2023
LRRC23 truncation impairs radial spoke 3 head assembly and sperm motility underlying male infertility
Hwang J, Chai P, Nawaz S, Choi J, Lopez-Giraldez F, Hussain S, Bilguvar K, Mane S, Lifton R, Ahmad W, Zhang K, Chung J. LRRC23 truncation impairs radial spoke 3 head assembly and sperm motility underlying male infertility. ELife 2023, 12: rp90095. PMID: 38091523, PMCID: PMC10721216, DOI: 10.7554/elife.90095.Peer-Reviewed Original ResearchA 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
CatSper Calcium Channels: 20 Years On
Hwang J, Chung J. CatSper Calcium Channels: 20 Years On. Physiology 2022, 38: 125-140. PMID: 36512352, PMCID: PMC10085559, DOI: 10.1152/physiol.00028.2022.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsSelenoprotein TXNRD3 supports male fertility via the redox regulation of spermatogenesis
Dou Q, Turanov AA, Mariotti M, Hwang JY, Wang H, Lee SG, Paulo JA, Yim SH, Gygi SP, Chung JJ, Gladyshev VN. Selenoprotein TXNRD3 supports male fertility via the redox regulation of spermatogenesis. Journal Of Biological Chemistry 2022, 298: 102183. PMID: 35753352, PMCID: PMC9352919, DOI: 10.1016/j.jbc.2022.102183.Peer-Reviewed Original ResearchConceptsThioredoxin/glutathione reductaseThiol redox controlSperm quality controlThiol redox statusGene duplicationThiol oxidoreductasesRedox regulationProteomic analysisRedox controlGross phenotypeThioredoxin reductaseSperm maturationMovement phenotypesSperm cellsRedox statusMale reproductionKnockout animalsMale fertilityGlutathione reductaseCritical roleReductasePhenotypeTXNRD3Knockout miceSpermatogenesis3D structure and in situ arrangements of CatSper channel in the sperm flagellum
Zhao Y, Wang H, Wiesehoefer C, Shah NB, Reetz E, Hwang JY, Huang X, Wang TE, Lishko PV, Davies KM, Wennemuth G, Nicastro D, Chung JJ. 3D structure and in situ arrangements of CatSper channel in the sperm flagellum. Nature Communications 2022, 13: 3439. PMID: 35715406, PMCID: PMC9205950, DOI: 10.1038/s41467-022-31050-8.Peer-Reviewed Original ResearchConceptsCatSper complexSperm flagellaCryo-electron tomographyHigher-order organizationMammalian spermIntracellular domainStructural basisExtracellular domainTetrameric channelChannel CatSperSuccessful fertilizationFlagellar movementCatSper channelsChannel poreSitu mapSitu arrangementHuman sperm flagellumPrimary Ca2CatSperDimer formationFlagellaCentral roleSpermAtomic modelSperm motilityRedox regulation by TXNRD3 during epididymal maturation underlies capacitation-associated mitochondrial activity and sperm motility in mice
Wang H, Dou Q, Jeong KJ, Choi J, Gladyshev VN, Chung JJ. Redox regulation by TXNRD3 during epididymal maturation underlies capacitation-associated mitochondrial activity and sperm motility in mice. Journal Of Biological Chemistry 2022, 298: 102077. PMID: 35643315, PMCID: PMC9218152, DOI: 10.1016/j.jbc.2022.102077.Peer-Reviewed Original ResearchConceptsRedox regulationRedox homeostasisMolecular mechanismsSperm maturationMitochondrial sheath formationCell imaging analysisThioredoxin glutathione reductaseSperm developmentMammalian spermatozoaEpididymal transitMitochondrial ultrastructureMitochondrial activityRedox statusMale fertilityCapacitationHomeostasisMaturationRegulationMotilityFamily membersFertilizationSperm morphologySperm motilityMitochondriaBioenergeticsCatSper and its CaM‐like Ca2+ sensor EFCAB9 are necessary for the path chirality of sperm
Wiesehöfer C, Wiesehöfer M, Dankert JT, Chung J, von Ostau N, Singer BB, Wennemuth G. CatSper and its CaM‐like Ca2+ sensor EFCAB9 are necessary for the path chirality of sperm. The FASEB Journal 2022, 36: e22288. PMID: 35438819, PMCID: PMC9835897, DOI: 10.1096/fj.202101656rr.Peer-Reviewed Original ResearchConceptsNNC 55Exposure of spermMotility changesPharmacological inhibitionLateral head excursionCatSper activationIntracellular CaPhysiological stimuliCatSper channelsProtein 2Zona pellucida protein 2Zona pellucida glycoproteinsCapacitation stateCatSperHead excursionMouse spermPellucida glycoproteinsSpermSuccessful fertilizationMibefradilHigh frequencyC2cd6-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
2021
Mitochondria–cytoskeleton interactions in mammalian sperm revealed by cryoelectron tomography
Wang H, Chung JJ. Mitochondria–cytoskeleton interactions in mammalian sperm revealed by cryoelectron tomography. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2118020118. PMID: 34819381, PMCID: PMC8640839, DOI: 10.1073/pnas.2118020118.Commentaries, Editorials and LettersMolecular Evolution of CatSper in Mammals and Function of Sperm Hyperactivation in Gray Short-Tailed Opossum
