Evidence map›Paper›PMID 25013170›Full record

ArticleNucleic acids research2014

Hypermethylated-capped selenoprotein mRNAs in mammals.

Laurence Wurth, Anne-Sophie Gribling-Burrer, Céline Verheggen, Michael Leichter, Akiko Takeuchi, Stéphanie Baudrey, Franck Martin, Alain Krol, Edouard Bertrand, Christine Allmang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

36 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Global analysis by LC-MS/MS ofRNA (New York, N.Y.) · 2025
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Application of Mammalian Nudix Enzymes to Capped RNA Analysis.Pharmaceuticals (Basel, Switzerland) · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023
    Review
  13. PIMT Controls Insulin Synthesis and Secretion through PDX1.International journal of molecular sciences · 2023
    Article
  14. Review
  15. Article
  16. Review
  17. HIV-1 hypermethylated guanosine cap licenses specialized translation unaffected by mTOR.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Ribosome Fate during Decoding of UGA-Sec Codons.International journal of molecular sciences · 2021
    Review
  19. A Trimethylguanosine Synthase1-like (TGS1) homologue is implicated in vernalisation and flowering time control.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021
    Article
  20. Article
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

10 authors at 4 institutions in 1 country.

Laurence WurthArchitecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France.
Anne-Sophie Gribling-BurrerArchitecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France.
Céline VerheggenEquipe labélisée Ligue contre le cancer, Institut de Génétique Moléculaire, Centre National de la Recherche Scientifique, UMR 5535, 34293 Montpellier, France.
Michael LeichterArchitecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France.
Akiko TakeuchiArchitecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France.
Stéphanie BaudreyArchitecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France.
Franck MartinArchitecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France.
Alain KrolArchitecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France.
Edouard BertrandEquipe labélisée Ligue contre le cancer, Institut de Génétique Moléculaire, Centre National de la Recherche Scientifique, UMR 5535, 34293 Montpellier, France.
Christine AllmangArchitecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France c.allmang@unistra.fr.
Institut de Biologie Moléculaire et Cellulaire · FRArchitecture et Réactivité de l'arN · FRLa Ligue Contre le Cancer · FRUniversité de Strasbourg · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian mRNAs are generated by complex and coordinated biogenesis pathways and acquire 5'-end m(7)G caps that play fundamental roles in processing and translation. Here we show that several selenoprotein mRNAs are not recognized efficiently by translation initiation factor eIF4E because they bear a hypermethylated cap. This cap modification is acquired via a 5'-end maturation pathway similar to that of the small nucle(ol)ar RNAs (sn- and snoRNAs). Our findings also establish that the trimethylguanosine synthase 1 (Tgs1) interacts with selenoprotein mRNAs for cap hypermethylation and that assembly chaperones and core proteins devoted to sn- and snoRNP maturation contribute to recruiting Tgs1 to selenoprotein mRNPs. We further demonstrate that the hypermethylated-capped selenoprotein mRNAs localize to the cytoplasm, are associated with polysomes and thus translated. Moreover, we found that the activity of Tgs1, but not of eIF4E, is required for the synthesis of the GPx1 selenoprotein in vivo.

Indexed as

Cell LineEukaryotic Initiation Factor-4EGlutathione PeroxidaseGlutathione Peroxidase GPX1HumansMethylationMethyltransferasesNuclear ProteinsPolyribosomesProtein BiosynthesisRibonucleoproteins, Small NucleolarRNA-Binding ProteinsRNA CapsRNA, MessengerSelenoproteinsSMN Complex ProteinsEukaryotic Initiation Factor-4EGlutathione PeroxidaseGlutathione Peroxidase GPX1GPX1 protein, humanMethyltransferasesNOP58 protein, humanNuclear ProteinsRibonucleoproteins, Small NucleolarRNA-Binding ProteinsRNA CapsRNA, MessengerSECISBP2 protein, humanSelenoproteinsSMN Complex Proteinstrimethylguanosine synthase

Identifiers

PMID25013170
PMCPMC4117793
OpenAlexW2130565528

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.