2022
Single particle cryo-EM structure of the outer hair cell motor protein prestin
Butan C, Song Q, Bai JP, Tan WJT, Navaratnam D, Santos-Sacchi J. Single particle cryo-EM structure of the outer hair cell motor protein prestin. Nature Communications 2022, 13: 290. PMID: 35022426, PMCID: PMC8755724, DOI: 10.1038/s41467-021-27915-z.Peer-Reviewed Original ResearchConceptsTransmembrane domainProtein prestinSingle-particle cryo-EM structuresAnti-sigma factor antagonist domainOuter hair cell motor protein prestinCryo-EM structureCryo-electron microscopyMotor protein prestinSLC26 family membersSulfate transportersTransmembrane segmentsPrestin functionÅ resolutionPrestinOHC electromotilityOpen stateCochlear amplificationPutative mechanismsFamily membersDomainRepeatsSLC26A9TransportersMutationsElectromotility
2017
Current carried by the Slc26 family member prestin does not flow through the transporter pathway
Bai JP, Moeini-Naghani I, Zhong S, Li FY, Bian S, Sigworth FJ, Santos-Sacchi J, Navaratnam D. Current carried by the Slc26 family member prestin does not flow through the transporter pathway. Scientific Reports 2017, 7: 46619. PMID: 28422190, PMCID: PMC5395958, DOI: 10.1038/srep46619.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCHO CellsCricetulusHEK293 CellsHumansIon Channel GatingIon TransportMutationProtein Structure, SecondarySulfate Transporters
2013
IR Laser-Induced Perturbations of the Voltage-Dependent Solute Carrier Protein SLC26a5
Okunade O, Santos-Sacchi J. IR Laser-Induced Perturbations of the Voltage-Dependent Solute Carrier Protein SLC26a5. Biophysical Journal 2013, 105: 1822-1828. PMID: 24138858, PMCID: PMC3797594, DOI: 10.1016/j.bpj.2013.09.008.Peer-Reviewed Original ResearchReal Time Measures of Prestin Charge and Fluorescence during Plasma Membrane Trafficking Reveal Sub-Tetrameric Activity
Bian S, Navaratnam D, Santos-Sacchi J. Real Time Measures of Prestin Charge and Fluorescence during Plasma Membrane Trafficking Reveal Sub-Tetrameric Activity. PLOS ONE 2013, 8: e66078. PMID: 23762468, PMCID: PMC3677934, DOI: 10.1371/journal.pone.0066078.Peer-Reviewed Original ResearchConceptsObligate tetramerPlasma membraneMembrane motor proteinIntegral membrane proteinsTetracycline-inducible cell lineMembrane proteinsMotor proteinsPrestin densityTemperature blockPrestinFluorescence measuresMembrane fluorescenceCell linesNonlinear capacitanceCochlear amplificationProteinTetramerMembraneFluorescencePrevious observationsVoltage clampFluorescence methodCellsAmplification
2010
Prestin Surface Expression and Activity Are Augmented by Interaction with MAP1S, a Microtubule-associated Protein*
Bai JP, Surguchev A, Ogando Y, Song L, Bian S, Santos-Sacchi J, Navaratnam D. Prestin Surface Expression and Activity Are Augmented by Interaction with MAP1S, a Microtubule-associated Protein*. Journal Of Biological Chemistry 2010, 285: 20834-20843. PMID: 20418376, PMCID: PMC2898336, DOI: 10.1074/jbc.m110.117853.Peer-Reviewed Original Research
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
2003
New tunes from Corti’s organ: the outer hair cell boogie rules
Santos-Sacchi J. New tunes from Corti’s organ: the outer hair cell boogie rules. Current Opinion In Neurobiology 2003, 13: 459-468. PMID: 12965294, DOI: 10.1016/s0959-4388(03)00100-4.Peer-Reviewed Original ResearchMeSH KeywordsAcoustic StimulationAnimalsAnion Transport ProteinsHair Cells, Auditory, OuterHumansMembrane PotentialsOrgan of CortiProteinsSulfate TransportersConceptsSpecial cell typesHair cellsOuter hair cell electromotilityHair cell electromotilityMolecular identificationCell typesMammalsMechanism of actionOuter hair cellsAdditional mechanismVertebratesCellsAmplificationMechanismKnockoutElectromotilityOrgansSuch amplificationCorti's organAcoustic stimuliRemarkable progress
2001
Temperature dependence of non-linear capacitance in human embryonic kidney cells transfected with prestin, the outer hair cell motor protein
Meltzer J, Santos-Sacchi J. Temperature dependence of non-linear capacitance in human embryonic kidney cells transfected with prestin, the outer hair cell motor protein. Neuroscience Letters 2001, 313: 141-144. PMID: 11682147, DOI: 10.1016/s0304-3940(01)02266-2.Peer-Reviewed Original ResearchEffects of membrane potential and tension on prestin, the outer hair cell lateral membrane motor protein
Santos‐Sacchi J, Shen W, Zheng J, Dallos P. Effects of membrane potential and tension on prestin, the outer hair cell lateral membrane motor protein. The Journal Of Physiology 2001, 531: 661-666. PMID: 11251048, PMCID: PMC2278494, DOI: 10.1111/j.1469-7793.2001.0661h.x.Peer-Reviewed Original ResearchConceptsMembrane tensionMembrane motor proteinMembrane-bound proteinsHuman embryonic kidney cellsLateral plasma membraneEmbryonic kidney cellsMolecular basisPlasma membraneProtein prestinMotor proteinsConformational changesHigh-resolution analysisPrestin activityPrestinKidney cellsMembrane potential