Evidence map›Paper›PMID 17170706›Full record

ArticleThe EMBO journal2007

Proteasome substrate degradation requires association plus extended peptide.

Junko Takeuchi, Hui Chen, Philip Coffino

Abstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
–field-weighted citation impact
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

76 citing papers in PubMed.

  1. Proteasomal surveillance of exposed cysteines.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Ubiquitin-Independent Degradation: An Emerging PROTAC Approach?BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Ubiquitin modulates 26Science advances · 2022
    Article
  13. Article
  14. Article
  15. Mechanisms of substrate recognition by the 26S proteasome.Current opinion in structural biology · 2021
    Review
  16. Review
  17. Review
  18. Article
  19. Substrate selection by the proteasome through initiation regions.Protein science : a publication of the Protein Society · 2019
    Review
  20. Article

16 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

3 authors.

Junko TakeuchiDepartment of Microbiology and Immunology, University of California, San Francisco, CA 94143, USA.
Hui Chen
Philip Coffino

Funding

Ubiquitin-Independent Proteasome DegradationR01GM045335 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COFFINO, PHILIP · 1991 to 2012
$4.5M
Energy production and utilization in the proteasomeR01GM074760 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COFFINO, PHILIP · 2005 to 2008
$953k
NIGMS NIH HHS GM074760NIGMS NIH HHS GM45335NIGMS NIH HHS R01 GM045335NIGMS NIH HHS R01 GM074760
6 · The paper itself

Abstract

To determine the minimum requirements for substrate recognition and processing by proteasomes, the functional elements of a ubiquitin-independent degradation tag were dissected. The 37-residue C-terminus of ornithine decarboxylase (cODC) is a native degron, which also functions when appended to diverse proteins. Mutating the cysteine 441 residue within cODC impaired its proteasome association in the context of ornithine decarboxylase and prevented the turnover of GFP-cODC in yeast cells. Degradation of GFP-cODC with C441 mutations was restored by providing an alternate proteasome association element via fusion to the Rpn10 proteasome subunit. However, Rpn10-GFP was stable, unless extended by cODC or other peptides of similar size. In vitro reconstitution experiments confirmed the requirement for both proteasome tethering and a loosely structured region. Therefore, cODC and degradation tags in general must serve two functions: proteasome association and a site, consisting of an extended peptide region, used for initiating insertion into the protease.

Indexed as

AnimalsBinding, CompetitiveCarrier ProteinsDose-Response Relationship, DrugGreen Fluorescent ProteinsOrnithine DecarboxylasePeptidesPlasmidsProteasome Endopeptidase ComplexProtein FoldingProtein Structure, TertiaryRatsRecombinant ProteinsSaccharomyces cerevisiae ProteinsUbiquitinATP dependent 26S proteaseCarrier ProteinsGreen Fluorescent ProteinsOrnithine DecarboxylasePeptidesProteasome Endopeptidase ComplexRecombinant ProteinsRPN10 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin

Identifiers

PMID17170706
PMCPMC1782366

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.