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
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 cellsExtracellular 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
The 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