Evidence map›Paper›PMID 15660529›Full record

ArticleThe Biochemical journal2005

Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome.

Marlies Löscher, Klaus Fortschegger, Gustav Ritter, Martina Wostry, Regina Voglauer, Johannes A Schmid, Steven Watters, A Jennifer Rivett, Paul Ajuh, Angus I Lamond and 2 more

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

33 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. SNEVStem cell reports · 2017
    Article
  9. Review
  10. Article
  11. Ubiquitous overexpression of the DNA repair factorNPJ aging and mechanisms of disease · 2017
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
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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

12 authors at 2 institutions in 1 country.

Marlies LöscherInstitute of Applied Microbiology, University of Natural Resources and Applied Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Klaus Fortschegger
Gustav Ritter
Martina Wostry
Regina Voglauer
Johannes A Schmid
Steven Watters
A Jennifer Rivett
Paul Ajuh
Angus I Lamond
Hermann Katinger
Johannes Grillari
BOKU University · ATUniversity of Vienna · AT

Funding

Wellcome Trust 073980
6 · The paper itself

Abstract

Recognition of specific substrates for degradation by the ubiquitin-proteasome pathway is ensured by a cascade of ubiquitin transferases E1, E2 and E3. The mechanism by which the target proteins are transported to the proteasome is not clear, but two yeast E3s and one mammalian E3 ligase seem to be involved in the delivery of targets to the proteasome, by escorting them and by binding to the 19 S regulatory particle of the proteasome. In the present study, we show that SNEV (senescence evasion factor), a protein with in vitro E3 ligase activity, which is also involved in DNA repair and splicing, associates with the proteasome by directly binding to the beta7 subunit of the 20 S proteasome. Upon inhibition of proteasome activity, SNEV does not accumulate within the cells although its co-localization with the proteasome increases significantly. Since immunofluorescence microscopy also shows increased co-localization of SNEV with ubiquitin after proteasome inhibition, without SNEV being ubiquitinated by itself, we suggest that SNEV shows E3 ligase activity not only in vitro but also in vivo and escorts its substrate to the proteasome. Since the yeast homologue of SNEV, Prp19, also interacts with the yeast beta7 subunit of the proteasome, this mechanism seems to be conserved during evolution. Therefore these results support the hypothesis that E3 ligases might generally be involved in substrate transport to the proteasome. Additionally, our results provide the first evidence for a physical link between components of the ubiquitin-proteasome system and the spliceosome.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCaenorhabditis elegansCarrier ProteinsCell LineConserved SequenceCysteine EndopeptidasesDNA Repair EnzymesEvolution, MolecularHumansMolecular Sequence DataNuclear ProteinsProteasome Endopeptidase ComplexProtein BindingProtein ConformationCarrier ProteinsCysteine EndopeptidasesDNA Repair EnzymesNuclear ProteinsProteasome Endopeptidase ComplexPRPF19 protein, humanPSMB4 protein, humanRNA Splicing FactorsUbiquitin-Protein Ligases

Identifiers

PMID15660529
PMCPMC1138967
OpenAlexW2165114978

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.