ArticleThe Journal of biological chemistry2013
The V499G/Y501H mutation impairs fast motor kinetics of prestin and has significance for defining functional independence of individual prestin subunits.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Structural Mechanism of Prestin-Membrane Mechanotransduction.bioRxiv : the preprint server for biology · 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
- The pathogenic roles of the p.R130S prestin variant in DFNB61 hearing loss.The Journal of physiology · 2024Article
- 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
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- State dependent effects on the frequency response of prestin's real and imaginary components of nonlinear capacitance.Scientific reports · 2021Article
- Prestin amplifies cardiac motor functions.Cell reports · 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
- Complex nonlinear capacitance in outer hair cell macro-patches: effects of membrane tension.Scientific reports · 2020Article
- Systematic quantification of the anion transport function of pendrin (SLC26A4) and its disease-associated variants.Human mutation · 2020Article
- Outer hair cell electromotility is low-pass filtered relative to the molecular conformational changes that produce nonlinear capacitance.The Journal of general physiology · 2019Article
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- Deletion of exons 17 and 18 in prestin's STAS domain results in loss of function.Scientific reports · 2019Article
- The susceptibility of cochlear outer hair cells to cyclodextrin is not related to their electromotile activity.Acta neuropathologica communications · 2018Article
- The extracellular loop of pendrin and prestin modulates their voltage-sensing property.The Journal of biological chemistry · 2018Article
- Prestin Contributes to Membrane Compartmentalization and Is Required for Normal Innervation of Outer Hair Cells.Frontiers in cellular neuroscience · 2018Article
- The R130S mutation significantly affects the function of prestin, the outer hair cell motor protein.Journal of molecular medicine (Berlin, Germany) · 2016Article
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Authors and funding
5 authors.
Funding
Abstract
Outer hair cells (OHCs) are a mammalian innovation for mechanically amplifying sound energy to overcome the viscous damping of the cochlear partition. Although the voltage-dependent OHC membrane motor, prestin, has been demonstrated to be essential for mammalian cochlear amplification, the molecular mechanism by which prestin converts electrical energy into mechanical displacement/force remains elusive. Identifying mutations that alter the motor function of prestin provides vital information for unraveling the energy transduction mechanism of prestin. We show that the V499G/Y501H mutation does not deprive prestin of its voltage-induced motor activity, but it does significantly impair the fast motor kinetics and voltage operating range. Furthermore, mutagenesis studies suggest that Val-499 is the primary site responsible for these changes. We also show that V499G/Y501H prestin forms heteromers with wild-type prestin and that the fast motor kinetics of wild-type prestin is not affected by heteromer formation with V499G/Y501H prestin. These results suggest that prestin subunits are individually functional within a given multimer.
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