Evidence map›Paper›PMID 20943949›Full record

ArticleMolecular biology of the cell2010

AS160 associates with the Na+,K+-ATPase and mediates the adenosine monophosphate-stimulated protein kinase-dependent regulation of sodium pump surface expression.

Daiane S Alves, Glen A Farr, Patricia Seo-Mayer, Michael J Caplan

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. The role of AMPK in regulation of NaJournal of muscle research and cell motility · 2021
    Review
  4. Article
  5. AMPK alleviates high uric acid-induced NaExperimental & molecular medicine · 2019
    Article
  6. Article
  7. AMP-Activated Protein Kinase (AMPK)-Dependent Regulation of Renal Transport.International journal of molecular sciences · 2018
    Review
  8. Coordinated Control of ENaC and Na+,K+-ATPase in Renal Collecting Duct.Journal of the American Society of Nephrology : JASN · 2016
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Reciprocal regulation of endocytosis and metabolism.Cold Spring Harbor perspectives in biology · 2014
    Review
  15. Article
  16. Article
  17. AMPK couples plasma renin to cellular metabolism by phosphorylation of ACC1.American journal of physiology. Renal physiology · 2013
    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

4 authors at 1 institution in 1 country.

Daiane S AlvesDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026, USA.
Glen A Farr
Patricia Seo-Mayer
Michael J Caplan
Yale University · US

Funding

The Regulation of Renal Epithelial Cell Junction Assembly and PolarizationP01DK017433 · NIDDK · YALE UNIVERSITY · PI FORBUSH, BLISS · 1986 to 2018
$29.5M
Pathways and Partners in Renal Epithelial Cell PolarityR01DK072614 · NIDDK · YALE UNIVERSITY · PI CAPLAN, MICHAEL J. · 2005 to 2022
$6.9M
NIDDK NIH HHS DK-072612NIDDK NIH HHS DK-17433NIDDK NIH HHS P01 DK017433NIDDK NIH HHS R01 DK072614
6 · The paper itself

Abstract

The Na(+),K(+)-ATPase is the major active transport protein found in the plasma membranes of most epithelial cell types. The regulation of Na(+),K(+)-ATPase activity involves a variety of mechanisms, including regulated endocytosis and recycling. Our efforts to identify novel Na(+),K(+)-ATPase binding partners revealed a direct association between the Na(+),K(+)-ATPase and AS160, a Rab-GTPase-activating protein. In COS cells, coexpression of AS160 and Na(+),K(+)-ATPase led to the intracellular retention of the sodium pump. We find that AS160 interacts with the large cytoplasmic NP domain of the α-subunit of the Na(+),K(+)-ATPase. Inhibition of the activity of the adenosine monophosphate-stimulated protein kinase (AMPK) in Madin-Darby canine kidney cells through treatment with Compound C induces Na(+),K(+)-ATPase endocytosis. This effect of Compound C is prevented through the short hairpin RNA-mediated knockdown of AS160, demonstrating that AMPK and AS160 participate in a common pathway to modulate the cell surface expression of the Na(+),K(+)-ATPase.

Indexed as

AMP-Activated Protein KinasesAnimalsBiological TransportCell LineChlorocebus aethiopsCOS CellsDogsDose-Response Relationship, DrugEndocytosisEpithelial CellsGene ExpressionGene Knockdown TechniquesGTPase-Activating ProteinsHumansImmunoprecipitationPhosphorylationAMP-Activated Protein KinasesdorsomorphinGTPase-Activating ProteinsPyrazolesPyrimidinesSodium-Potassium-Exchanging ATPaseTBC1D4 protein, human

Identifiers

PMID20943949
PMCPMC3002392
OpenAlexW2096192678

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.