Evidence map›Paper›PMID 19029946›Full record

ArticleEMBO reports2009

Quinone reductase acts as a redox switch of the 20S yeast proteasome.

Sonja Sollner, Markus Schober, Andrea Wagner, Anna Prem, Lucie Lorkova, Bruce A Palfey, Michael Groll, Peter Macheroux

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Context-dependent resistance to proteolysis of intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2011
    Review
  14. Article
  15. Article
  16. Flavin redox switching of protein functions.Antioxidants & redox signaling · 2011
    Review
  17. Article
  18. Article
  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 3 institutions in 3 countries.

Sonja SollnerInstitute of Biochemistry, Graz University of Technology, Graz, Austria.
Markus Schober
Andrea Wagner
Anna Prem
Lucie Lorkova
Bruce A Palfey
Michael Groll
Peter Macheroux
Graz University of Technology · ATTechnical University of Munich · DEUniversity of Michigan–Ann Arbor · US

Funding

Austrian Science Fund FWF W 901NIGMS NIH HHS R01GM61807
6 · The paper itself

Abstract

The proteasome has an essential function in the intracellular degradation of protein in eukaryotic cells. We found that the dimeric quinone reductase Lot6 uses the flavin mononucleotide (FMN)-binding site to bind to the 20S proteasome with a 1:2 stoichiometry-that is, one 20S proteasome molecule can associate with two quinone reductases. Furthermore, reduction of the FMN cofactor by either NADH or light irradiation results in the binding of the b-Zip transcription factor Yap4 to the Lot6-proteasome complex, indicating that recruitment of the transcription factor depends on the redox state of the quinone reductase. Here, we show that binding of Yap4 to the complex not only protects it from ubiquitin-independent proteasomal degradation, but also regulates its cellular localization. In non-stressed wild-type cells, we did not detect any Yap4 in the nucleus, whereas Yap4 was present in the nuclei from quinone-stressed yeast cultures. Thus, the Lot6-proteasome complex can be regarded as a redox switch in which the quinone reductase acts as a sensor for oxidative stress.

Indexed as

FlavinsFMN ReductaseNAD(P)H Dehydrogenase (Quinone)Nuclear ProteinsOxidation-ReductionProteasome Endopeptidase ComplexProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsCin5 protein, S cerevisiaeFlavinsFMN ReductaseLOT6 protein, S cerevisiaeNAD(P)H Dehydrogenase (Quinone)Nuclear ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID19029946
PMCPMC2613204
OpenAlexW2132391006

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.