Evidence map›Paper›PMID 22506713›Full record

ReviewCritical reviews in biochemistry and molecular biology

Organization of the ENaC-regulatory machinery.

Rama Soundararajan, Ming Lu, David Pearce

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. The renal response to potassium stress: integrating past with present.Current opinion in nephrology and hypertension · 2017
    Review
  13. Article
  14. Serum and Glucocorticoid Regulated Kinase 1 in Sodium Homeostasis.International journal of molecular sciences · 2016
    Review
  15. Regulation of the epithelial Na+ channel by the mTORC2/SGK1 pathway.Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association · 2016
    Review
  16. Review
  17. Article
  18. Inhibition of ENaC by endothelin-1.Vitamins and hormones · 2015
    Review
  19. Review
  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

3 authors at 1 institution in 1 country.

Rama SoundararajanDivision of Nephrology, Department of Medicine, University of California San Francisco, San Francisco, CA 94143, USA.
Ming Lu
David Pearce
University of California, San Francisco · US

Funding

SGK Regulation of Epithelial Sodium TransportR01DK056695 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DAVID PEARCE · 2000 to 2026
$8.1M
GILZ Regulation of ENaCR01DK085101 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PEARCE, DAVID · 2009 to 2012
$1.4M
The Functional Role of GilZ in Epithelial Sodium TransportK01DK078679 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SOUNDARARAJAN, RAMA · 2007 to 2011
$690k
NIDDK NIH HHS K01 DK078679NIDDK NIH HHS K01-DK078679NIDDK NIH HHS R01 DK056695NIDDK NIH HHS R01 DK085101NIDDK NIH HHS R01-DK56695NIDDK NIH HHS R01-DK85101
6 · The paper itself

Abstract

The control of fluid and electrolyte homeostasis in vertebrates requires the integration of a diverse set of signaling inputs, which control epithelial Na(+) transport, the principal ionic component of extracellular fluid. The key site of regulation is a segment of the kidney tubules, frequently termed the aldosterone-sensitive distal nephron, wherein the epithelial Na(+) channel (or ENaC) mediates apical ion entry. Na(+) transport in this segment is strongly regulated by the salt-retaining hormone, aldosterone, which acts through the mineralocorticoid receptor (MR) to influence the expression of a selected set of target genes, most notably the serine-threonine kinase SGK1, which phosphorylates and inhibits the E3 ubiquitin ligase Nedd4-2. It has long been known that ENaC activity is tightly regulated in vertebrate epithelia. Recent evidence suggests that SGK1 and Nedd4-2, along with other ENaC-regulatory proteins, physically associate with each other and with ENaC in a multi-protein complex. The various components of the complex are regulated by diverse signaling networks, including steroid receptor-, PI3-kinase-, mTOR-, and Raf-MEK-ERK-dependent pathways. In this review, we focus on the organization of the targets of these pathways by multi-domain scaffold proteins and lipid platforms into a unified complex, thereby providing a molecular basis for signal integration in the control of ENaC.

Indexed as

AldosteroneAnimalsEpithelial Sodium ChannelsHumansMembrane MicrodomainsNuclear Matrix-Associated ProteinsSignal TransductionAldosteroneEpithelial Sodium ChannelsNuclear Matrix-Associated Proteins

Identifiers

PMID22506713
PMCPMC4319811
OpenAlexW2074467476

What OpenQuestion holds

Textmetadata
LicenceTDM
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.