Evidence map›Paper›PMID 20110346›Full record

ArticleMolecular biology of the cell2010

The endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones.

Teresa M Buck, Alexander R Kolb, Cary R Boyd, Thomas R Kleyman, Jeffrey L Brodsky

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 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
3.5field-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

66 citing papers in PubMed, 88 citations in OpenAlex.

  1. The scaffold protein IQGAP1 regulates the epithelial NaThe Journal of biological chemistry · 2025
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  2. Review
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  6. Review
  7. Article
  8. Paraoxonase 2 is an ER chaperone that regulates the epithelial NaAmerican journal of physiology. Cell physiology · 2022
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis.Biochimica et biophysica acta. Molecular cell research · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

6 more citing papers are in PubMed but not listed here.

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 1 country.

Teresa M BuckDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Alexander R Kolb
Cary R Boyd
Thomas R Kleyman
Jeffrey L Brodsky
University of Pittsburgh · US

Funding

Single Nephron and MetabolomicsP30DK079307 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CARATTINO, MARCELO DANIEL · 2008 to 2022
$13.4M
ER Associated Degradation of Membrane Proteins in YeastR01GM075061 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BRODSKY, JEFFREY L. · 2006 to 2019
$3.2M
Renal and Epithelial Biology Training ProgramT32DK061296 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLEYMAN, THOMAS R · 2002 to 2022
$3.1M
Sodium Channel BiogenesisR01DK065161 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HUGHEY, REBECCA P, KLEYMAN, THOMAS R · 2004 to 2013
$2.8M
Sodium Channel BiogenesisR56DK065161 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HUGHEY, REBECCA P, KLEYMAN, THOMAS R · 2008 to 2008
$226k
Identification and Characterization of Factors Involved in ENaC BiogenesisF32GM083540 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BUCK, TERESA M · 2008 to 2009
$80k
NIDDK NIH HHS DK61296NIDDK NIH HHS DK65161NIDDK NIH HHS DK79307NIDDK NIH HHS P30 DK079307NIDDK NIH HHS R01 DK065161NIDDK NIH HHS R56 DK065161NIDDK NIH HHS T32 DK061296NIGMS NIH HHS F32 GM083540NIGMS NIH HHS GM75061NIGMS NIH HHS GM83540NIGMS NIH HHS R01 GM075061
6 · The paper itself

Abstract

The epithelial sodium channel (ENaC) is composed of a single copy of an alpha-, beta-, and gamma-subunit and plays an essential role in water and salt balance. Because ENaC assembles inefficiently after its insertion into the ER, a substantial percentage of each subunit is targeted for ER-associated degradation (ERAD). To define how the ENaC subunits are selected for degradation, we developed novel yeast expression systems for each ENaC subunit. Data from this analysis suggested that ENaC subunits display folding defects in more than one compartment and that subunit turnover might require a unique group of factors. Consistent with this hypothesis, yeast lacking the lumenal Hsp40s, Jem1 and Scj1, exhibited defects in ENaC degradation, whereas BiP function was dispensable. We also discovered that Jem1 and Scj1 assist in ENaC ubiquitination, and overexpression of ERdj3 and ERdj4, two lumenal mammalian Hsp40s, increased the proteasome-mediated degradation of ENaC in vertebrate cells. Our data indicate that Hsp40s can act independently of Hsp70 to select substrates for ERAD.

Indexed as

AnimalsEndoplasmic ReticulumEpithelial Sodium ChannelsMiceMolecular ChaperonesOocytesPatch-Clamp TechniquesProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationXenopus laevisEpithelial Sodium ChannelsMolecular ChaperonesProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID20110346
PMCPMC2836957
OpenAlexW2099465007

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.