2009
The N-Terminal Domain of Slack Determines the Formation and Trafficking of Slick/Slack Heteromeric Sodium-Activated Potassium Channels
Chen H, Kronengold J, Yan Y, Gazula VR, Brown MR, Ma L, Ferreira G, Yang Y, Bhattacharjee A, Sigworth FJ, Salkoff L, Kaczmarek LK. The N-Terminal Domain of Slack Determines the Formation and Trafficking of Slick/Slack Heteromeric Sodium-Activated Potassium Channels. Journal Of Neuroscience 2009, 29: 5654-5665. PMID: 19403831, PMCID: PMC3688047, DOI: 10.1523/jneurosci.5978-08.2009.Peer-Reviewed Original ResearchConceptsTerminal domainN-terminal domainAlternative splice variantsPotassium channelsSubcellular localizationPlasma membraneMolecular explanationHeteromer formationSplice variantsHeteromeric channelsDistinct rolesSingle-channel levelSubunitsUnitary conductanceCentral neuronsSlack channelsImmunocytochemical studyFiring patternsDomainLocalizationNeuronsGenesTraffickingChannel levelHomomers
1994
The minK potassium channel exists in functional and nonfunctional forms when expressed in the plasma membrane of Xenopus oocytes
Blumenthal E, Kaczmarek L. The minK potassium channel exists in functional and nonfunctional forms when expressed in the plasma membrane of Xenopus oocytes. Journal Of Neuroscience 1994, 14: 3097-3105. PMID: 7514215, PMCID: PMC6577436, DOI: 10.1523/jneurosci.14-05-03097.1994.Peer-Reviewed Original ResearchConceptsN-terminal domainMinK proteinPlasma membraneInjected mRNAXenopus oocytesMinK potassium channelsFunctional potassium channelsPotassium channelsAmino acid epitopeProtein sequencesLevels of proteinMink genesLive oocytesIntracellular cAMP levelsKinetics of activationProteinOocytesMinK mRNANonfunctional formMRNASurface expressionRNAMinK currentsMRNA levelsCAMP levels