About
Titles
Safety Advisor – Team Lead
Biography
Dr. Shumin Bian was trained in biochemistry and biophysics at Ohio
State University before joining Professor Edward Moczydlowski’s lab in
the Pharmacology Department at Yale School of Medicine to study the
mechanisms of calcium activation of BK channels. Now he is a member of
Fred Sigworth’s lab working on the biochemistry of ion channels,
particularly using cryoEM for structure-functional study. He is also
interested in channel-associated proteins and the involvement of ion
channels in signal transduction.
Research
Research at a Glance
Yale Co-Authors
Frequent collaborators of Shumin Bian's published research.
Publications Timeline
A big-picture view of Shumin Bian's research output by year.
Joseph Santos-Sacchi, PhD
Dhasakumar Navaratnam, MD, PhD
Jun-Ping Bai, PhD
Lei Song, MD, PhD
Fangyong Li, MS, MPH
Michael Caplan, PhD, MD
13Publications
310Citations
Publications
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 ResearchCitationsMeSH Keywords and Concepts
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 ResearchCitationsMeSH Keywords and ConceptsConceptsObligate 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 ResearchCitationsMeSH Keywords and ConceptsConceptsPotassium 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 ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH 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 ResearchCitationsExtracellular 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 ResearchCitations
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 ResearchCitationsCombinatorial 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 ResearchCitationsMeSH Keywords and ConceptsConceptsDisulfide 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 ResearchCitations
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