2009
PI3K/Akt signalling‐mediated protein surface expression sensed by 14‐3‐3 interacting motif
Chung J, Okamoto Y, Coblitz B, Li M, Qiu Y, Shikano S. PI3K/Akt signalling‐mediated protein surface expression sensed by 14‐3‐3 interacting motif. The FEBS Journal 2009, 276: 5547-5558. PMID: 19691494, PMCID: PMC4301307, DOI: 10.1111/j.1742-4658.2009.07241.x.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCattleCell LineCell MembraneHumansMembrane ProteinsPhosphatidylinositol 3-KinasesPhosphorylationProtein BindingProto-Oncogene Proteins c-aktReceptors, G-Protein-CoupledReceptors, PeptideRecombinant Fusion ProteinsSignal TransductionTransfectionConceptsCell surface expressionMembrane proteinsEndoplasmic reticulum localization signalsSurface expressionDifferent extracellular signalsFetal bovine serumPost-translational modificationsSpecific protein localizationG protein-coupled receptorsDominant-negative AktC-terminal sequencesKinase B pathwayProtein-coupled receptorsGenetic screenCell surface membraneLocalization signalCargo proteinsActive kinaseExtracellular signalingExtracellular signalsProtein localizationProtein surface expressionKinase activityBovine serumCellular responses
2008
Ion channels that control fertility in mammalian spermatozoa
Navarro B, Kirichok Y, Chung JJ, Clapham DE. Ion channels that control fertility in mammalian spermatozoa. The International Journal Of Developmental Biology 2008, 52: 607-613. PMID: 18649274, PMCID: PMC4297656, DOI: 10.1387/ijdb.072554bn.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsMammalian spermatozoaGenetic deletion strategiesMammalian spermPhysiological roleIon channelsDeletion strategyIon channel currentsHyperactivated motilityChannel currentsUnambiguous identificationIntracellular alkalinizationWhole-cell voltage clampSpermatozoaGenesTechnical advancesVoltage clampSpermMotilityExpressionFertilizationCa2FertilityIdentification
2005
Biochemical characterization of the native Kv2.1 potassium channel
Chung J, Li M. Biochemical characterization of the native Kv2.1 potassium channel. The FEBS Journal 2005, 272: 3743-3755. PMID: 16008572, DOI: 10.1111/j.1742-4658.2005.04802.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineChromatography, AffinityChromatography, GelHumansMolecular Sequence DataPotassium Channels, Voltage-GatedProsencephalonProtein BindingProteomicsRatsRats, Sprague-DawleyShab Potassium ChannelsSolubilitySpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationConceptsBiochemical characterizationChannel complexLarge macromolecular complexesPotassium channelsPore-forming subunitRecombinant cell linesEukaryotic cellsPore complexFunctional diversityPosttranslational regulationKv2.2 subunitsSubunit assemblyVariety of tissuesMacromolecular complexesKv2.1 potassium channelOligomeric sizeNative polypeptideExpression cloningNative rat brainPhysiological relevanceRectifier potassium channelGel filtration chromatographySubunitsMRNA distributionModulatory subunit
2000
Functional impairment of lens aquaporin in two families with dominantly inherited cataracts
Francis P, Chung JJ, Yasui M, Berry V, Moore A, Wyatt MK, Wistow G, Bhattacharya SS, Agre P. Functional impairment of lens aquaporin in two families with dominantly inherited cataracts. Human Molecular Genetics 2000, 9: 2329-2334. PMID: 11001937, DOI: 10.1093/oxfordjournals.hmg.a018925.Peer-Reviewed Original ResearchConceptsAQP0 proteinMutant proteinsWater channel activityDominant-negative behaviorOocyte plasma membraneOocyte expression systemXenopus laevis oocyte expression systemLens aquaporinsDifferent point mutationsPlasma membraneExpression systemSevere defectsPoint mutationsMissense mutationsProteinChannel activityAQP2 proteinRecessive traitFunctional defectsPathophysiological relevanceMutationsCongenital cataractFamilyCataract formationAQP0