Evidence map›Paper›PMID 12634850›Full record

ArticleEMBO reports2003

Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain.

Eri Sakata, Yoshiki Yamaguchi, Eiji Kurimoto, Jun Kikuchi, Shigeyuki Yokoyama, Shingo Yamada, Hiroyuki Kawahara, Hideyoshi Yokosawa, Nobutaka Hattori, Yoshikuni Mizuno and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

85 citing papers in PubMed, 247 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Ubiquitin-modifying enzymes in Huntington's disease.Frontiers in molecular biosciences · 2023
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. PINK1/Parkin Mediated Mitophagy, CaInternational journal of molecular sciences · 2020
    Review
  14. Proteins containing ubiquitin-like (Ubl) domains not only bind to 26S proteasomes but also induce their activation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. UBL domain of Usp14 and other proteins stimulates proteasome activities and protein degradation in cells.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. Article

25 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

12 authors at 7 institutions in 2 countries.

Eri SakataDepartment of Structural Biology and Biomolecular Engineering, Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan.
Yoshiki Yamaguchi
Eiji Kurimoto
Jun Kikuchi
Shigeyuki Yokoyama
Shingo Yamada
Hiroyuki Kawahara
Hideyoshi Yokosawa
Nobutaka Hattori
Yoshikuni Mizuno
Keiji Tanaka
Koichi Kato
Nagoya City University · JPHokkaido University · JPJuntendo University · JPCenter for Genomic Science · ITHokkaido Pharmaceutical University · JPTokyo Metropolitan Institute of Medical Science · JPTokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Parkin, a product of the causative gene of autosomal-recessive juvenile parkinsonism (AR-JP), is a RING-type E3 ubiquitin ligase and has an amino-terminal ubiquitin-like (Ubl) domain. Although a single mutation that causes an Arg to Pro substitution at position 42 of the Ubl domain (the Arg 42 mutation) has been identified in AR-JP patients, the function of this domain is not clear. In this study, we determined the three-dimensional structure of the Ubl domain of parkin by NMR, in particular by extensive use of backbone (15)N-(1)H residual dipolar-coupling data. Inspection of chemical-shift-perturbation data showed that the parkin Ubl domain binds the Rpn10 subunit of 26S proteasomes via the region of parkin that includes position 42. Our findings suggest that the Arg 42 mutation induces a conformational change in the Rpn10-binding site of Ubl, resulting in impaired proteasomal binding of parkin, which could be the cause of AR-JP.

Indexed as

Proteasome Endopeptidase ComplexUbiquitin-Protein LigasesAmino Acid SequenceAmino Acid SubstitutionBinding SitesCarrier ProteinsGenes, RecessiveHumansLigasesModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedParkinsonian DisordersPeptide HydrolasesProtein ConformationRNA-Binding ProteinsATP dependent 26S proteaseCarrier ProteinsLigasesparkin proteinPeptide HydrolasesProteasome Endopeptidase ComplexPSMD4 protein, humanRNA-Binding ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID12634850
PMCPMC1315892
OpenAlexW2097062199

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.