phosphorylation and the Regulation of Neuronal Ion Channels. Journal Of Experimental Biology 1986, 124: 375-392. PMID: 2428907, DOI: 10.1242/jeb.124.1.375.Peer-Reviewed Original ResearchConceptsProtein kinase CKinase CProtein kinase C resultsPhorbol esterNeuronal ion channelsProtein phosphorylationPlasma membraneLipid environmentIntact cellsIon channelsSuch activatorsEndogenous diacylglycerolVertebratesDiacylglycerolSynthetic diacylglycerolPhosphatidyl serineActivatorEndogenous electrical propertiesInactive speciesSynaptic transmissionInvertebratesCalcium channelsKinasePhosphorylationNervous system