ArticleBiophysical journal2010
Conformational state-dependent anion binding in prestin: evidence for allosteric modulation.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Conformational changes underlying electromechanical transduction in prestin resemble a transport transition in pendrin.bioRxiv : the preprint server for biology · 2026Article
- Chloride binding does not influence prestin motor speed at very high frequencies in the mouse outer hair cell.Structure (London, England : 1993) · 2025Article
- Folding of prestin's anion-binding site and the mechanism of outer hair cell electromotility.eLife · 2023Article
- On the frequency response of prestin charge movement in membrane patches.Biophysical journal · 2022Article
- Single particle cryo-EM structure of the outer hair cell motor protein prestin.Nature communications · 2022Article
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- State dependent effects on the frequency response of prestin's real and imaginary components of nonlinear capacitance.Scientific reports · 2021Article
- Comparative Molecular Dynamics Investigation of the Electromotile Hearing Protein Prestin.International journal of molecular sciences · 2021Article
- Prestin amplifies cardiac motor functions.Cell reports · 2021Article
- Complex nonlinear capacitance in outer hair cell macro-patches: effects of membrane tension.Scientific reports · 2020Article
- Maturation of Voltage-induced Shifts in SLC26a5 (Prestin) Operating Point during Trafficking and Membrane Insertion.Neuroscience · 2020Article
- Voltage Does Not Drive Prestin (SLC26a5) Electro-Mechanical Activity at High Frequencies Where Cochlear Amplification Is Best.iScience · 2019Article
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- Chansporter complexes in cell signaling.FEBS letters · 2017Review
- Current carried by the Slc26 family member prestin does not flow through the transporter pathway.Scientific reports · 2017Article
- Diflunisal inhibits prestin by chloride-dependent mechanism.PloS one · 2017Article
- Membrane prestin expression correlates with the magnitude of prestin-associated charge movement.Hearing research · 2016Article
- Chloride Anions Regulate Kinetics but Not Voltage-Sensor Qmax of the Solute Carrier SLC26a5.Biophysical journal · 2016Article
- Analysis of the Damage Mechanism Related to CONeural plasticity · 2016Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Outer hair cells boost auditory performance in mammals. This amplification relies on an expansive array of intramembranous molecular motors, identified as prestin, that drive somatic electromotility. By measuring nonlinear capacitance, the electrical signature of electromotility, we are able to assess prestin's conformational state and interrogate the effectiveness of anions on prestin's activity. We find that the affinity of anions depends on the state of prestin that we set with a variety of perturbations (in membrane tension, temperature, and voltage), and that movement into the expanded state reduces the affinity of prestin for anions. These data signify that anions work allosterically on prestin. Consequently, anions are released from prestin's binding site during expansion, i.e., during hyperpolarization. This is at odds with the extrinsic voltage sensor model, which suggests that prestin-bound intracellular anions are propelled deep into the membrane. Furthermore, we hypothesize that prestin's susceptibility to many biophysical forces, and notably its piezoelectric nature, may reflect anion interactions with the motor.
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Registered trials
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