ArticleCell2021
Molecular mechanism of prestin electromotive signal amplification.
Article in Cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
60 citing papers in PubMed, 102 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Prestin as a potential biomarker for cochlear injury: Current evidence and future directions.European archives of oto-rhino-laryngology : official journal of the European Federation of Oto-Rhino-Laryngological Societies (EUFOS) : affiliated with the German Society for Oto-Rhino-Laryngology - Head and Neck Surgery · 2026Review
- SLC26A11 is an atypical solute carrier with dual transport-channel function mediating lysosomal sulfate transport.Nature communications · 2026Article
- Structural and dynamic insights into SPDT for phosphorus allocation in rice.Science China. Life sciences · 2026Article
- Stable mammalian expression of His-tagged prestin in Chinese hamster ovary cells.Cytotechnology · 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
- Enhancing prestin oligomerization for superior sonogenetics.Theranostics · 2026Article
- Structural Mechanism of Prestin-Membrane Mechanotransduction.bioRxiv : the preprint server for biology · 2025Article
- LRRC8A Regulates Outer Hair Cell Volume and Electromotility and is Required for Hearing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Molecular mechanism underlying phosphate distribution by SULTR family transporter SPDT inScience advances · 2025Article
- Allosteric coupling between a lipid bilayer and a membrane protein.Biophysical journal · 2025Article
- Structural basis for substrate recognition mechanism of human SLC26A7.Nature communications · 2025Article
- Chloride binding does not influence prestin motor speed at very high frequencies in the mouse outer hair cell.Structure (London, England : 1993) · 2025Article
- Hearing Loss and Audiogenic Seizures Induced by Hypofunctional Prestin Variants.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Protein Structures of Urea Transporters.Sub-cellular biochemistry · 2025Review
- CRISPR/Cas9-mediated exon skipping to restore premature translation termination in a DFNB4 mouse model.Gene therapy · 2024Article
- MYH1 deficiency disrupts outer hair cell electromotility, resulting in hearing loss.Experimental & molecular medicine · 2024Article
- Recent advancement of sonogenetics: A promising noninvasive cellular manipulation by ultrasound.Genes & diseases · 2024Review
- Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA.Nature communications · 2024Article
- Activation mechanisms of dimeric mechanosensitive OSCA/TMEM63 channels.Nature communications · 2024Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Hearing involves two fundamental processes: mechano-electrical transduction and signal amplification. Despite decades of studies, the molecular bases for both remain elusive. Here, we show how prestin, the electromotive molecule of outer hair cells (OHCs) that senses both voltage and membrane tension, mediates signal amplification by coupling conformational changes to alterations in membrane surface area. Cryoelectron microscopy (cryo-EM) structures of human prestin bound with chloride or salicylate at a common "anion site" adopt contracted or expanded states, respectively. Prestin is ensconced within a perimeter of well-ordered lipids, through which it induces dramatic deformation in the membrane and couples protein conformational changes to the bulk membrane. Together with computational studies, we illustrate how the anion site is allosterically coupled to changes in the transmembrane domain cross-sectional area and the surrounding membrane. These studies provide insight into OHC electromotility by providing a structure-based mechanism of the membrane motor prestin.
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Registered trials
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.