2012
An evolutionarily conserved mode of modulation of Shaw‐like K+ channels
Cotella D, Hernandez‐Enriquez B, Duan Z, Wu X, Gazula V, Brown MR, Kaczmarek LK, Sesti F. An evolutionarily conserved mode of modulation of Shaw‐like K+ channels. The FASEB Journal 2012, 27: 1381-1393. PMID: 23233530, PMCID: PMC3606535, DOI: 10.1096/fj.12-222778.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrain StemCaenorhabditis elegansEvolution, MolecularMembrane PotentialsMiceMice, Inbred C57BLNeuronsPhosphorylationShaw Potassium ChannelsConceptsEffect of phosphorylationC. elegansACP-2Acid phosphataseMammalian homologMammalian homologueCaenorhabditis elegansMouse nervous systemRegulatory partnersBiochemical experimentsMolecular mechanismsElegansBehavioral defectsMode of modulationPhosphorylationPharmacological disruptionShaw familyMammalian brainSubset of neuronsVentricular zonePhosphataseModel systemNervous systemMice resultsElectrophysiological analysis
2003
The Sodium-Activated Potassium Channel Is Encoded by a Member of the Slo Gene Family
Yuan A, Santi CM, Wei A, Wang Z, Pollak K, Nonet M, Kaczmarek L, Crowder CM, Salkoff L. The Sodium-Activated Potassium Channel Is Encoded by a Member of the Slo Gene Family. Neuron 2003, 37: 765-773. PMID: 12628167, DOI: 10.1016/s0896-6273(03)00096-5.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCaenorhabditis elegansCells, CulturedFemaleLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMolecular Sequence DataMultigene FamilyMutationNerve Tissue ProteinsOocytesPotassium ChannelsPotassium Channels, Calcium-ActivatedPotassium Channels, Sodium-ActivatedSequence Homology, Amino AcidSodiumXenopus
1998
Formation of intermediate-conductance calcium-activated potassium channels by interaction of Slack and Slo subunits
Joiner W, Tang M, Wang L, Dworetzky S, Boissard C, Gan L, Gribkoff V, Kaczmarek L. Formation of intermediate-conductance calcium-activated potassium channels by interaction of Slack and Slo subunits. Nature Neuroscience 1998, 1: 462-469. PMID: 10196543, DOI: 10.1038/2176.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsElectric ConductivityIntermediate-Conductance Calcium-Activated Potassium ChannelsIsomerismLarge-Conductance Calcium-Activated Potassium ChannelsMolecular Sequence DataNerve Tissue ProteinsPotassium ChannelsPotassium Channels, Calcium-ActivatedPotassium Channels, Sodium-ActivatedConceptsCalcium-activated potassium channelsIntracellular calciumNervous systemIntermediate-conductance calcium-activated potassium channelsPotassium channelsLarge-conductance calcium-activated potassium channelsControl of excitabilitySlo subunitIntermediate conductance channelPotassium channel genesPharmacological propertiesIntermediate conductanceCytoplasmic calciumChannel subunitsSlo channelsSlack channelsChannel genesSingle-channel conductanceUnitary conductanceCalciumExcitabilitySLOSecretion
1995
A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem
Ketchum K, Joiner W, Sellers A, Kaczmarek L, Goldstein S. A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem. Nature 1995, 376: 690-695. PMID: 7651518, DOI: 10.1038/376690a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCells, CulturedDNA PrimersDrosophilaMolecular Sequence DataOocytesPatch-Clamp TechniquesPotassiumPotassium ChannelsProtein ConformationRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSodiumXenopus laevisConceptsP domainPotassium channel proteinCaenorhabditis elegansCommon structural motifChannel proteinsPore domainCellular membranesPrimary structureExcised membrane patchesSignature sequencesFlow of ionsAmino acidsXenopus laevisSelective currentMembrane potentialStructural motifsMembrane patchesPotassium channelsExternal divalent cationsDivalent cationsFunctional propertiesElegansVoltage-dependent mannerGenomeDomain