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
CatSper and Two-Pore channels (TPC) in GtoPdb v.2022.1
Chung J, Clapham D, Garbers D, Grimm C, Ren D. CatSper and Two-Pore channels (TPC) in GtoPdb v.2022.1. IUPHAR/BPS Guide To Pharmacology CITE 2022, 2022 DOI: 10.2218/gtopdb/f70/2022.1.Peer-Reviewed Original ResearchTwo-pore channelsCatSper channelsCatSper subunitsLike subunitsPlasma membraneSperm tailPrinciple pieceCatSperIndividual domainsTPC1TPC3Number of TMGtoPdb v.TPC2SubunitsProteinVoltage-activated calcium channelsPermeant channelsChannel inhibitorsPatch clampCalcium channelsEndosomesMammalsCatSper1LysosomesC2cd6-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
2019
CatSper and Two-Pore channels (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database
Chung J, Clapham D, Garbers D, Ren D. CatSper and Two-Pore channels (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database. IUPHAR/BPS Guide To Pharmacology CITE 2019, 2019 DOI: 10.2218/gtopdb/f70/2019.4.Peer-Reviewed Original ResearchTwo-pore channelsCatSper channelsCatSper subunitsLike subunitsPlasma membraneSperm tailIUPHAR/BPS GuidePrinciple pieceCatSperIndividual domainsTPC1Number of TMTPC3TPC2SubunitsProteinVoltage-activated calcium channelsPermeant channelsChannel inhibitorsPatch clampCalcium channelsEndosomesMammalsPharmacology DatabaseCatSper1
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
2003
Genome-wide Analyses of Carboxyl-terminal Sequences*
Chung JJ, Yang H, Li M. Genome-wide Analyses of Carboxyl-terminal Sequences*. Molecular & Cellular Proteomics 2003, 2: 173-181. PMID: 12682279, DOI: 10.1074/mcp.m300008-mcp200.Peer-Reviewed Original ResearchConceptsCarboxyl-terminal sequenceBiological functionsYeast open reading framesTerminal sequenceGenome-wide analysisProtein carboxyl terminusCarboxyl-terminal signalUnknown biological functionEndoplasmic reticulum retentionSpecific biological functionsOpen reading frameHDEL sequenceProteome levelSequence motifsEntire proteomeProteome databaseReading frameCarboxyl terminusRecognition signatureBiochemical processesFunctional classificationProteomeSequenceDetermination of proteinProtein
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