2023
A CUG-initiated CATSPERθ functions in the CatSper channel assembly and serves as a checkpoint for flagellar trafficking
Huang X, Miyata H, Wang H, Mori G, Iida-Norita R, Ikawa M, Percudani R, Chung J. A CUG-initiated CATSPERθ functions in the CatSper channel assembly and serves as a checkpoint for flagellar trafficking. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2304409120. PMID: 37725640, PMCID: PMC10523455, DOI: 10.1073/pnas.2304409120.Peer-Reviewed Original ResearchConceptsChannel assemblySperm flagellaTransmembrane domain-containing proteinsSperm tail formationDomain-containing proteinsCatSper channel complexMale fertilityFlagellar traffickingMacromolecular complexesTail formationPhysiological roleSuccessful fertilizationCalcium signalingCatSper channelsFlagellaGenetic abrogationChannel complexNormal expressionDimer formationSpermatid cellsProteinCheckpointHyperactivated motilityAssemblyPotential role
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