Evidence map›Paper›PMID 15743908›Full record

ArticleMolecular biology of the cell2005

FXYD3 (Mat-8), a new regulator of Na,K-ATPase.

Gilles Crambert, Ciming Li, Dirk Claeys, Käthi Geering

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.8field-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

31 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. FXYD proteins and sodium pump regulatory mechanisms.The Journal of general physiology · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. FXYD8, a Novel Regulator of Renal NaFrontiers in physiology · 2017
    Article
  16. Article
  17. FXYD5: Na(+)/K(+)-ATPase Regulator in Health and Disease.Frontiers in cell and developmental biology · 2016
    Review
  18. Article
  19. Article
  20. The Na-K-ATPase α₁β₁ heterodimer as a cell adhesion molecule in epithelia.American journal of physiology. Cell physiology · 2012
    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

4 authors at 1 institution in 1 country.

Gilles CrambertDepartment of Pharmacology and Toxicology, University of Lausanne, CH-1005 Lausanne, Switzerland.
Ciming Li
Dirk Claeys
Käthi Geering
University of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Four of the seven members of the FXYD protein family have been identified as specific regulators of Na,K-ATPase. In this study, we show that FXYD3, also known as Mat-8, is able to associate with and to modify the transport properties of Na,K-ATPase. In addition to this shared function, FXYD3 displays some uncommon characteristics. First, in contrast to other FXYD proteins, which were shown to be type I membrane proteins, FXYD3 may have a second transmembrane-like domain because of the presence of a noncleavable signal peptide. Second, FXYD3 can associate with Na,K- as well as H,K-ATPases when expressed in Xenopus oocytes. However, in situ (stomach), FXYD3 is associated only with Na,K-ATPase because its expression is restricted to mucous cells in which H,K-ATPase is absent. Coexpressed in Xenopus oocytes, FXYD3 modulates the glycosylation processing of the beta subunit of X,K-ATPase dependent on the presence of the signal peptide. Finally, FXYD3 decreases both the apparent affinity for Na+ and K+ of Na,K-ATPase.

Indexed as

Amino Acid SequenceAnimalsCloning, MolecularFemaleGastric MucosaGlycosylationH(+)-K(+)-Exchanging ATPaseIn Vitro TechniquesMembrane ProteinsMiceMolecular Sequence DataMutagenesis, Site-DirectedNeoplasm ProteinsOocytesProtein Processing, Post-TranslationalProtein Sorting SignalsFxyd3 protein, mouseH(+)-K(+)-Exchanging ATPaseMembrane ProteinsNeoplasm ProteinsProtein Sorting SignalsRecombinant ProteinsSodium-Potassium-Exchanging ATPase

Identifiers

PMID15743908
PMCPMC1087241
OpenAlexW1965254924

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.