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
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
2002
Functional diversity of protein C-termini: more than zipcoding?
Chung J, Shikano S, Hanyu Y, Li M. Functional diversity of protein C-termini: more than zipcoding? Trends In Cell Biology 2002, 12: 146-150. PMID: 11859027, DOI: 10.1016/s0962-8924(01)02241-3.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsProtein C-terminusC-terminusProtein domainsTermini of proteinsCell biological processesTerminal sequence motifCell biological functionsProtein targetingTPR domainFunctional proteomicsFunctional diversitySequence motifsAlpha-carboxyl groupPosttranslational modificationsSequence diversityMacromolecular complexesProtein degradationDiverse functionsTerminal alpha-carboxyl groupBiological processesRecognition signatureTemporal specificityDiversityTerminal epitopesCombination of diversity