Hwang JY, Maziarz J, Wagner GP, Chung JJ. Molecular Evolution of CatSper in Mammals and Function of Sperm Hyperactivation in Gray Short-Tailed Opossum. Cells 2021, 10: 1047. PMID: 33946695, PMCID: PMC8147001, DOI: 10.3390/cells10051047.Peer-Reviewed Original ResearchConceptsMolecular evolutionHigh sequence divergenceSperm-specific ion channelIQ-like motifSequence divergenceCatSper activityCatSper subunitsMolecular regulationFertilization environmentSperm hyperactivationCatSper proteinsAmerican marsupialsCatSper functionSequence analysisMarsupialsFemale reproductive tractGray Short-Tailed OpossumsEutheriansSperm flagellaCatSper channelsIon channelsCatSperCurrent understandingOpossumSperm
2020
Sperm ion channels and transporters in male fertility and infertility
Wang H, McGoldrick LL, Chung JJ. Sperm ion channels and transporters in male fertility and infertility. Nature Reviews Urology 2020, 18: 46-66. PMID: 33214707, PMCID: PMC7852504, DOI: 10.1038/s41585-020-00390-9.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsSperm ion channelsIon channelsSperm cellsMammalian sperm cellsIon signalingDynamic regulationDefective sperm functionFemale reproductive tractChannel CatSperHuman geneticsMembrane receptorsMale fertilityHealth careAttractive targetDirect electrophysiological recordingsOverall health careHuman infertilityReproductive health careSperm functionPrincipal Ca2Development of contraceptivesSperm activityGene variantsReproductive tractGenetic abnormalities3D 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
2019
Dual Sensing of Physiologic pH and Calcium by EFCAB9 Regulates Sperm Motility
Hwang JY, Mannowetz N, Zhang Y, Everley RA, Gygi SP, Bewersdorf J, Lishko PV, Chung JJ. Dual Sensing of Physiologic pH and Calcium by EFCAB9 Regulates Sperm Motility. Cell 2019, 177: 1480-1494.e19. PMID: 31056283, PMCID: PMC8808721, DOI: 10.1016/j.cell.2019.03.047.Peer-Reviewed Original Research
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
2014
Structurally Distinct Ca2+ Signaling Domains of Sperm Flagella Orchestrate Tyrosine Phosphorylation and Motility
Chung JJ, Shim SH, Everley RA, Gygi SP, Zhuang X, Clapham DE. Structurally Distinct Ca2+ Signaling Domains of Sperm Flagella Orchestrate Tyrosine Phosphorylation and Motility. Cell 2014, 157: 808-822. PMID: 24813608, PMCID: PMC4032590, DOI: 10.1016/j.cell.2014.02.056.Peer-Reviewed Original ResearchConceptsTyrosine phosphorylationSperm-specific calcium channelsSpecific protein tyrosine phosphorylationProtein tyrosine phosphorylationSuper-resolution fluorescence microscopyMammalian flagellumUnique molecular phenotypeFlagellar switchHeterogeneous sperm populationsPaternal DNASignaling domainsMolecular phenotypesCatSper channelsMature eggsPhosphorylationFluorescence microscopyDistinct Ca2FlagellaAdaptive strategiesSperm populationCascade organizationSpermUniflagellateCalcium domainsPhosphoproteomics
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
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
2001
9-cis-Retinoic acid represses transcription of the gonadotropin-releasing hormone (GnRH) gene via proximal promoter region that is distinct from all-trans-retinoic acid response element
Cho S, Chung J, Han J, Lee B, Do Han Kim, Rhee K, Kim K. 9-cis-Retinoic acid represses transcription of the gonadotropin-releasing hormone (GnRH) gene via proximal promoter region that is distinct from all-trans-retinoic acid response element. Brain Research 2001, 87: 214-222. PMID: 11245924, DOI: 10.1016/s0169-328x(01)00020-1.Peer-Reviewed Original ResearchMeSH KeywordsAlitretinoinAnimalsAntineoplastic AgentsCells, CulturedDose-Response Relationship, DrugGene Expression RegulationGonadotropin-Releasing HormoneLigandsPromoter Regions, GeneticRatsReceptors, Retinoic AcidRetinoid X ReceptorsRNA, MessengerTranscription FactorsTranscription, GeneticTransfectionTretinoinConceptsGT1-1 cellsRat GnRH promoterPromoter-driven luciferase activityRetinoid X receptorTrans-RAGnRH expressionGnRH transcriptionLuciferase activityImmortalized GnRH neuronsRXR beta expressionGnRH promoterVehicle-treated controlsGnRH mRNA levelsGonadotropin-releasing hormone gene transcriptionGnRH gene expressionGonadotropin-releasing hormone (GnRH) geneTime-related mannerGnRH promoter activityTrans retinoic acidGnRH gene transcriptionTime-dependent mannerGnRH neuronsPresent studyBeta expressionResponse element