Evidence map›Paper›PMID 31327703›Full record

ArticleCell chemical biology2019

Regulation of Autophagic Flux by the 20S Proteasome.

Evert Njomen, Jetze J Tepe

Open access · bronzeAbstract read
In one paragraph

Article in Cell chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. The roles of the ubiquitin-proteasome system in renal disease.International journal of medical sciences · 2025
    Review
  6. Proteasome: Role in T Cell Function Regulation.International journal of biological sciences · 2025
    Review
  7. Article
  8. Tumor biomarkers for diagnosis, prognosis and targeted therapy.Signal transduction and targeted therapy · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Small molecule probes for targeting autophagy.Nature chemical biology · 2021
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  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.

Evert NjomenDepartment of Chemistry and Pharmacology & Toxicology, Michigan State University, East Lansing, MI 48824, USA.
Jetze J TepeDepartment of Chemistry and Pharmacology & Toxicology, Michigan State University, East Lansing, MI 48824, USA. Electronic address: tepe@chemistry.msu.edu.
Michigan State University · US

Funding

Integrative Training in the Pharmacological SciencesT32GM092715 · NIGMS · MICHIGAN STATE UNIVERSITY · PI NEUBIG, RICHARD R · 2011 to 2020
$1.5M
Non-competitive proteasome inhibitors to treat chronic, drug-resistant tuberculosisR21AI117018 · NIAID · MICHIGAN STATE UNIVERSITY · PI ABRAMOVITCH, ROBERT B, TEPE, JETZE J. · 2016 to 2017
$400k
NIAID NIH HHS R21 AI117018NIGMS NIH HHS T32 GM092715
6 · The paper itself

Abstract

The proteolytic arm of the protein homeostasis network is maintained by both the ubiquitin-proteasome system (UPS) and autophagy. A well-balanced crosstalk between the two catabolic pathways ensures energy-efficient maintenance of cellular function. Our current understanding of the crosstalk between the UPS and autophagy is centered around substrate ubiquitination. Herein we report an additional method of crosstalk involving ubiquitin-independent 20S proteasome regulation of autophagosome-lysosome fusion. We found that enhancement of 20S proteasome activity increased the degradation of the disordered soluble N-ethylmaleimide-sensitive factor activating protein receptor proteins, synaptosomal-associated protein 29 (SNAP29), and syntaxin 17 (STX17), but not vesicle-associated membrane protein 8. This resulted in a reduction of autophagosome-lysosome fusion, which was ameliorated upon overexpression of both SNAP29 and STX17. In all, we herein present a mechanism of crosstalk between the proteasome and autophagy pathway that is regulated by ubiquitin-independent 20S proteasome-mediated degradation of SNAP29 and STX17.

Indexed as

AnimalsAutophagyCell LineHEK293 CellsHeLa CellsHumansLysosomesMembrane FusionProteasome Endopeptidase ComplexQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsR-SNARE ProteinsUbiquitinUbiquitinationProteasome Endopeptidase ComplexQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsR-SNARE ProteinsSNAP29 protein, humanUbiquitinVAMP8 protein, human20S proteasomeautophagosome-lysosome fusionautophagyproteasomeproteasome activationSNAP29SNARE proteinsSyntaxin17ubiquitin-independentUPS

Identifiers

PMID31327703
PMCPMC6754308
OpenAlexW2963023495

What OpenQuestion holds

Textmetadata
LicenceTDM
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.