Evidence map›Paper›PMID 19286978›Full record

ArticleAmerican journal of respiratory cell and molecular biology2009

Ubiquitination participates in the lysosomal degradation of Na,K-ATPase in steady-state conditions.

Emilia Lecuona, Haiying Sun, Christine Vohwinkel, Aaron Ciechanover, Jacob I Sznajder

Abstract read
In one paragraph

Article in American journal of respiratory cell and molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Mechanisms of impaired alveolar fluid clearance.Anatomical record (Hoboken, N.J. : 2007) · 2025
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  10. The inositol pyrophosphate 5-InsPScience advances · 2020
    Article
  11. American journal of physiology. Gastrointestinal and liver physiology · 2020
    Article
  12. Article
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  15. Article
  16. Article
  17. Article
  18. Protein expression profile of rat type two alveolar epithelial cells during hyperoxic stress and recovery.American journal of physiology. Lung cellular and molecular physiology · 2013
    Article
  19. Functional genomic assessment of phosgene-induced acute lung injury in mice.American journal of respiratory cell and molecular biology · 2013
    Article
  20. 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

5 authors at 1 institution in 2 countries.

Emilia LecuonaPulmonary and Critical Care Medicine, Feinberg School of Medicine, Northwestern University, 240 E. Huron, McGaw M300, Chicago, IL 60611, USA. e-lecuona@northwestern.edu
Haiying Sun
Christine Vohwinkel
Aaron Ciechanover
Jacob I Sznajder
Northwestern University · US

Funding

Role of LUBAC and Na K-ATPase in Acute Lung InjuryP01HL071643 · NHLBI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CHANDEL, NAVDEEP S · 2003 to 2019
$30.8M
The injurious effects of hypercapnia on the alveolar epitheliumR01HL085534 · NHLBI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SZNAJDER, JACOB I · 2006 to 2018
$4.9M
Role and Regulation of Sodium, Potasium ATPase in LungR37HL048129 · NHLBI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SZNAJDER, JACOB I · 2008 to 2017
$4.0M
ROLE AND REGULATION OF SODIUM, POTASSIUM ATPASE IN LUNGR01HL048129 · NHLBI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SZNAJDER, JACOB I · 1996 to 2007
$2.7M
NHLBI NIH HHS HL48129NHLBI NIH HHS HL71643NHLBI NIH HHS HL85534
6 · The paper itself

Abstract

The alveolar epithelial cell (AEC) Na,K-ATPase contributes to vectorial Na(+) transport and plays an important role in keeping the lungs free of edema. We determined, by cell surface labeling with biotin and immunofluorescence, that approximately 30% of total Na,K-ATPase is at the plasma membrane of AEC in steady-state conditions. The half-life of the plasma membrane Na,K-ATPase was about 4 hours, and the incorporation of new Na,K-ATPase to the plasma membrane was Brefeldin A sensitive. Both protein kinase C (PKC) inhibition with bisindolylmaleimide (10 microM) and infection with an adenovirus expressing dominant-negative PKCzeta prevented Na,K-ATPase degradation. In cells expressing the Na,K-ATPase alpha1-subunit lacking the PKC phosphorylation sites, the plasma membrane Na,K-ATPase had a moderate increase in half-life. We also found that the Na,K-ATPase was ubiquitinated in steady-state conditions and that proteasomal inhibitors prevented its degradation. Interestingly, mutation of the four lysines described to be necessary for ubiquitination and endocytosis of the Na,K-ATPase in injurious conditions did not have an effect on its half-life in steady-state conditions. Lysosomal inhibitors prevented Na,K-ATPase degradation, and co-localization of Na,K-ATPase and lysosomes was found after labeling and chasing the plasma membrane Na,K-ATPase for 4 hours. Accordingly, we provide evidence suggesting that phosphorylation and ubiquitination are necessary for the steady-state degradation of the plasma membrane Na,K-ATPase in the lysosomes in alveolar epithelial cells.

Indexed as

AnimalsCell LineCell MembraneCells, CulturedEndocytosisEpithelial CellsGreen Fluorescent ProteinsHalf-LifeHumansKineticsLysosomesPhosphorylationProtein Kinase CProtein Kinase C zetaPulmonary AlveoliRatsGreen Fluorescent ProteinsProtein Kinase CProtein Kinase C zetaRecombinant Fusion ProteinsSodium-Potassium-Exchanging ATPase

Identifiers

PMID19286978
PMCPMC2784405
OpenAlexW2000917227

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.