Evidence map›Paper›PMID 26181331›Full record

ArticlePLoS genetics2015

A Role for Macro-ER-Phagy in ER Quality Control.

Zhanna Lipatova, Nava Segev

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed, 3 pooled it
7.6field-weighted citation impact, top 2% 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

50 citing papers in PubMed, 3 syntheses or guidelines pooled it, 78 citations in OpenAlex.

  1. Pooled it
  2. Guideline
  3. Guideline
  4. Review
  5. Review
  6. Article
  7. Viruses and autophagy: bend, but don't break.Nature reviews. Microbiology · 2024
    Review
  8. A selective ER-phagy exerts neuroprotective effects via modulation of α-synuclein clearance in parkinsonian models.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Protein quality control ofFrontiers in cellular neuroscience · 2022
    Review
  18. Article
  19. Endoplasmic Reticulum (ER) and ER-Phagy.Progress in molecular and subcellular biology · 2021
    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

2 authors at 1 institution in 1 country.

Zhanna LipatovaDepartment of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois, United States of America.
Nava SegevDepartment of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois, United States of America.
University of Illinois Chicago · US

Funding

YPTL GTPASE AND VESICULAR TRANSPORTR01GM045444 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SEGEV, NAVA · 1992 to 2020
$6.4M
NIGMS NIH HHS GM-45444NIGMS NIH HHS R01 GM045444
6 · The paper itself

Abstract

The endoplasmic-reticulum quality-control (ERQC) system shuttles misfolded proteins for degradation by the proteasome through the well-defined ER-associated degradation (ERAD) pathway. In contrast, very little is known about the role of autophagy in ERQC. Macro-autophagy, a collection of pathways that deliver proteins through autophagosomes (APs) for degradation in the lysosome (vacuole in yeast), is mediated by autophagy-specific proteins, Atgs, and regulated by Ypt/Rab GTPases. Until recently, the term ER-phagy was used to describe degradation of ER membrane and proteins in the lysosome under stress: either ER stress induced by drugs or whole-cell stress induced by starvation. These two types of stresses induce micro-ER-phagy, which does not use autophagic organelles and machinery, and non-selective autophagy. Here, we characterize the macro-ER-phagy pathway and uncover its role in ERQC. This pathway delivers 20-50% of certain ER-resident membrane proteins to the vacuole and is further induced to >90% by overexpression of a single integral-membrane protein. Even though such overexpression in cells defective in macro-ER-phagy induces the unfolded-protein response (UPR), UPR is not needed for macro-ER-phagy. We show that macro-ER-phagy is dependent on Atgs and Ypt GTPases and its cargo passes through APs. Moreover, for the first time the role of Atg9, the only integral-membrane core Atg, is uncoupled from that of other core Atgs. Finally, three sequential steps of this pathway are delineated: Atg9-dependent exit from the ER en route to autophagy, Ypt1- and core Atgs-mediated pre-autophagsomal-structure organization, and Ypt51-mediated delivery of APs to the vacuole.

Indexed as

AnimalsAutophagyAutophagy-Related ProteinsEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationEndoplasmic Reticulum StressLysosomesMembrane ProteinsProtein FoldingProteolysisrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsATG9 protein, S cerevisiaeAutophagy-Related ProteinsMembrane Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsVPS21 protein, S cerevisiaeYPT1 protein, S cerevisiae

Identifiers

PMID26181331
PMCPMC4504476
OpenAlexW986700140

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.