2014
Use of label-free optical biosensors to detect modulation of potassium channels by G-protein coupled receptors.
Fleming MR, Shamah SM, Kaczmarek LK. Use of label-free optical biosensors to detect modulation of potassium channels by G-protein coupled receptors. Journal Of Visualized Experiments 2014, e51307. PMID: 24562095, PMCID: PMC4122194, DOI: 10.3791/51307.Peer-Reviewed Original ResearchConceptsG protein-coupled receptorsOptical biosensorPlasma membraneLabel-free optical biosensorProtein-protein interactionsIon channelsChannel-protein interactionsExcitable cell typesReceptor tyrosine kinasesProtein-coupled receptorsLigand-induced changesCell surface receptorsPotassium channelsRegulatory proteinsTyrosine kinaseG proteinsProtein behaviorSodium-activated potassium channelsExogenous labelsPhysiological relevanceCell adhesionLiving cellsCell typesHeteromeric channelsSurface receptors
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
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
1996
Insulin receptor in Aplysia neurons: characterization, molecular cloning, and modulation of ion currents
Jonas E, Knox R, Kaczmarek L, Schwartz J, Solomon D. Insulin receptor in Aplysia neurons: characterization, molecular cloning, and modulation of ion currents. Journal Of Neuroscience 1996, 16: 1645-1658. PMID: 8774433, PMCID: PMC6578688, DOI: 10.1523/jneurosci.16-05-01645.1996.Peer-Reviewed Original ResearchMeSH KeywordsAction PotentialsAmino Acid SequenceAnimalsAplysiaBase SequenceCalcium ChannelsCloning, MolecularDNA, ComplementaryElectrophysiologyImmunohistochemistryInsulinIon ChannelsMolecular ProbesMolecular Sequence DataNeuronsPotassium ChannelsProtein-Tyrosine KinasesReceptor, InsulinTissue DistributionConceptsBag cell neuronsInsulin receptorInsulin-like peptidesImmunocytochemical staining showCell neuronsTyrosine kinase receptorsVertebrate insulinsMolecular cloningHerbimycin ATyrosine residuesTyrosine kinaseKinase receptorsInsulin-like growth factor-1Factor 1Staining showsVoltage-clamped neuronsVoltage-dependent Ca2Growth factor-1Aplysia californicaAplysia neuronsNervous systemReceptorsAction potentialsNeuronsInsulin
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