Evidence map›Paper›PMID 30150655›Full record

ArticleScientific reports2018

The splicing factor SRSF3 is functionally connected to the nuclear RNA exosome for intronless mRNA decay.

Fabrice Mure, Antoine Corbin, Nour El Houda Benbahouche, Edouard Bertrand, Evelyne Manet, Henri Gruffat

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
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  7. Targeting RNA splicing modulation: new perspectives for anticancer strategy?Journal of experimental & clinical cancer research : CR · 2025
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Oncogenic SRSF3 in health and diseases.International journal of biological sciences · 2023
    Review
  16. Article
  17. Exploring the multifunctionality of SR proteins.Biochemical Society transactions · 2022
    Article
  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 3 institutions in 1 country.

Fabrice MureCIRI, Centre International de Recherche en Infectiologie, (Oncogenic Herpesviruses Team), Univ Lyon; Inserm, U1111, Université Claude Bernard Lyon 1; CNRS, UMR5308; ENS de Lyon, F-69007, Lyon, France.
Antoine CorbinCIRI, Centre International de Recherche en Infectiologie, (Oncogenic Herpesviruses Team), Univ Lyon; Inserm, U1111, Université Claude Bernard Lyon 1; CNRS, UMR5308; ENS de Lyon, F-69007, Lyon, France.
Nour El Houda BenbahoucheEquipe labellisée Ligue contre le Cancer, Institut de Génétique Moléculaire de Montpellier (IGMM), Université de Montpellier; CNRS, UMR5535, F-34293, Montpellier, France.
Edouard BertrandEquipe labellisée Ligue contre le Cancer, Institut de Génétique Moléculaire de Montpellier (IGMM), Université de Montpellier; CNRS, UMR5535, F-34293, Montpellier, France.
Evelyne ManetCIRI, Centre International de Recherche en Infectiologie, (Oncogenic Herpesviruses Team), Univ Lyon; Inserm, U1111, Université Claude Bernard Lyon 1; CNRS, UMR5308; ENS de Lyon, F-69007, Lyon, France.
Henri GruffatCIRI, Centre International de Recherche en Infectiologie, (Oncogenic Herpesviruses Team), Univ Lyon; Inserm, U1111, Université Claude Bernard Lyon 1; CNRS, UMR5308; ENS de Lyon, F-69007, Lyon, France. henri.gruffat@ens-lyon.fr.
École Normale Supérieure de Lyon · FRCentre National de la Recherche Scientifique · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RNA exosome fulfills important functions in the processing and degradation of numerous RNAs species. However, the mechanisms of recruitment to its various nuclear substrates are poorly understood. Using Epstein-Barr virus mRNAs as a model, we have discovered a novel function for the splicing factor SRSF3 in the quality control of nuclear mRNAs. We have found that viral mRNAs generated from intronless genes are particularly unstable due to their degradation by the nuclear RNA exosome. This effect is counteracted by the viral RNA-binding protein EB2 which stabilizes these mRNAs in the nucleus and stimulates both their export to the cytoplasm and their translation. In the absence of EB2, SRSF3 participates in the destabilization of these viral RNAs by interacting with both the RNA exosome and its adaptor complex NEXT. Taken together, our results provide direct evidence for a connection between the splicing machinery and mRNA decay mediated by the RNA exosome. Our results suggest that SRSF3 aids the nuclear RNA exosome and the NEXT complex in the recognition and degradation of certain mRNAs.

Indexed as

Blotting, WesternCell NucleusExosomesHeLa CellsHumansImmunoprecipitationRNA-Binding ProteinsRNA, MessengerRNA SplicingRNA StabilitySerine-Arginine Splicing FactorsRNA-Binding ProteinsRNA, MessengerSerine-Arginine Splicing FactorsSRSF3 protein, human

Identifiers

PMID30150655
PMCPMC6110769
OpenAlexW2888005468

What OpenQuestion holds

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LicenceCC BY
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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.