Evidence map›Paper›PMID 29624167›Full record

ArticleeLife2018

Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation.

Richard S Marshall, Richard D Vierstra

RetractedOpen access · goldAbstract readRetracted Publication
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 49 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 1 pooled it
5.9field-weighted citation impact, top 3% 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

49 citing papers in PubMed, 1 synthesis or guideline pooled it, 91 citations in OpenAlex.

  1. Guideline
  2. Review
  3. Proteasome condensate formation is driven by multivalent interactions with shuttle factors and ubiquitin chains.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Quiescence inAnnual review of genetics · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Design principles that protect the proteasome from self-destruction.Protein science : a publication of the Protein Society · 2022
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Quiescence Through the Prism of Evolution.Frontiers in cell and developmental biology · 2021
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Richard S MarshallDepartment of Biology, Washington University in St. Louis, St. Louis, United States.ORCID 0000-0002-6844-1078
Richard D VierstraDepartment of Biology, Washington University in St. Louis, St. Louis, United States.ORCID 0000-0003-0210-3516
Washington University in St. Louis · US

Funding

Autophagic Clearance of Proteasomes and CDC48 as Models for Amyloidogenic Protein Quality Control.R01GM124452 · NIGMS · WASHINGTON UNIVERSITY · PI JEZ, JOSEPH MARTIN · 2018 to 2025
$2.4M
NIGMS NIH HHS R01 GM124452NIH HHS R01-GM124452-01A1
6 · The paper itself

Abstract

26S proteasome abundance is tightly regulated at multiple levels, including the elimination of excess or inactive particles by autophagy. In yeast, this proteaphagy occurs upon nitrogen starvation but not carbon starvation, which instead stimulates the rapid sequestration of proteasomes into cytoplasmic puncta termed proteasome storage granules (PSGs). Here, we show that PSGs help protect proteasomes from autophagic degradation. Both the core protease and regulatory particle sub-complexes are sequestered separately into PSGs via pathways dependent on the accessory proteins Blm10 and Spg5, respectively. Modulating PSG formation, either by perturbing cellular energy status or pH, or by genetically eliminating factors required for granule assembly, not only influences the rate of proteasome degradation, but also impacts cell viability upon recovery from carbon starvation. PSG formation and concomitant protection against proteaphagy also occurs in

Indexed as

AutophagyArabidopsisCarbonCytoplasmic GranulesNitrogenProteasome Endopeptidase ComplexProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationATP dependent 26S proteaseCarbonNitrogenProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsUbiquitinA. thalianaautophagybiochemistrycell biologychemical biologyproteaphagyproteasomeproteasome storage granulesS. cerevisiaestarvationubiquitin

Identifiers

PMID29624167
PMCPMC5947986
OpenAlexW2795907507

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.