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 Research
2013
Real 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
2012
Expression, Purification and Functional Reconstitution of Slack Sodium-Activated Potassium Channels
Yan Y, Yang Y, Bian S, Sigworth FJ. Expression, Purification and Functional Reconstitution of Slack Sodium-Activated Potassium Channels. The Journal Of Membrane Biology 2012, 245: 667-674. PMID: 22729647, PMCID: PMC3903048, DOI: 10.1007/s00232-012-9425-7.Peer-Reviewed Original ResearchConceptsPotassium channel activityΑ-subunitPotassium channel α-subunitChannel activityGene codesFunctional reconstitutionMembrane vesiclesChannel familyCell typesPlanar bilayer membranesPotassium channelsBilayer membranesExpressionReconstitutionPurificationProteinVesiclesMembraneActivityFamilySodium ionsChloride Flux in Prestin-Expressing Cells
Zhong S, Bian S, Navaratnam D, Santos-Sacchi J. Chloride Flux in Prestin-Expressing Cells. Biophysical Journal 2012, 102: 246a. DOI: 10.1016/j.bpj.2011.11.1355.Peer-Reviewed Original Research
2011
Interactions between β-Catenin and the HSlo Potassium Channel Regulates HSlo Surface Expression
Bian S, Bai JP, Chapin H, Le Moellic C, Dong H, Caplan M, Sigworth FJ, Navaratnam DS. Interactions between β-Catenin and the HSlo Potassium Channel Regulates HSlo Surface Expression. PLOS ONE 2011, 6: e28264. PMID: 22194818, PMCID: PMC3237428, DOI: 10.1371/journal.pone.0028264.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBeta CateninBinding SitesBiological AssayCell MembraneChickensGene Knockdown TechniquesHair Cells, AuditoryHEK293 CellsHumansImmunoprecipitationIntercellular JunctionsKineticsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsModels, MolecularMolecular Sequence DataMutant ProteinsMutationPhosphorylationProtein BindingProtein TransportRNA, Small InterferingSequence DeletionTransfectionWnt Signaling PathwayConceptsΒ-cateninS10 regionHEK cellsSurface expressionCell biology toolsPotassium channel alpha subunitΒ-catenin interactionDownregulation of WntCytoskeleton frameworkChannel alpha subunitChicken hair cellsPhosphorylation sitesDeletion mutantsBiology toolsΒ-catenin-dependent canonical WntAlpha subunitCanonical WntMultiple binding sitesNumber of diseasesStable bindingWntPhysiological significanceBinding sitesReduced expressionHair cellsEvaluating Prestin's Changing Biophysical Attributes in Development Using a Tet‐Induced Cell Line
Bian S, Koo B, Kelleher S, Santos-Sacchi J, Navaratnam D, Shera C, Olson E. Evaluating Prestin's Changing Biophysical Attributes in Development Using a Tet‐Induced Cell Line. AIP Conference Proceedings 2011, 1403: 143-147. DOI: 10.1063/1.3658075.Peer-Reviewed Original ResearchExtracellular chloride regulation of Kv2.1, contributor to the major outward Kv current in mammalian outer hair cells
Li X, Surguchev A, Bian S, Navaratnam D, Santos-Sacchi J. Extracellular chloride regulation of Kv2.1, contributor to the major outward Kv current in mammalian outer hair cells. American Journal Of Physiology - Cell Physiology 2011, 302: c296-c306. PMID: 21940671, PMCID: PMC4054960, DOI: 10.1152/ajpcell.00177.2011.Peer-Reviewed Original Research
2010
A highly expressing Tet-inducible cell line recapitulates in situ developmental changes in prestin's Boltzmann characteristics and reveals early maturational events
Bian S, Koo BW, Kelleher S, Santos-Sacchi J, Navaratnam DS. A highly expressing Tet-inducible cell line recapitulates in situ developmental changes in prestin's Boltzmann characteristics and reveals early maturational events. American Journal Of Physiology - Cell Physiology 2010, 299: c828-c835. PMID: 20631244, PMCID: PMC3774197, DOI: 10.1152/ajpcell.00182.2010.Peer-Reviewed Original ResearchCombinatorial 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
2006
Synthesis of a Biotin Derivative of Iberiotoxin: Binding Interactions with Streptavidin and the BK Ca2+-Activated K+ Channel Expressed in a Human Cell Line
Bingham J, Bian S, Tan Z, Takacs Z, Moczydlowski E. Synthesis of a Biotin Derivative of Iberiotoxin: Binding Interactions with Streptavidin and the BK Ca2+-Activated K+ Channel Expressed in a Human Cell Line. Bioconjugate Chemistry 2006, 17: 689-699. PMID: 16704206, PMCID: PMC2505059, DOI: 10.1021/bc060002u.Peer-Reviewed Original ResearchThe calcium-sensitive large-conductance potassium channel (BK/MAXI K) is present in the inner mitochondrial membrane of rat brain
Douglas R, Lai J, Bian S, Cummins L, Moczydlowski E, Haddad G. The calcium-sensitive large-conductance potassium channel (BK/MAXI K) is present in the inner mitochondrial membrane of rat brain. Neuroscience 2006, 139: 1249-1261. PMID: 16567053, DOI: 10.1016/j.neuroscience.2006.01.061.Peer-Reviewed Original ResearchConceptsLarge conductance voltageInner mitochondrial membraneCalcium-sensitive channelsCytochrome c oxidaseMitochondrial membraneInner mitochondrial membrane proteinC oxidaseMitochondrial fractionInner membrane 23Mitochondrial-specific proteinsMitochondrial membrane proteinMicrotubule-associated protein 1Endoplasmic reticulum markerImmuno-gold electron microscopyLarge-conductance potassium channelsDiscrete subcellular fractionsGold particle labellingWestern blottingGolgi proteinsMembrane proteinsSubcellular localizationAlpha subunitProtein 1Mitochondrial pelletMitochondria
2001
Ca2+-binding activity of a COOH-terminal fragment of the Drosophila BK channel involved in Ca2+-dependent activation
Bian S, Favre I, Moczydlowski E. Ca2+-binding activity of a COOH-terminal fragment of the Drosophila BK channel involved in Ca2+-dependent activation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 4776-4781. PMID: 11274367, PMCID: PMC31910, DOI: 10.1073/pnas.081072398.Peer-Reviewed Original ResearchConceptsIntracellular COOH-terminal domainDependent activationBK channelsCOOH-terminal domainProtein blot assayBiochemical approachesStructural basisBiophysical analysisBK proteinAsp residuesControl proteinHEK293 cellsEscherichia coliProteinElectrophysiological assaysBlot assaysLarge conductanceTerminal fragmentSoluble formActivationResiduesFunctional correlationSpecific bindingSpecific regionsBinding