2020
Functional interactions of ion channels with the actin cytoskeleton: does coupling to dynamic actin regulate NMDA receptors?
Shaw JE, Koleske AJ. Functional interactions of ion channels with the actin cytoskeleton: does coupling to dynamic actin regulate NMDA receptors? The Journal Of Physiology 2020, 599: 431-441. PMID: 32034761, PMCID: PMC7416480, DOI: 10.1113/jp278702.Peer-Reviewed Original ResearchConceptsActin cytoskeletonIon channelsPostsynaptic compartmentsCytoskeletal protein actinActin binding proteinsNeurotransmitter release machineryNeurotransmitter receptorsProtein actinSynaptic neurotransmitter receptorsΑ-actininMolecular mechanismsBinding proteinCytoskeletonMolecular linkageFunctional interactionRelease machineryDiverse collectionActinNMDA receptorsTraffickingChannel openingProteinVoltage-gated NaReceptorsCompartments
2019
A silent agonist of α7 nicotinic acetylcholine receptors modulates inflammation ex vivo and attenuates EAE
Godin J, Roy P, Quadri M, Bagdas D, Toma W, Narendrula-Kotha R, Kishta O, Damaj M, Horenstein N, Papke R, Simard A. A silent agonist of α7 nicotinic acetylcholine receptors modulates inflammation ex vivo and attenuates EAE. Brain Behavior And Immunity 2019, 87: 286-300. PMID: 31874200, PMCID: PMC7604877, DOI: 10.1016/j.bbi.2019.12.014.Peer-Reviewed Original ResearchConceptsNicotinic acetylcholine receptorsSilent agonistInflammatory painCytokine productionΑ7 nAChRsAnimal modelsAcetylcholine receptorsΑ7 nicotinic acetylcholine receptorNon-neuronal nAChRsExperimental autoimmune encephalomyelitisChronic inflammatory painAnti-inflammatory compoundsInflammation ex vivoChannel openingAutoimmune encephalomyelitisAntagonist mecamylamineMultiple sclerosisInflammatory disordersModulates inflammationMacrophage numbersDisease manifestationsNervous systemReceptor desensitizationInflammationAgonists
2018
Pkd2l1 is required for mechanoception in cerebrospinal fluid-contacting neurons and maintenance of spine curvature
Sternberg JR, Prendergast AE, Brosse L, Cantaut-Belarif Y, Thouvenin O, Orts-Del’Immagine A, Castillo L, Djenoune L, Kurisu S, McDearmid JR, Bardet PL, Boccara C, Okamoto H, Delmas P, Wyart C. Pkd2l1 is required for mechanoception in cerebrospinal fluid-contacting neurons and maintenance of spine curvature. Nature Communications 2018, 9: 3804. PMID: 30228263, PMCID: PMC6143598, DOI: 10.1038/s41467-018-06225-x.Peer-Reviewed Original ResearchConceptsCentral canalCSF-cNsSpontaneous activityCSF flowCerebrospinal fluid-contacting neuronsSpine curvatureCSF-contacting neuronsCerebrospinal fluid flowSpinal cordIdiopathic scoliosisSingle-channel openingsCalcium activityPKD2L1 channelPKD2L1Mechanosensory cellsNeuronsCanalChannel openingMechanoceptionKyphosisCilia motilityCord
2006
Pharmacological activation and inhibition of Slack (Slo2.2) channels
Yang B, Gribkoff VK, Pan J, Damagnez V, Dworetzky SI, Boissard CG, Bhattacharjee A, Yan Y, Sigworth FJ, Kaczmarek LK. Pharmacological activation and inhibition of Slack (Slo2.2) channels. Neuropharmacology 2006, 51: 896-906. PMID: 16876206, DOI: 10.1016/j.neuropharm.2006.06.003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Infective Agents, LocalBepridilBithionolCalcium Channel BlockersCell Line, TransformedDose-Response Relationship, DrugDose-Response Relationship, RadiationElectric StimulationEnzyme ActivationEnzyme InhibitorsHumansMembrane PotentialsOocytesPatch-Clamp TechniquesPotassium Channels, Calcium-ActivatedQuinidineTransfectionXenopusConceptsSlack channelsConcentration-dependent mannerIschemic injuryPharmacological activationKNa channelsMammalian brainFiring ratePharmacological propertiesChannel subunitsReversible increaseChannel activityCell linesBepridilHEK cellsRobust activatorNeuronsStable cell linesInhibitionExcised patchesXenopus oocytesPresent studyBithionolChannel openingSpecific roleMembrane patchesPolicing the Ball: A New Potassium Channel Subunit Determines Inactivation Rate
