Evidence map›Paper›PMID 20418376›Full record

ArticleThe Journal of biological chemistry2010

Prestin surface expression and activity are augmented by interaction with MAP1S, a microtubule-associated protein.

Jun-Ping Bai, Alexei Surguchev, Yudelca Ogando, Lei Song, Shumin Bian, Joseph Santos-Sacchi, Dhasakumar Navaratnam

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. STAS domain structure and function.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2011
    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

7 authors.

Jun-Ping BaiDepartment of Neurology, Yale University School of Medicine, New Haven, CT 06510, USA.
Alexei Surguchev
Yudelca Ogando
Lei Song
Shumin Bian
Joseph Santos-Sacchi
Dhasakumar Navaratnam

Funding

MEMBRANES PROPERTIES OF CELLS COMPRISING THE OHC SYSTEMR01DC000273 · NIDCD · YALE UNIVERSITY · PI SANTOS-SACCHI, JOSEPH R · 1989 to 2015
$6.8M
Structural correlates of prestin activity.R01DC008130 · NIDCD · YALE UNIVERSITY · PI NAVARATNAM, DHASAKUMAR S, SANTOS-SACCHI, JOSEPH R · 2007 to 2021
$6.1M
Studies on hair cell BK channelsR01DC007894 · NIDCD · YALE UNIVERSITY · PI NAVARATNAM, DHASAKUMAR S · 2006 to 2017
$3.6M
NIDCD NIH HHS DC 000273NIDCD NIH HHS DC 007894NIDCD NIH HHS DC 0081130NIDCD NIH HHS R01 DC000273NIDCD NIH HHS R01 DC007894NIDCD NIH HHS R01 DC008130
6 · The paper itself

Abstract

Prestin is a member of the SLC26 family of anion transporters that is responsible for outer hair cell (OHC) electromotility. Measures of voltage-evoked charge density (Q(sp)) of prestin indicated that the protein is highly expressed in OHCs, with single cells expressing up to 10 million molecules within the lateral membrane. In contrast, charge density measures in transfected cells indicated that they express, at best, only a fifth as many proteins on their surface. We sought to determine whether associations with other OHC-specific proteins could account for this difference. Using a yeast two-hybrid technique, we found microtubule-associated protein 1S (MAP1S) bound to prestin. The interaction was limited to the STAS domain of prestin and the region connecting the heavy and light chain of MAP1S. Using reciprocal immunoprecipitation and Forster resonance energy transfer, we confirmed these interactions. Furthermore, co-expression of prestin with MAP1S resulted in a 2.7-fold increase in Q(sp) in single cells that was paralleled by a 2.8-fold increase in protein surface expression, indicating that the interactions are physiological. Quantitative PCR data showed gradients in the expression of prestin and MAP1S across the tonotopic axis that may partially contribute to a previously observed 6-fold increase in Q(sp) in high frequency hair cells. These data highlight the importance of protein partner effects on prestin.

Indexed as

AnimalsAnion Transport ProteinsBrainCochleaColchicineDNA PrimersFluorescence Resonance Energy TransferGerbillinaeGuinea PigsHair Cells, Auditory, OuterMicrotubule-Associated ProteinsOrgan of CortiOrgan SpecificityPolymerase Chain ReactionProteinsRatsAnion Transport ProteinsColchicineDNA PrimersMicrotubule-Associated ProteinsPres protein, Cavia porcellusProteinsSlc26a5 protein, ratSulfate Transporters

Identifiers

PMID20418376
PMCPMC2898336

What OpenQuestion holds

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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.