Evidence map›Paper›PMID 19333618›Full record

ArticlePflugers Archiv : European journal of physiology2009

AMPK controls epithelial Na(+) channels through Nedd4-2 and causes an epithelial phenotype when mutated.

Joana Almaça, Patthara Kongsuphol, Bernhard Hieke, Jiraporn Ousingsawat, Benoit Viollet, Rainer Schreiber, Margarida D Amaral, Karl Kunzelmann

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
9.1field-weighted citation impact, top 2% 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

33 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Review
  3. STIM1 in tumor cell death: angel or devil?Cell death discovery · 2023
    Review
  4. Article
  5. Article
  6. AMPK phosphorylation of the βAmerican journal of physiology. Renal physiology · 2019
    Article
  7. Article
  8. AMP-Activated Protein Kinase (AMPK)-Dependent Regulation of Renal Transport.International journal of molecular sciences · 2018
    Review
  9. βThe Journal of biological chemistry · 2018
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. AMP-activated protein kinase regulates hERG potassium channel.Pflugers Archiv : European journal of physiology · 2013
    Article
  17. AMPK couples plasma renin to cellular metabolism by phosphorylation of ACC1.American journal of physiology. Renal physiology · 2013
    Article
  18. Article
  19. Article
  20. AMPK: A regulator of ion channels.Communicative & integrative biology · 2012
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

Joana AlmaçaDepartment of Physiology, University of Regensburg, Regensburg, Germany.
Patthara Kongsuphol
Bernhard Hieke
Jiraporn Ousingsawat
Benoit Viollet
Rainer Schreiber
Margarida D Amaral
Karl Kunzelmann
University of Regensburg · DEInserm · FRNational Institute of Health Dr. Ricardo Jorge · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The metabolic sensor adenosine-monophosphate-activated kinase (AMPK) detects the cellular energy status and adjusts metabolic activity according to the cytosolic AMP to ATP ratio. Na(+) absorption by epithelial Na(+) channels (ENaC) is a highly energy-consuming process that is inhibited by AMPK. We show that the catalytic subunit alpha1 of AMPK inhibits ENaC in epithelial tissues from airways, kidney, and colon and that AMPK regulation of ENaC is absent in AMPKalpha1-/- mice. These mice demonstrate enhanced electrogenic Na(+) absorption that leads to subtle changes in intestinal and renal function and may also affect Na(+) absorption and mucociliary clearance in the airways. We demonstrate that AMPK uses the ubiquitin ligase Nedd4-2 to inhibit ENaC by increasing ubiquitination and endocytosis of ENaC. Thus, enhanced expression of epithelial Na(+) channels was detected in colon, airways, and kidney of AMPKalpha1-/- mice. Therefore, AMPKalpha1 is a physiologically important regulator of electrogenic Na(+) absorption and may provide a novel pharmacological target for controlling epithelial Na(+) transport.

Indexed as

AMP-Activated Protein KinasesAnimalsCells, CulturedEndosomal Sorting Complexes Required for TransportEpithelial CellsEpithelial Sodium ChannelsMiceMice, KnockoutMutationNedd4 Ubiquitin Protein LigasesSodiumUbiquitin-Protein LigasesAMP-Activated Protein KinasesEndosomal Sorting Complexes Required for TransportEpithelial Sodium ChannelsNedd4l protein, mouseNedd4 Ubiquitin Protein LigasesSodiumUbiquitin-Protein Ligases

Identifiers

PMID19333618
OpenAlexW1983563653

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.