Kaczmarek LK. Policing the Ball: A New Potassium Channel Subunit Determines Inactivation Rate. Neuron 2006, 49: 642-644. PMID: 16504937, DOI: 10.1016/j.neuron.2006.02.011.Peer-Reviewed Original Research
2005
Subunit arrangement and function in NMDA receptors
Furukawa H, Singh SK, Mancusso R, Gouaux E. Subunit arrangement and function in NMDA receptors. Nature 2005, 438: 185-192. PMID: 16281028, DOI: 10.1038/nature04089.Peer-Reviewed Original ResearchConceptsHeteromeric ion channelsNR1-NR2AMammalian central nervous systemSlow channel openingChannel openingHeterodimer interfaceTransduction cascadeIon channel openingSubunit arrangementSubunit interfaceIon channelsNR2 subunitsReceptor functionChannel deactivationNMDA receptorsNMDA receptor functionReceptorsExcitatory neurotransmissionFunctional unitsCentral nervous systemNR1GlutamateGlycineNervous systemHeterodimersRequirement of Voltage-Gated Calcium Channel ß4 Subunit for T Lymphocyte Functions
Badou A, Basavappa S, Desai R, Peng YQ, Matza D, Mehal WZ, Kaczmarek LK, Boulpaep EL, Flavell RA. Requirement of Voltage-Gated Calcium Channel ß4 Subunit for T Lymphocyte Functions. Science 2005, 307: 117-121. PMID: 15637280, DOI: 10.1126/science.1100582.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium Channels, L-TypeCalcium SignalingCD4-Positive T-LymphocytesCytokinesDNA-Binding ProteinsIon Channel GatingLymphocyte ActivationMembrane PotentialsMiceMice, Inbred C3HMice, Inbred C57BLMutationNFATC Transcription FactorsNuclear ProteinsPatch-Clamp TechniquesPhosphorylationProtein SubunitsReceptors, Antigen, T-CellT-LymphocytesTranscription FactorsConceptsT lymphocytesCalcium channelsVoltage-gated calcium channelsT lymphocyte functionT cell receptor stimulationCell receptor stimulationCytokine productionLymphocyte functionCalcium influxReceptor stimulationCalcium responseCalcium entryTranscription factor NFATCav1 channelsLymphocytesAlpha1 subunitCav channelsNormal functionNonexcitable cellsDisplay impairmentsExcitable cellsChannel openingMolecular identityDiverse physiological processesPhysiological processes
1997
ATP regulation of a swelling‐activated osmolyte channel in skate hepatocytes
Ballatori N, Boyer J. ATP regulation of a swelling‐activated osmolyte channel in skate hepatocytes. Journal Of Experimental Zoology 1997, 279: 471-475. PMID: 9392868, DOI: 10.1002/(sici)1097-010x(19971201)279:5<471::aid-jez9>3.0.co;2-l.Peer-Reviewed Original ResearchConceptsChannel blockersTaurine effluxRegulatory volume decreaseVolume-activated taurine effluxRelease of taurineSkate hepatocytesIntracellular ATPIon channel blockersChloride permeability ratioIntracellular ATP levelsControl levelsOsmolyte channelIntracellular organic osmolytesWhole cell preparationsCell preparationsATP levelsBlockersHypotonic swellingChannel openingHepatocytesVolume decreaseAdditional mechanismEffluxAgonist-induced closure of constitutively open γ-aminobutyric acid channels with mutated M2 domains
Pan Z, Zhang D, Zhang X, Lipton S. Agonist-induced closure of constitutively open γ-aminobutyric acid channels with mutated M2 domains. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 6490-6495. PMID: 9177245, PMCID: PMC21077, DOI: 10.1073/pnas.94.12.6490.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCloning, MolecularFemaleGABA AgonistsGABA Antagonistsgamma-Aminobutyric AcidIon Channel GatingIon ChannelsMacromolecular SubstancesMembrane PotentialsMolecular Sequence DataMutagenesis, Site-DirectedOocytesOrganophosphorus CompoundsPoint MutationRatsReceptors, GABAReceptors, GlycineReceptors, NicotinicRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidVirulence Factors, BordetellaXenopus laevisConceptsLigand-gated ion channelsChannel gatingIon channelsAmino acid residuesAminobutyric acid channelsSingle-point mutantsAbsence of ligandChannel pore regionStructure-function relationshipsPoint mutantsAcid channelImportant new insightsAllosteric transitionSubunit resultsAcid residuesM2 domainConstitutive currentReceptor proteinPore regionAgonist bindingAgonist regulationSubstituting alanineM2 regionSpontaneous channel openingChannel opening
