ArticleThe Journal of physiology2012
Anion transport by the cochlear motor protein prestin.
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, 35 citations in OpenAlex.
- SLC26A11 is an atypical solute carrier with dual transport-channel function mediating lysosomal sulfate transport.Nature communications · 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
- Sonogenetics for precision medicine: from molecular toolkit to clinical translation.Theranostics · 2026Review
- SLC26 Anion Transporters.Handbook of experimental pharmacology · 2024Review
- Vesicular glutamate transporters are HNature communications · 2023Article
- Single particle cryo-EM structure of the outer hair cell motor protein prestin.Nature communications · 2022Article
- Functional Characterization ofFrontiers in molecular neuroscience · 2022Article
- SLC26A7 constitutes the thiocyanate-selective anion conductance of the basolateral membrane of the retinal pigment epithelium.American journal of physiology. Cell physiology · 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
- Mouse retinal pigment epithelial cells exhibit a thiocyanate-selective conductance.American journal of physiology. Cell physiology · 2018Article
- Current carried by the Slc26 family member prestin does not flow through the transporter pathway.Scientific reports · 2017Article
- Reduced Membrane Insertion of CLC-K by V33L Barttin Results in Loss of Hearing, but Leaves Kidney Function Intact.Frontiers in physiology · 2017Article
- 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 properties, functions, and pathophysiology of maxi-anion channels.Pflugers Archiv : European journal of physiology · 2016Review
- Impaired surface membrane insertion of homo- and heterodimeric human muscle chloride channels carrying amino-terminal myotonia-causing mutations.Scientific reports · 2015Article
- Chloride-driven electromechanical phase lags at acoustic frequencies are generated by SLC26a5, the outer hair cell motor protein.Biophysical journal · 2014Article
- Prestin at year 14: progress and prospect.Hearing research · 2014Review
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prestin is a member of the SLC26 solute carrier family and functions as a motor protein in cochlear outer hair cells. While other SLC26 homologues were demonstrated to transport a wide variety of anions, no electrogenic transport activity has been assigned so far to mammalian prestin. We here use heterologous expression in mammalian cells, patch clamp recordings and measurements of expression levels of individual cells to study anion transport by rat prestin. We demonstrated that cells expressing rat prestin exhibit SCN(-) currents that are proportional to the number of prestin molecules. Variation of the SCN(-) concentration resulted in changes of the current reversal potential that obey the Nernst equation indicating that SCN(-) transport is not stoichiometrically coupled to other anions. Application of external SCN(-) causes large increases of anion currents, but only minor changes in non-linear charge movements suggesting that only a very small percentage of prestin molecules function as SCN(-) transporters under these conditions. Unitary current amplitudes are below the resolution limit of noise analysis and thus much smaller than expected for pore-mediated anion transport. A comparison with a non-mammalian prestin from D. rerio - recently shown to function as Cl(-)/SO(4)(2-) antiporter - and an SLC26 anion channel, human SLC26A7, revealed that SCN(-) transport is conserved in these distinct members of the SLC26 family. We conclude that mammalian prestin is capable of mediating electrogenic anion transport and suggest that SLC26 proteins converting membrane voltage oscillations into conformational changes and those functioning as channels or transporters share certain transport capabilities.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.