2020
Maturation of Voltage-induced Shifts in SLC26a5 (Prestin) Operating Point during Trafficking and Membrane Insertion
Zhai F, Song L, Bai JP, Dai C, Navaratnam D, Santos-Sacchi J. Maturation of Voltage-induced Shifts in SLC26a5 (Prestin) Operating Point during Trafficking and Membrane Insertion. Neuroscience 2020, 431: 128-133. PMID: 32061780, PMCID: PMC8720582, DOI: 10.1016/j.neuroscience.2020.02.003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnion Transport ProteinsCell MembraneElectric CapacitanceHair Cells, Auditory, OuterMembrane PotentialsPatch-Clamp TechniquesProteinsConceptsMembrane motor proteinVoltage-dependent proteinsMembrane insertionOuter hair cellsMotor proteinsPrestin densityHEK cell linesConformational changesBiophysical forcesOHC electromotilityProteinCell linesMembrane potentialCooperative interactionsPrestinHair cellsCochlear amplificationTransmembrane voltageNonlinear capacitanceMammalsTraffickingVoltage-induced shiftElectromotilityMaturationMembrane
2014
Chloride and Salicylate Influence Prestin-dependent Specific Membrane Capacitance SUPPORT FOR THE AREA MOTOR MODEL* * This work was supported, in whole or in part, by National Institutes of Health Grant NIDCD DC00273 (to J. S. S.).
Santos-Sacchi J, Song L. Chloride and Salicylate Influence Prestin-dependent Specific Membrane Capacitance SUPPORT FOR THE AREA MOTOR MODEL* * This work was supported, in whole or in part, by National Institutes of Health Grant NIDCD DC00273 (to J. S. S.). Journal Of Biological Chemistry 2014, 289: 10823-10830. PMID: 24554714, PMCID: PMC4036195, DOI: 10.1074/jbc.m114.549329.Peer-Reviewed Original Research
2010
Combinatorial 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 blotPrestin 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