2025
Chloride binding does not influence prestin motor speed at very high frequencies in the mouse outer hair cell
Bai J, Zhang C, Bahader I, Strenzke N, Renigunta V, Oliver D, Navaratnam D, Beckstein O, Santos-Sacchi J. Chloride binding does not influence prestin motor speed at very high frequencies in the mouse outer hair cell. Structure 2025 PMID: 40403717, DOI: 10.1016/j.str.2025.04.019.Peer-Reviewed Original Research
2010
β4-Subunit increases Slo responsiveness to physiological Ca2+ concentrations and together with β1 reduces surface expression of Slo in hair cells
Bai JP, Surguchev A, Navaratnam D. β4-Subunit increases Slo responsiveness to physiological Ca2+ concentrations and together with β1 reduces surface expression of Slo in hair cells. American Journal Of Physiology - Cell Physiology 2010, 300: c435-c446. PMID: 21178105, PMCID: PMC3063969, DOI: 10.1152/ajpcell.00449.2010.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium SignalingCell MembraneChickensCochleaDown-RegulationHair Cells, AuditoryIon Channel GatingLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsMechanotransduction, CellularMembrane PotentialsOocytesXenopus laevisConceptsLow-frequency hair cellsHair cellsLarge-conductance potassium channelsBK channelsSurface expressionBK channel functionNonmammalian vertebratesAccessory subunitsΑ-subunitMolecular underpinningsΒ-subunitChannel functionSubunitsΒ4 subunitPhysiological Ca2Critical rolePotassium channelsCellsBK currentsAdditional mechanismExpressionVertebratesDramatic increaseChicksIntracellularCombinatorial Cysteine Mutagenesis Reveals a Critical Intramonomer Role for Cysteines in Prestin Voltage Sensing
Bai JP, Surguchev A, Bian S, Song L, Santos-Sacchi J, Navaratnam D. Combinatorial Cysteine Mutagenesis Reveals a Critical Intramonomer Role for Cysteines in Prestin Voltage Sensing. Biophysical Journal 2010, 99: 85-94. PMID: 20655836, PMCID: PMC2895379, DOI: 10.1016/j.bpj.2010.03.066.Peer-Reviewed Original ResearchConceptsDisulfide bond formationCysteine residuesCysteine residue pairsSingle cysteine residueCysteine mutagenesisTransmembrane proteinSubstitution mutantsSLC26 familyResidue pairsFörster resonance energy transferCharge movementVoltage-dependent charge movementDisulfide interactionsResonance energy transferPrestinProteinMutantsDimer formationResiduesCysteineHair cellsSurface expressionAnion transportersCochlear amplificationWestern blot
2009
Prestin's Anion Transport and Voltage-Sensing Capabilities Are Independent
Bai JP, Surguchev A, Montoya S, Aronson PS, Santos-Sacchi J, Navaratnam D. Prestin's Anion Transport and Voltage-Sensing Capabilities Are Independent. Biophysical Journal 2009, 96: 3179-3186. PMID: 19383462, PMCID: PMC2718310, DOI: 10.1016/j.bpj.2008.12.3948.Peer-Reviewed Original ResearchMeSH Keywords4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAnalysis of VarianceAnimalsAnion Transport ProteinsAntiportersCarbon RadioisotopesChloridesCHO CellsCricetinaeCricetulusElectric CapacitanceFormatesGerbillinaeIon TransportMiceMutation, MissenseOxalatesPatch-Clamp TechniquesSalicylatesSulfate TransportersConceptsClosest phylogenetic relativesTransmembrane regionSLC26 anion transporter familyMammalian outer hair cellsMembrane protein prestinPrestin's motor functionAnion transportPhylogenetic relativesAnion transporter familyTransporter familyProtein prestinChloride-binding siteGating charge movementPrestinCharge movementHair cellsOuter hair cellsResiduesMechanistic conceptsVoltage sensingTransport capabilityCellsVoltage sensorPrevious observationsUptake studies
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