Evidence map›Paper›PMID 21151492›Full record

ArticlePloS one2010

Interplay of substrate retention and export signals in endoplasmic reticulum quality control.

Shinichi Kawaguchi, Chia-Ling Hsu, Davis T W Ng

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Protein quality control in the secretory pathway.The Journal of cell biology · 2019
    Review
  6. Article
  7. The glycan-dependent ERAD machinery degrades topologically diverse misfolded proteins.The Plant journal : for cell and molecular biology · 2018
    Article
  8. Protein sorting at the ER-Golgi interface.The Journal of cell biology · 2016
    Review
  9. Article
  10. Review
  11. Article
  12. The endoplasmic reticulum-associated degradation pathways of budding yeast.Cold Spring Harbor perspectives in biology · 2012
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. 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

3 authors at 2 institutions in 1 country.

Shinichi KawaguchiTemasek Life Sciences Laboratory, Department of Biological Sciences, National University of Singapore, Singapore, Singapore.
Chia-Ling Hsu
Davis T W Ng
National University of Singapore · SGTemasek Life Sciences Laboratory · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundEndoplasmic reticulum (ER) quality control mechanisms are part of a comprehensive system to manage cell stress. The flux of molecules is monitored to retain folding intermediates and target misfolded molecules to ER-associated degradation (ERAD) pathways. The mechanisms of sorting remain unclear. While some proteins are retained statically, the classical model substrate CPY* is found in COPII transport vesicles, suggesting a retrieval mechanism for retention. However, its management can be even more dynamic. If ERAD is saturated under stress, excess CPY* traffics to the vacuole for degradation. These observations suggest that misfolded proteins might display different signals for their management. METHODOLOGY/PRINCIPAL

findingsHere, we report the existence of a functional ER exit signal in the pro-domain of CPY*. Compromising its integrity causes ER retention through exclusion from COPII vesicles. The signal co-exists with other signals used for retention and degradation. Physiologically, the export signal is important for stress tolerance. Disabling it converts a benign protein into one that is intrinsically cytotoxic. CONCLUSIONS/SIGNIFICANCE: These data reveal the remarkable interplay between opposing signals embedded within ERAD substrate molecules and the mechanisms that decipher them. Our findings demonstrate the diversity of mechanisms deployed for protein quality control and maintenance of protein homeostasis.

Indexed as

Signal TransductionEndoplasmic ReticulumGlycosylationGolgi ApparatusMicroscopy, FluorescenceMutationPolysaccharidesProtein FoldingProtein Processing, Post-TranslationalProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPolysaccharidesSaccharomyces cerevisiae Proteins

Identifiers

PMID21151492
PMCPMC2991357
OpenAlexW2033651879

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.