Evidence map›Paper›PMID 32200094›Full record

ArticleiScience2020

Cul5-type Ubiquitin Ligase KLHDC1 Contributes to the Elimination of Truncated SELENOS Produced by Failed UGA/Sec Decoding.

Fumihiko Okumura, Yuha Fujiki, Nodoka Oki, Kana Osaki, Akihiko Nishikimi, Yoshinori Fukui, Kunio Nakatsukasa, Takumi Kamura

Open access · goldAbstract read
In one paragraph

Article in iScience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Selenoprotein K at the intersection of cellular pathways.Archives of biochemistry and biophysics · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Molecules and cells · 2021
    Article
  14. 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

8 authors at 5 institutions in 1 country.

Fumihiko OkumuraDepartment of Food and Health Sciences, International College of Arts and Sciences, Fukuoka Women's University, Fukuoka 813-8582, Japan. Electronic address: okumura@fwu.ac.jp.
Yuha FujikiDepartment of Food and Health Sciences, International College of Arts and Sciences, Fukuoka Women's University, Fukuoka 813-8582, Japan.
Nodoka OkiDepartment of Food and Health Sciences, International College of Arts and Sciences, Fukuoka Women's University, Fukuoka 813-8582, Japan.
Kana OsakiDepartment of Food and Health Sciences, International College of Arts and Sciences, Fukuoka Women's University, Fukuoka 813-8582, Japan.
Akihiko NishikimiLaboratory of Biosafety Research, National Center for Geriatrics and Gerontology, Aichi 474-8511, Japan.
Yoshinori FukuiDivision of Immunogenetics, Department of Immunobiology and Neuroscience and Research Center for Advanced Immunology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.
Kunio NakatsukasaGraduate School of Natural Sciences, Nagoya City University, Aichi 467-8501, Japan.
Takumi KamuraDivision of Biological Science, Graduate School of Science, Nagoya University, Aichi 464-8602, Japan. Electronic address: z47617a@nucc.cc.nagoya-u.ac.jp.
Fukuoka Women's University · JPKyushu University · JPNagoya City University · JPNagoya University · JPNational Center for Geriatrics and Gerontology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The UGA codon signals protein translation termination, but it can also be translated into selenocysteine (Sec, U) to produce selenocysteine-containing proteins (selenoproteins) by dedicated machinery. As Sec incorporation can fail, Sec-containing longer and Sec-lacking shorter proteins co-exist. Cul2-type ubiquitin ligases were recently shown to destabilize such truncated proteins; however, which ubiquitin ligase targets truncated proteins for degradation remained unclear. We report that the Cul5-type ubiquitin ligase KLHDC1 targets truncated SELENOS, a selenoprotein, for proteasomal degradation. SELENOS is involved in endoplasmic reticulum (ER)-associated degradation, which is linked to reactive oxygen species (ROS) production, and the knockdown of KLHDC1 in U2OS cells decreased ER stress-induced cell death. Knockdown of SELENOS increased the cell population with lower ROS levels. Our findings reveal that, in addition to Cul2-type ubiquitin ligases, KLHDC1 is involved in the elimination of truncated oxidoreductase-inactive SELENOS, which would be crucial for maintaining ROS levels and preventing cancer development.

Indexed as

CancerCell BiologyMolecular Biology

Identifiers

PMID32200094
PMCPMC7090344
OpenAlexW3009425243

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.