Evidence map›Paper›PMID 21047933›Full record

ArticleJournal of neurophysiology2011

From zebrafish to mammal: functional evolution of prestin, the motor protein of cochlear outer hair cells.

Xiaodong Tan, Jason L Pecka, Jie Tang, Oseremen E Okoruwa, Qian Zhang, Kirk W Beisel, David Z Z He

Abstract read
In one paragraph

Article in Journal of neurophysiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

37 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Structural Mechanism of Prestin-Membrane Mechanotransduction.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. A Functional Perspective on the Evolution of the Cochlea.Cold Spring Harbor perspectives in medicine · 2019
    Review
  13. Water Waves to Sound Waves: Using Zebrafish to Explore Hair Cell Biology.Journal of the Association for Research in Otolaryngology : JARO · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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 1 institution in 1 country.

Xiaodong TanCreighton University School of Medicine, Department of Biomedical Sciences, 2500 California Plaza, Omaha, NE 68178, USA.
Jason L Pecka
Jie Tang
Oseremen E Okoruwa
Qian Zhang
Kirk W Beisel
David Z Z He
Creighton University · US

Funding

BIOPHYSICS AND DEVELOPMENT OF COCHLEAR OUTER HAIR CELLSR01DC004696 · NIDCD · FATHER FLANAGAN'S BOYS'HOME · PI HE, ZHI-ZHOU · 2001 to 2016
$4.2M
CONSTRUCTION OF RESEARCH FACILITYC06RR017417 · NCRR · CREIGHTON UNIVERSITY · PI WILSON, M. ROY · 2002 to 2002
$2.0M
MOLECULAR DISSECTION OF THE ORGAN OF CORTIR01DC005009 · NIDCD · FATHER FLANAGAN'S BOYS'HOME · PI BEISEL, KIRK W. · 2002 to 2006
$1.8M
NCRR NIH HHS C06 RR-17417NIDCD NIH HHS R01 DC-004696NIDCD NIH HHS R01 DC004696NIDCD NIH HHS R01 DC-005009
6 · The paper itself

Abstract

Prestin is the motor protein of cochlear outer hair cells. It belongs to a distinct anion transporter family called solute carrier protein 26A, or SLC26A. Members of this family serve two fundamentally distinct functions. Although most members transport different anion substrates across a variety of epithelia, prestin (SLC26A5) is unique, functioning as a voltage-dependent motor protein. Recent evidence suggests that prestin orthologs from zebrafish and chicken are electrogenic divalent/chloride anion exchangers/transporters with no motor function. These studies appear to suggest that prestin was evolved from an anion transporter. We examined the motor and transport functions of prestin and its orthologs from four different species in the vertebrate lineage, to gain insights of how these two physiological functions became distinct. Somatic motility, voltage-dependent nonlinear capacitance (NLC), and transporter function were measured in transfected human embryonic kidney (HEK) cells using voltage-clamp and anion uptake techniques. Zebrafish and chicken prestins both exhibited weak NLC, with peaks significantly shifted in the depolarization (right) direction. This was contrasted by robust NLC with peaks left shifted in the platypus and gerbil. The platypus and gerbil prestins retained little transporter function compared with robust anion transport capacities in the zebrafish and chicken orthologs. Somatic motility was detected only in the platypus and gerbil prestins. There appears to be an inverse relationship between NLC and anion transport functions, whereas motor function appears to have emerged only in mammalian prestin. Our results suggest that motor function is an innovation of therian prestin and is concurrent with diminished transporter capabilities.

Indexed as

Biological EvolutionAnimalsAnion Transport ProteinsAntiportersCell MovementCells, CulturedChickensCHO CellsCricetinaeCricetulusFemaleGerbillinaeHair Cells, Auditory, OuterHumansKidneyMotor ActivityAnion Transport ProteinsAntiportersslc26a5 protein, zebrafishZebrafish Proteins

Identifiers

PMID21047933
PMCPMC3023371
OpenAlexW2053476349

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.