Evidence map›Paper›PMID 32246734›Full record

ArticleTraffic (Copenhagen, Denmark)2020

Size-dependent secretory protein reflux into the cytosol in association with acute endoplasmic reticulum stress.

Patrick Lajoie, Erik L Snapp

Abstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Spatial protein redistribution: wandering but not lost.Cellular and molecular life sciences : CMLS · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. ER chaperone GRP78/BiP translocates to the nucleus under stress and acts as a transcriptional regulator.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. CaBMC biology · 2020
    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

2 authors.

Patrick LajoieDepartment of Anatomy and Cell Biology, The University of Western Ontario, London, Ontario, Canada.ORCID 0000-0002-1614-176X
Erik L SnappJanelia Research Campus Ashburn, Virginia, USA.ORCID 0000-0001-9482-2272

Funding

Natural Sciences and Engineering Research Council of Canada RGPIN-2015-06400NIGMS NIH HHS 1R01GM10599-01
6 · The paper itself

Abstract

Once secretory proteins have been targeted to the endoplasmic reticulum (ER) lumen, the proteins typically remain partitioned from the cytosol. If the secretory proteins misfold, they can be unfolded and retrotranslocated into the cytosol for destruction by the proteasome by ER-Associated protein Degradation (ERAD). Here, we report that correctly folded and targeted luminal ER fluorescent protein reporters accumulate in the cytosol during acute misfolded secretory protein stress in yeast. Photoactivation fluorescence microscopy experiments reveal that luminal reporters already localized to the ER relocalize to the cytosol, even in the absence of essential ERAD machinery. We named this process "ER reflux." Reflux appears to be regulated in a size-dependent manner for reporters. Interestingly, prior heat shock stress also prevents ER stress-induced reflux. Together, our findings establish a new ER stress-regulated pathway for relocalization of small luminal secretory proteins into the cytosol, distinct from the ERAD and preemptive quality control pathways. Importantly, our results highlight the value of fully characterizing the cell biology of reporters and describe a simple modification to maintain luminal ER reporters in the ER during acute ER stress.

Indexed as

Endoplasmic Reticulum StressProtein FoldingCytosolEndoplasmic ReticulumEndoplasmic Reticulum-Associated Degradationendoplasmic reticulumERADfluorescent proteinGFPintracellular transportphotoactivationsignal peptidetraffictranslocationUPR

Identifiers

PMID32246734
PMCPMC7317852

What OpenQuestion holds

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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.