ArticleThe Journal of physiology2012
Mammalian prestin is a weak Cl⁻/HCO₃⁻ electrogenic antiporter.
Article in The Journal of physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 32 citations in OpenAlex.
- Conformational changes underlying electromechanical transduction in prestin resemble a transport transition in pendrin.bioRxiv : the preprint server for biology · 2026Article
- From transporter to motor: Evolutionary and structural insights into the emergence of prestin's area-motor activity in mammals.Protein science : a publication of the Protein Society · 2026Article
- SLC26 Anion Transporters.Handbook of experimental pharmacology · 2024Review
- The Remarkable Outer Hair Cell: Proceedings of a Symposium in Honour of W. E. Brownell.Journal of the Association for Research in Otolaryngology : JARO · 2023Review
- Prestin's fast motor kinetics is essential for mammalian cochlear amplification.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility.Nature communications · 2022Article
- The Roles of Solute Carriers in Auditory Function.Frontiers in genetics · 2022Review
- Listening in to the Cell.Bioelectricity · 2020Article
- A novel theoretical framework reveals more than one voltage-sensing pathway in the lateral membrane of outer hair cells.The Journal of general physiology · 2020Article
- Outer Hair Cells and Electromotility.Cold Spring Harbor perspectives in medicine · 2019Review
- Importance of SLC26 Transmembrane Anion Exchangers in Sperm Post-testicular Maturation and Fertilization Potential.Frontiers in cell and developmental biology · 2019Review
- The extracellular loop of pendrin and prestin modulates their voltage-sensing property.The Journal of biological chemistry · 2018Article
- Current carried by the Slc26 family member prestin does not flow through the transporter pathway.Scientific reports · 2017Article
- Accelerating the search for the missing proteins in the human proteome.Nature communications · 2017Review
- The R130S mutation significantly affects the function of prestin, the outer hair cell motor protein.Journal of molecular medicine (Berlin, Germany) · 2016Article
- Chloride Anions Regulate Kinetics but Not Voltage-Sensor Qmax of the Solute Carrier SLC26a5.Biophysical journal · 2016Article
- The chloride-channel blocker 9-anthracenecarboxylic acid reduces the nonlinear capacitance of prestin-associated charge movement.The European journal of neuroscience · 2016Article
- An electrical inspection of the subsurface cisternae of the outer hair cell.Biophysical journal · 2015Article
- A model of ionic transport and osmotic volume control in cochlear outer hair cells.Interface focus · 2014Article
- Chloride-driven electromechanical phase lags at acoustic frequencies are generated by SLC26a5, the outer hair cell motor protein.Biophysical journal · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The lateral membrane of mammalian cochlear outer hair cells contains prestin, a protein which can act as a fast voltage-driven actuator responsible for electromotility and enhanced sensitivity to sound. The protein belongs to the SLC26 family of transporters whose members are characterised as able to exchange halides for SO(4)(2-) or HCO(3)(-) yet previous analyses of mammalian prestin have suggested that such exchange functions were minimal. Here anion transport is investigated both in guinea-pig outer hair cells (OHCs) and in an expression system where we employ a sensitive intracellular pH (pH(i)) probe, pHluorin, to report HCO(3)(-) transport and to monitor the small pH(i) changes observable in the cells. In the presence of extracellular HCO(3)(-), pH(i) recovered from an acid load 4 times faster in prestin-transfected cells. The acceleration required a chloride gradient established by reducing extracellular chloride to 2 mm. Similar results were also shown using BCECF as an alternative pH(i) sensor, but with recovery only found in those cells expressing prestin. Simultaneous electrophysiological recording of the transfected cells during bicarbonate exposure produced a shift in the reversal potential to more negative potentials, consistent with electrogenic transport. These data therefore suggest that prestin can act as a weak Cl(-)/HCO(3)(-) antiporter and it is proposed that, in addition to participating in wide band cochlear sound amplification, prestin may also be involved in the slow time scale (>10 s) phenomena where changes in cell stiffness and internal pressure have been implicated. The results show the importance of considering the effects of the endogenous bicarbonate buffering system in evaluating the function of prestin in cochlear outer hair cells.
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