Evidence map›Paper›PMID 24710176›Full record

ArticleNature communications2014

Molecular architecture and the structural basis for anion interaction in prestin and SLC26 transporters.

Dmitry Gorbunov, Mattia Sturlese, Florian Nies, Murielle Kluge, Massimo Bellanda, Roberto Battistutta, Dominik Oliver

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.6field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

46 citing papers in PubMed, 91 citations in OpenAlex.

  1. Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026
    Review
  2. Article
  3. Review
  4. Structural Mechanism of Prestin-Membrane Mechanotransduction.bioRxiv : the preprint server for biology · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. SLC26 Anion Transporters.Handbook of experimental pharmacology · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mutation Screening and Functional Study ofJournal of clinical research in pediatric endocrinology · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Dmitry Gorbunov1] Department of Neurophysiology, Institute of Physiology and Pathophysiology, Philipps University, 35037 Marburg, Germany [2].
Mattia Sturlese1] Department of Chemical Sciences, University of Padua, via Marzolo 1, Padova 35131, Italy [2].
Florian NiesDepartment of Neurophysiology, Institute of Physiology and Pathophysiology, Philipps University, 35037 Marburg, Germany.
Murielle KlugeDepartment of Neurophysiology, Institute of Physiology and Pathophysiology, Philipps University, 35037 Marburg, Germany.
Massimo BellandaDepartment of Chemical Sciences, University of Padua, via Marzolo 1, Padova 35131, Italy.
Roberto Battistutta1] Department of Chemical Sciences, University of Padua, via Marzolo 1, Padova 35131, Italy [2] Venetian Institute for Molecular Medicine (VIMM), via Orus 2, Padova 35129, Italy.
Dominik OliverDepartment of Neurophysiology, Institute of Physiology and Pathophysiology, Philipps University, 35037 Marburg, Germany.
Philipps University of Marburg · DEUniversity of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prestin (SLC26A5) is a member of the SLC26/SulP anion transporter family. Its unique quasi-piezoelectric mechanical activity generates fast cellular motility of cochlear outer hair cells, a key process underlying active amplification in the mammalian ear. Despite its established physiological role, it is essentially unknown how prestin can generate mechanical force, since structural information on SLC26/SulP proteins is lacking. Here we derive a structural model of prestin and related transporters by combining homology modelling, MD simulations and cysteine accessibility scanning. Prestin's transmembrane core region is organized in a 7+7 inverted repeat architecture. The model suggests a central cavity as the substrate-binding site located midway of the anion permeation pathway, which is supported by experimental solute accessibility and mutational analysis. Anion binding to this site also controls the electromotile activity of prestin. The combined structural and functional data provide a framework for understanding electromotility and anion transport by SLC26 transporters.

Indexed as

AnimalsAnion Transport ProteinsAntiportersChickensDrosophilaDrosophila ProteinsEscherichia coli ProteinsHair Cells, Auditory, OuterMembrane Transport ProteinsMiceModels, StructuralMolecular Docking SimulationMolecular Motor ProteinsRatsSulfate TransportersZebrafishAnion Transport ProteinsAntiportersDrosophila ProteinsEscherichia coli ProteinsMembrane Transport ProteinsMolecular Motor ProteinsPres protein, mouseprestin protein, DrosophilaSlc26a5 protein, ratslc26a5 protein, zebrafishSlc26a6 protein, mouseSulfate TransportersUraA protein, E coliZebrafish Proteins

Identifiers

PMID24710176
PMCPMC3988826
OpenAlexW1980603636

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.