Evidence map›Paper›PMID 20843792›Full record

ArticleThe Journal of biological chemistry2010

ASK1 negatively regulates the 26 S proteasome.

Ji Won Um, Eunju Im, Joongkyu Park, Yohan Oh, Boram Min, Hyun Jung Lee, Jong Bok Yoon, Kwang Chul Chung

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

27 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. cGMP via PKG activates 26S proteasomes and enhances degradation of proteins, including ones that cause neurodegenerative diseases.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Review
  7. Review
  8. Review
  9. Exploring the Regulation of Proteasome Function by Subunit Phosphorylation.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond.Journal of molecular and cellular cardiology · 2014
    Review
  19. Article
  20. 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

8 authors at 1 institution in 1 country.

Ji Won UmDepartment of Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea.
Eunju Im
Joongkyu Park
Yohan Oh
Boram Min
Hyun Jung Lee
Jong Bok Yoon
Kwang Chul Chung
Yonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 26 S proteasome, composed of the 20 S core and 19 S regulatory particle, plays a central role in ubiquitin-dependent proteolysis. Disruption of this process contributes to the pathogenesis of the various diseases; however, the mechanisms underlying the regulation of 26 S proteasome activity remain elusive. Here, cell culture experiments and in vitro assays demonstrated that apoptosis signal-regulating kinase 1 (ASK1), a member of the MAPK kinase kinase family, negatively regulated 26 S proteasome activity. Immunoprecipitation/Western blot analyses revealed that ASK1 did not interact with 20 S catalytic core but did interact with ATPases making up the 19 S particle, which is responsible for recognizing polyubiquitinated proteins, unfolding them, and translocating them into the 20 S catalytic core in an ATP-dependent process. Importantly, ASK1 phosphorylated Rpt5, an AAA ATPase of the 19 S proteasome, and inhibited its ATPase activity, an effect that may underlie the ability of ASK1 to inhibit 26 S proteasome activity. The current findings point to a novel role for ASK1 in the regulation of 26 S proteasome and offer new strategies for treating human diseases caused by proteasome malfunction.

Indexed as

AnimalsBlotting, WesternCells, CulturedEmbryo, MammalianFibroblastsGliomaHeLa CellsHumansImmunoprecipitationKidneyMAP Kinase Kinase Kinase 5MiceMice, KnockoutNeuroblastomaProteasome Endopeptidase ComplexProtein SubunitsATP dependent 26S proteaseMAP Kinase Kinase Kinase 5Proteasome Endopeptidase ComplexProtein SubunitsRNA, MessengerRNA, Small Interfering

Identifiers

PMID20843792
PMCPMC2978573
OpenAlexW2086207143

What OpenQuestion holds

Textmetadata
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.