ArticleThe Journal of biological chemistry2011
Engineered pendrin protein, an anion transporter and molecular motor.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 22 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
- Single particle cryo-EM structure of the outer hair cell motor protein prestin.Nature communications · 2022Article
- Low-Intensity Ultrasound Causes Direct Excitation of Auditory Cortical Neurons.Neural plasticity · 2021Article
- The extracellular loop of pendrin and prestin modulates their voltage-sensing property.The Journal of biological chemistry · 2018Article
- Auditory Brainstem Response and Outer Hair Cell Whole-cell Patch Clamp Recording in Postnatal Rats.Journal of visualized experiments : JoVE · 2018Article
- The Effects of Urethane on Rat Outer Hair Cells.Neural plasticity · 2016Article
- Synchronized Progression of Prestin Expression and Auditory Brainstem Response during Postnatal Development in Rats.Neural plasticity · 2016Article
- Glutamate transporter homolog-based model predicts that anion-π interaction is the mechanism for the voltage-dependent response of prestin.The Journal of biological chemistry · 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
- The conserved tetrameric subunit stoichiometry of Slc26 proteins.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2013Article
- Disparities in voltage-sensor charge and electromotility imply slow chloride-driven state transitions in the solute carrier SLC26a5.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- 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
- Article
- Mammalian prestin is a weak Cl⁻/HCO₃⁻ electrogenic antiporter.The Journal of physiology · 2012Article
- A motif of eleven amino acids is a structural adaptation that facilitates motor capability of eutherian prestin.Journal of cell science · 2012Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Pendrin and prestin both belong to a distinct anion transporter family called solute carrier protein 26A, or SLC26A. Pendrin (SLC26A4) is a chloride-iodide transporter that is found at the luminal membrane of follicular cells in the thyroid gland as well as in the endolymphatic duct and sac of the inner ear, whereas prestin (SLC26A5) is expressed in the plasma membrane of cochlear outer hair cells and functions as a unique voltage-dependent motor. We recently identified a motif that is critical for the motor function of prestin. We questioned whether it was possible to create a chimeric pendrin protein with motor capability by integrating this motility motif from prestin. The chimeric pendrin was constructed by substituting residues 160-179 in human pendrin with residues 156-169 from gerbil prestin. Non-linear capacitance and somatic motility, two hallmarks representing prestin function, were measured from chimeric pendrin-transfected human embryonic kidney 293 cells using the voltage clamp technique and photodiode-based displacement measurement system. We showed that this 14-amino acid substitution from prestin was able to confer pendrin with voltage-dependent motor capability despite the amino acid sequence disparity between pendrin and prestin. The molecular mechanism that facilitates motor function appeared to be the same as prestin because the motor activity depended on the concentration of intracellular chloride and was blocked by salicylate treatment. Radioisotope-labeled formate uptake measurements showed that the chimeric pendrin protein retained the capability to transport formate, suggesting that the gain of motor function was not at the expense of its inherent transport capability. Thus, the engineered pendrin was capable of both transporting anions and generating force.
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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.