1994
Regulation of CFTR channel gating
Gadsby D, Nairn A. Regulation of CFTR channel gating. Trends In Biochemical Sciences 1994, 19: 513-518. PMID: 7531880, DOI: 10.1016/0968-0004(94)90141-4.Peer-Reviewed Original ResearchConceptsChannel gatingCystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channelAMP-dependent protein kinaseCFTR channel gatingReceptor-mediated activationRegulatory domainProtein kinaseATP hydrolysisCFTR channelsCl- channelsEpithelial cellsChannel openingComplex mechanismsCellsRecent advancesKinaseGenesPhosphorylationSerineGatingCFTRMutationsRegulationStemActivationCoupling of CFTR Cl− channel gating to an ATP hydrolysis cycle
Baukrowitz T, Hwang T, Nairn A, Gadsby D. Coupling of CFTR Cl− channel gating to an ATP hydrolysis cycle. Neuron 1994, 12: 473-482. PMID: 7512348, DOI: 10.1016/0896-6273(94)90206-2.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorATP hydrolysis cycleHydrolysis cycleCFTR channelsFibrosis transmembrane conductance regulatorProtein kinase ATransmembrane conductance regulatorATP hydrolysisKinase AConductance regulatorNucleoside triphosphatesChannel openingInorganic phosphate analogueATPPhosphate analogueCardiac myocytesInorganic phosphateMean open timeRegulatorHydrolysis productsBeF3Open timeCycleTriphosphateRegulation of CFTR channel gating.
Gadsby D, Hwang T, Baukrowitz T, Nagel G, Horie M, Nairn A. Regulation of CFTR channel gating. The Journal Of Physiological Sciences 1994, 44 Suppl 2: s183-92. PMID: 7752525.Peer-Reviewed Original ResearchConceptsNon-hydrolyzable ATP analog AMP-PNPCystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channelAMP-PNPCFTR channel gatingProtein kinase A (PKA) phosphorylationATP analogue AMP-PNPAnalogue AMP-PNPCFTR's twoA PhosphorylationATP hydrolysisChannel gatingCl- channelsChannel openingNBDRegulationMultiple sitesPhosphorylationCFTROrthovanadateATPGatingDomain
1993
ATP modulates the function of inositol 1,4,5-trisphosphate-gated channels at two sites
Bezprozvanny I, Ehrlich B. ATP modulates the function of inositol 1,4,5-trisphosphate-gated channels at two sites. Neuron 1993, 10: 1175-1184. PMID: 7686381, DOI: 10.1016/0896-6273(93)90065-y.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCalciumCalcium ChannelsCerebellumDogsEndoplasmic ReticulumInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsIon Channel GatingIon ChannelsKineticsLipid BilayersMathematicsMicrosomesModels, NeurologicalReceptors, Cell SurfaceReceptors, Cytoplasmic and NuclearSignal TransductionConceptsPresence of IP3Effect of ATPTrisphosphate-gated channelsIntracellular Ca2Average durationAllosteric modulationSingle-channel levelFunction of inositolIP3 receptorChannel activityCell viabilityReceptorsTrisphosphate receptorIP3Channel openingPermeable channelsCa2ATPInositolAddition of ATPNonhydrolyzable ATP analogChannel conductanceChannel incorporation
1986
Open channel noise. II. A test for coupling between current fluctuations and conformational transitions in the acetylcholine receptor
Sigworth F. Open channel noise. II. A test for coupling between current fluctuations and conformational transitions in the acetylcholine receptor. Biophysical Journal 1986, 49: 1041-1046. PMID: 2423148, PMCID: PMC1329684, DOI: 10.1016/s0006-3495(86)83732-8.Peer-Reviewed Original Research
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