ArticleBiophysical journal2011
Membrane thickness sensitivity of prestin orthologs: the evolution of a piezoelectric protein.
Article in Biophysical journal, 2011. 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, 16 citations in OpenAlex.
- 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
- Piezoelectric Biomaterials for Osteochondral Tissue Engineering: Advances, Mechanisms, and Translational Prospects.Journal of functional biomaterials · 2026Review
- Structural Mechanism of Prestin-Membrane Mechanotransduction.bioRxiv : the preprint server for biology · 2025Article
- Design and Manufacturing of Piezoelectric Biomaterials for Bioelectronics and Biomedical Applications.Chemical reviews · 2025Review
- Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility.Nature communications · 2022Article
- Article
- Outer hair cell electromotility is low-pass filtered relative to the molecular conformational changes that produce nonlinear capacitance.The Journal of general physiology · 2019Article
- Review
- Mechanical transduction by ion channels: A cautionary tale.World journal of neurology · 2015Article
- The V499G/Y501H mutation impairs fast motor kinetics of prestin and has significance for defining functional independence of individual prestin subunits.The Journal of biological chemistry · 2013Article
- The capacitance and electromechanical coupling of lipid membranes close to transitions: the effect of electrostriction.Biophysical journal · 2012Article
- A motif of eleven amino acids is a structural adaptation that facilitates motor capability of eutherian prestin.Journal of cell science · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
How proteins evolve new functionality is an important question in biology; prestin (SLC26A5) is a case in point. Prestin drives outer hair cell somatic motility and amplifies mechanical vibrations in the mammalian cochlea. The motility of mammalian prestin is analogous to piezoelectricity, in which charge transfer is coupled to changes in membrane area occupied by the protein. Intriguingly, nonmammalian prestin orthologs function as anion exchangers but are apparently nonmotile. We previously found that mammalian prestin is sensitive to membrane thickness, suggesting that prestin's extended conformation has a thinner hydrophobic height in the lipid bilayer. Because prestin-based motility is a mammalian specialization, we initially hypothesized that nonmotile prestin orthologs, while functioning as anion transporters, should be much less sensitive to membrane thickness. We found the exact opposite to be true. Chicken prestin was the most sensitive to thickness changes, displaying the largest shift in voltage dependence. Platypus prestin displayed an intermediate response to membrane thickness and gerbil prestin was the least sensitive. To explain these observations, we present a theory where force production, rather than displacement, was selected for the evolution of prestin as a piezoelectric membrane motor.
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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.