Evidence map›Paper›PMID 19383462›Full record

ArticleBiophysical journal2009

Prestin's anion transport and voltage-sensing capabilities are independent.

Jun-Ping Bai, Alexei Surguchev, Simone Montoya, Peter S Aronson, Joseph Santos-Sacchi, Dhasakumar Navaratnam

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

56 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. SLC26 Anion Transporters.Handbook of experimental pharmacology · 2024
    Review
  7. Article
  8. Article
  9. Oxalate homeostasis.Nature reviews. Nephrology · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Outer Hair Cells and Electromotility.Cold Spring Harbor perspectives in medicine · 2019
    Review
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

6 authors at 1 institution in 1 country.

Jun-Ping BaiDepartment of Neurology, Yale University School of Medicine, New Haven, Connecticut, USA.
Alexei Surguchev
Simone Montoya
Peter S Aronson
Joseph Santos-Sacchi
Dhasakumar Navaratnam
Yale University · US

Funding

MEMBRANES PROPERTIES OF CELLS COMPRISING THE OHC SYSTEMR01DC000273 · NIDCD · YALE UNIVERSITY · PI SANTOS-SACCHI, JOSEPH R · 1989 to 2015
$6.8M
Roles of SLC26A6 in Renal NaCI Transport and Prevention of Oxalate UrolithiasisR37DK033793 · NIDDK · YALE UNIVERSITY · PI ARONSON, PETER S. · 1994 to 2016
$6.8M
Structural correlates of prestin activity.R01DC008130 · NIDCD · YALE UNIVERSITY · PI NAVARATNAM, DHASAKUMAR S, SANTOS-SACCHI, JOSEPH R · 2007 to 2021
$6.1M
NIDCD NIH HHS DC 000273NIDCD NIH HHS DC 008130NIDCD NIH HHS R01 DC000273NIDCD NIH HHS R01 DC008130NIDDK NIH HHS R37 DK033793
6 · The paper itself

Abstract

The integral membrane protein prestin, a member of the SLC26 anion transporter family, is responsible for the voltage-driven electromotility of mammalian outer hair cells. It was argued that the evolution of prestin's motor function required a loss of the protein's transport capabilities. Instead, it was proposed that prestin manages only an abortive hemicycle that results in the trapped anion acting as a voltage sensor, to generate the motor's signature gating charge movement or nonlinear capacitance. We demonstrate, using classical radioactive anion ([(14)C]formate and [(14)C]oxalate) uptake studies, that in contrast to previous observations, prestin is able to transport anions. The prestin-dependent uptake of both these anions was twofold that of cells transfected with vector alone, and comparable to SLC26a6, prestin's closest phylogenetic relative. Furthermore, we identify a potential chloride-binding site in which the mutations of two residues (P328A and L326A) preserve nonlinear capacitance, yet negate anion transport. Finally, we distinguish 12 charged residues out of 22, residing within prestin's transmembrane regions, that contribute to unitary charge movement, i.e., voltage sensing. These data redefine our mechanistic concept of prestin.

Indexed as

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAnalysis of VarianceAnimalsAnion Transport ProteinsAntiportersCarbon RadioisotopesChloridesCHO CellsCricetinaeCricetulusElectric CapacitanceFormatesGerbillinaeIon TransportMiceMutation, Missense4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAnion Transport ProteinsAntiportersCarbon RadioisotopesChloridesFormatesformic acidOxalatesSalicylatesSlc26a6 protein, mouseSulfate Transporters

Identifiers

PMID19383462
PMCPMC2718310
OpenAlexW2067797983

What OpenQuestion holds

Textmetadata
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.