Evidence map›Paper›PMID 26670610›Full record

ArticleThe Journal of biological chemistry2016

Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles.

Kenrick A Waite, Alina De-La Mota-Peynado, Gabrielle Vontz, Jeroen Roelofs

Abstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed, 2 pooled it
–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

73 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Guideline
  2. Pooled it
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  14. 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
  15. Article
  16. Article
  17. Review
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  19. Article
  20. Quiescence inAnnual review of genetics · 2022
    Review

13 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

4 authors.

Kenrick A WaiteFrom the Division of Biology, Kansas State University, Manhattan, Kansas 66506.
Alina De-La Mota-PeynadoFrom the Division of Biology, Kansas State University, Manhattan, Kansas 66506.
Gabrielle VontzFrom the Division of Biology, Kansas State University, Manhattan, Kansas 66506.
Jeroen RoelofsFrom the Division of Biology, Kansas State University, Manhattan, Kansas 66506 jroelofs@ksu.edu.ORCID http://orcid.org/0000-0003-0944-2465

Funding

Mentoring CoreP20GM103418 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI SUSAN J. BROWN · 2012 to 2026
$63.0M
Mechanism of degradation of the proteasome through autophagyR01GM118660 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI ROELOFS, JEROEN · 2016 to 2020
$1.5M
Allosteric Mechanisms Controlling the Formation of Different Proteasome ComplexesR15GM112142 · NIGMS · KANSAS STATE UNIVERSITY · PI ROELOFS, JEROEN · 2015 to 2015
$360k
NIGMS NIH HHS 1R15GM112142-01A1NIGMS NIH HHS P20 GM103418NIGMS NIH HHS R01 GM118660NIGMS NIH HHS R15 GM112142
6 · The paper itself

Abstract

The proteasome is responsible for the degradation of many cellular proteins. If and how this abundant and normally stable complex is degraded by cells is largely unknown. Here we show that in yeast, upon nitrogen starvation, proteasomes are targeted for vacuolar degradation through autophagy. Using GFP-tagged proteasome subunits, we observed that autophagy of a core particle (CP) subunit depends on the deubiquitinating enzyme Ubp3, although a regulatory particle (RP) subunit does not. Furthermore, upon blocking of autophagy, RP remained largely nuclear, although CP largely localized to the cytosol as well as granular structures within the cytosol. In all, our data reveal a regulated process for the removal of proteasomes upon nitrogen starvation. This process involves CP and RP dissociation, nuclear export, and independent vacuolar targeting of CP and RP. Thus, in addition to the well characterized transcriptional up-regulation of genes encoding proteasome subunits, cells are also capable of down-regulating cellular levels of proteasomes through proteaphagy.

Indexed as

AutophagyMicrobiological PhenomenaStress, PhysiologicalAutophagy-Related Protein 7Autophagy-Related ProteinsCell NucleusEndopeptidasesGene DeletionGreen Fluorescent ProteinsMicroscopy, FluorescenceMutationNitrogen CycleNutritional Physiological PhenomenaProteasome Endopeptidase ComplexProtein TransportProteolysisAtg11 protein, S cerevisiaeATG7 protein, S cerevisiaeAutophagy-Related Protein 7Autophagy-Related ProteinsEndopeptidasesGreen Fluorescent ProteinsPRE2 protein, S cerevisiaeProteasome Endopeptidase ComplexRecombinant Fusion ProteinsRPN1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUBP3 protein, S cerevisiaeVesicular Transport Proteinsautophagydeubiquitylation (deubiquitination)nitrogen starvationproteaphagyproteasomeprotein translocationribophagyvacuoleyeast

Identifiers

PMID26670610
PMCPMC4751371

What OpenQuestion holds

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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.