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 Research
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 Statements
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 abnormalities
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
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
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