2015
Ion Channels Are Membrane Proteins
Levitan I, Kaczmarek L. Ion Channels Are Membrane Proteins. 2015, 85-102. DOI: 10.1093/med/9780199773893.003.0005.ChaptersMembrane-spanning segmentsHomologous domainsPrimary subunitIon channelsFunctional potassium channelsPotassium channelsVoltage-dependent ion channelsThree-dimensional structureMembrane proteinsSodium channelsMutational analysisProtein regionsVoltage-gated sodiumChannel proteinsChannel gatingProtein conformationStructural modulesChannel poreGlobal changeVoltage-dependent activationVoltage-dependent channelsSubunitsProteinOverall structureIon selectivityDiversity in the Structure and Function of Ion Channels
Levitan I, Kaczmarek L. Diversity in the Structure and Function of Ion Channels. 2015, 127-150. DOI: 10.1093/med/9780199773893.003.0007.ChaptersIon channelsPotassium channelsFormation of heterotetramersAlternative splicingIndividual genesMultiple genesAuxiliary subunitsTwo-poreDiverse familyHuman diseasesMolecular biologyMessenger RNASubunitsDiversityGenesRectifier channelsVoltage-dependent sodiumChannel propertiesPatch-clamp techniqueSplicingDifferent mechanismsHeterotetramerClamp techniqueElectrophysiological measurementsRNA
2010
Kv1.3 is the exclusive voltage‐gated K+ channel of platelets and megakaryocytes: roles in membrane potential, Ca2+ signalling and platelet count
McCloskey C, Jones S, Amisten S, Snowden RT, Kaczmarek LK, Erlinge D, Goodall AH, Forsythe ID, Mahaut‐Smith M. Kv1.3 is the exclusive voltage‐gated K+ channel of platelets and megakaryocytes: roles in membrane potential, Ca2+ signalling and platelet count. The Journal Of Physiology 2010, 588: 1399-1406. PMID: 20308249, PMCID: PMC2876798, DOI: 10.1113/jphysiol.2010.188136.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlood PlateletsCalcium SignalingCell SizeDNA, ComplementaryHumansIn Vitro TechniquesKv1.3 Potassium ChannelMegakaryocytesMembrane PotentialsMiceMice, Inbred C57BLPatch-Clamp TechniquesPlatelet CountReverse Transcriptase Polymerase Chain ReactionScorpion VenomsSecond Messenger SystemsConceptsLarge ionic conductanceMembrane potentialHuman plateletsKv alphaMegakaryocyte developmentAncillary subunitsQuantitative RT-PCRMolecular levelKv channelsRole of Kv1.3MegakaryocytesKv1.3RT-PCRWild-type miceKv currentsSubunitsSignalingMiceApoptosisMargatoxinPlatelet activationRoleIonic conductancesPlateletsActivation
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
2008
PKC-Induced Intracellular Trafficking of CaV2 Precedes Its Rapid Recruitment to the Plasma Membrane
Zhang Y, Helm JS, Senatore A, Spafford JD, Kaczmarek LK, Jonas EA. PKC-Induced Intracellular Trafficking of CaV2 Precedes Its Rapid Recruitment to the Plasma Membrane. Journal Of Neuroscience 2008, 28: 2601-2612. PMID: 18322103, PMCID: PMC2830008, DOI: 10.1523/jneurosci.4314-07.Peer-Reviewed Original ResearchConceptsProtein kinase CActivation of PKCPlasma membraneGrowth conesLatrunculin BIntracellular traffickingActin polymerizationIntact microtubulesIntact actinKinase CChannel insertionPKC activationIon channelsMicrotubule polymerizationRapid recruitmentOrganellesLamellipodiumSubunitsMicrotubulesActinMembraneActivationRecruitmentCone terminalsNew sites
1997
Properties and regulation of the minK potassium channel protein
Kaczmarek L, Blumenthal E. Properties and regulation of the minK potassium channel protein. Physiological Reviews 1997, 77: 627-641. PMID: 9234960, DOI: 10.1152/physrev.1997.77.3.627.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsMinK proteinSingle transmembrane segmentPotassium channel proteinChannel-forming subunitTransmembrane segmentsMink genesChannel proteinsSecond messengerAmino acidsKvLQT1 channelsXenopus oocytesProteinNative currentsEpithelial cellsMinK mRNAIon selectivityVoltage-dependent potassium currentsResultant channelPotassium currentStrong candidateCellsGenesSubunitsVestibular organsMessenger