Evidence map›Paper›PMID 26138980›Full record

ArticleScience (New York, N.Y.)2015

SELENOPROTEINS. CRL2 aids elimination of truncated selenoproteins produced by failed UGA/Sec decoding.

Hsiu-Chuan Lin, Szu-Chi Ho, Yi-Yun Chen, Kay-Hooi Khoo, Pang-Hung Hsu, Hsueh-Chi S Yen

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
  6. Article
  7. Review
  8. Selenoprotein K at the intersection of cellular pathways.Archives of biochemistry and biophysics · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Selenoprotein S: A versatile disordered protein.Archives of biochemistry and biophysics · 2022
    Review
  18. Article
  19. Article
  20. Review
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

6 authors at 2 institutions in 1 country.

Hsiu-Chuan LinInstitute of Molecular Biology, Academia Sinica, Taiwan. Genome and Systems Biology Degree Program, National Taiwan University, Taiwan.
Szu-Chi HoInstitute of Molecular Biology, Academia Sinica, Taiwan.
Yi-Yun ChenInstitute of Biological Chemistry, Academia Sinica, Taiwan.
Kay-Hooi KhooGenome and Systems Biology Degree Program, National Taiwan University, Taiwan. Institute of Biological Chemistry, Academia Sinica, Taiwan.
Pang-Hung HsuDepartment of Life Science, Institute of Bioscience and Biotechnology, National Taiwan Ocean University, Taiwan.
Hsueh-Chi S YenInstitute of Molecular Biology, Academia Sinica, Taiwan. Genome and Systems Biology Degree Program, National Taiwan University, Taiwan.
Institute of Molecular Biology, Academia Sinica · TWInstitute of Biological Chemistry, Academia Sinica · TW

Funding

Ubiquitin Mediated Proteolysis and Cell Cycle ControlR01AG011085 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JEFFREY W HARPER · 1993 to 2026
$10.9M
NIA NIH HHS AG011085NIA NIH HHS R01 AG011085
6 · The paper itself

Abstract

Selenocysteine (Sec) is translated from the codon UGA, typically a termination signal. Codon duality extends the genetic code; however, the coexistence of two competing UGA-decoding mechanisms immediately compromises proteome fidelity. Selenium availability tunes the reassignment of UGA to Sec. We report a CRL2 ubiquitin ligase-mediated protein quality-control system that specifically eliminates truncated proteins that result from reassignment failures. Exposing the peptide immediately N-terminal to Sec, a CRL2 recognition degron, promotes protein degradation. Sec incorporation destroys the degron, protecting read-through proteins from detection by CRL2. Our findings reveal a coupling between directed translation termination and proteolysis-assisted protein quality control, as well as a cellular strategy to cope with fluctuations in organismal selenium intake.

Indexed as

ProteolysisCodon, TerminatorHEK293 CellsHumansPeptide Chain Termination, TranslationalSeleniumSelenocysteineSelenoproteinsSKP Cullin F-Box Protein LigasesUbiquitinCodon, TerminatorSeleniumSelenocysteineSelenoproteinsSKP Cullin F-Box Protein LigasesUbiquitin

Identifiers

PMID26138980
PMCPMC4766860
OpenAlexW1919513821

What OpenQuestion holds

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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.