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
2022
C2cd6-encoded CatSperτ targets sperm calcium channel to Ca2+ signaling domains in the flagellar membrane
Hwang JY, Wang H, Lu Y, Ikawa M, Chung JJ. C2cd6-encoded CatSperτ targets sperm calcium channel to Ca2+ signaling domains in the flagellar membrane. Cell Reports 2022, 38: 110226. PMID: 34998468, PMCID: PMC8857959, DOI: 10.1016/j.celrep.2021.110226.Peer-Reviewed Original ResearchConceptsFlagellar membraneFlagellar membrane targetingC2 domain proteinsCatSper channelsCatSper channel complexMammalian sperm cellsSperm hyperactivated motilityMale fertilityMembrane targetingTrafficking machineryDomain proteinsLoss of functionHyperactivated motilitySpatiotemporal CaChannel assemblyMolecular mechanismsSperm cellsChannel complexFlagellaMotilityC2CD6MembraneCalcium channelsMachineryProtein
2020
3D in situ imaging of female reproductive tract reveals molecular signatures of fertilizing spermatozoa in mice
Ded L, Hwang JY, Miki K, Shi HF, Chung JJ. 3D in situ imaging of female reproductive tract reveals molecular signatures of fertilizing spermatozoa in mice. ELife 2020, 9: e62043. PMID: 33078708, PMCID: PMC7707823, DOI: 10.7554/elife.62043.Peer-Reviewed Original ResearchConceptsFemale reproductive tractFemale tractCalcium channel complexSitu molecular imagingReproductive tractMolecular insightsSuccessful fertilizationCatSper channelsMolecular signaturesSperm cellsSperm selectionChannel complexMouse spermatozoaFertilization siteSpermSperm migrationSpermatozoaMammalsPhosphorylationCatSper1ProteinSitu imagingAcrosomeUtero-tubal junctionSelection
2017
CatSperζ regulates the structural continuity of sperm Ca2+ signaling domains and is required for normal fertility
Chung JJ, Miki K, Kim D, Shim SH, Shi HF, Hwang JY, Cai X, Iseri Y, Zhuang X, Clapham DE. CatSperζ regulates the structural continuity of sperm Ca2+ signaling domains and is required for normal fertility. ELife 2017, 6: e23082. PMID: 28226241, PMCID: PMC5362262, DOI: 10.7554/elife.23082.Peer-Reviewed Original ResearchConceptsMammalian female reproductive tractSevere male subfertilityFemale reproductive tractIon channel complexNovel subunitCatSper complexEvolutionary adaptationMale subfertilityReproductive tractMouse spermSperm Ca2Normal fertilityTargeted disruptionSperm cellsFlagellaChannel complexFemale uterusSubunitsEpididymal spermatozoaSpermComplexesFertilizationSubfertilityUterusMice
2011
A novel gene required for male fertility and functional CATSPER channel formation in spermatozoa
Chung JJ, Navarro B, Krapivinsky G, Krapivinsky L, Clapham DE. A novel gene required for male fertility and functional CATSPER channel formation in spermatozoa. Nature Communications 2011, 2: 153. PMID: 21224844, PMCID: PMC3999383, DOI: 10.1038/ncomms1153.Peer-Reviewed Original ResearchHyperactivation of motilityCatSper channel complexMale fertilityChannel α-subunitsNovel subunitNovel genesHyperactivated motilitySperm proteinsGene productsChannel assemblyAuxiliary subunitsΑ-subunitSuccessful fertilizationCalcium signalingSelective poresSpermatozoa lackChannel functionSubunitsSperm Ca2Channel complexCation channelsGenesChannel formationProteinAcrosome reaction
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