ArticleThe Journal of biological chemistry2018
The extracellular loop of pendrin and prestin modulates their voltage-sensing property.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Identification of a novel isoform of Slc26a4 by single-cell RNA-sequencing of pendrin-expressing cells in the cochlea.Human genetics · 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
- Hearing Loss and Audiogenic Seizures Induced by Hypofunctional Prestin Variants.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Genetic heterogeneity in patients with enlarged vestibular aqueduct and Pendred syndrome.Molecular medicine (Cambridge, Mass.) · 2025Article
- Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility.Nature communications · 2022Article
- Single particle cryo-EM structure of the outer hair cell motor protein prestin.Nature communications · 2022Article
- Identification and characterization of amphibian SLC26A5 using RNA-Seq.BMC genomics · 2021Article
- Three-Dimensional Otic Neuronal Progenitor Spheroids Derived from Human Embryonic Stem Cells.Tissue engineering. Part A · 2021Article
- 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
- An In Vitro Study on Prestin Analog Gene in the Bullfrog Hearing Organs.Neural plasticity · 2020Article
- Systematic quantification of the anion transport function of pendrin (SLC26A4) and its disease-associated variants.Human mutation · 2020Article
- Deletion of exons 17 and 18 in prestin's STAS domain results in loss of function.Scientific reports · 2019Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Pendrin and prestin belong to the solute carrier 26 (SLC26) family of anion transporters. Prestin is unique among the SLC26 family members in that it displays voltage-driven motor activity (electromotility) and concurrent gating currents that manifest as nonlinear cell membrane electrical capacitance (nonlinear capacitance (NLC)). Although the anion transport mechanism of the SLC26 proteins has begun to be elucidated, the molecular mechanism of electromotility, which is thought to have evolved from an ancestral ion transport mechanism, still remains largely elusive. Here, we demonstrate that pendrin also exhibits large NLC and that charged residues present in one of the extracellular loops of pendrin and prestin play significant roles in setting the voltage-operating points of NLC. Our results suggest that the molecular mechanism responsible for sensing voltage is not unique to prestin among the members of the SLC26 family and that this voltage-sensing mechanism works independently of the anion transport mechanism.
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