Evidence map›Paper›PMID 34131137›Full record

ArticleNature communications2021

TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation.

Klára Klimešová, Jitka Vojáčková, Nenad Radivojević, Franck Vandermoere, Edouard Bertrand, Celine Verheggen, David Staněk

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-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

21 citing papers in PubMed, 25 citations in OpenAlex.

  1. Detection and sequencing of ApProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. AProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Addressing the tissue specificity of U5 snRNP spliceosomopathies.Frontiers in cell and developmental biology · 2025
    Article
  8. Article
  9. Structural basis of human U5 snRNP late biogenesis and recycling.Nature structural & molecular biology · 2024
    Article
  10. Structure of the human 20S U5 snRNP.Nature structural & molecular biology · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Coilin and Cajal bodies.Nucleus (Austin, Tex.) · 2023
    Review
  15. Review
  16. Article
  17. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. 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

7 authors at 2 institutions in 3 countries.

Klára Klimešová *Institute of Molecular Genetics, Czech Academy of Sciences, Prague, Czech Republic.ORCID 0000-0001-5828-3363
Jitka Vojáčková *Institute of Molecular Genetics, Czech Academy of Sciences, Prague, Czech Republic.ORCID 0000-0002-8263-6277
Nenad RadivojevićInstitute of Molecular Genetics, Czech Academy of Sciences, Prague, Czech Republic.ORCID 0000-0001-9484-9002
Franck VandermoereInstitut de Génomique Fonctionnelle, University of Montpellier, CNRS, INSERM, Montpellier, France.ORCID 0000-0001-5724-7037
Edouard BertrandInstitut de Génétique Moléculaire de Montpellier, University of Montpellier, CNRS, Montpellier, France.ORCID 0000-0002-9642-7994
Celine VerheggenInstitut de Génétique Moléculaire de Montpellier, University of Montpellier, CNRS, Montpellier, France.ORCID 0000-0003-2459-9700
David StaněkInstitute of Molecular Genetics, Czech Academy of Sciences, Prague, Czech Republic. stanek@img.cas.cz.ORCID 0000-0002-5865-175X
Czech Academy of Sciences · CZCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

U5 snRNP is a complex particle essential for RNA splicing. U5 snRNPs undergo intricate biogenesis that ensures that only a fully mature particle assembles into a splicing competent U4/U6•U5 tri-snRNP and enters the splicing reaction. During splicing, U5 snRNP is substantially rearranged and leaves as a U5/PRPF19 post-splicing particle, which requires re-generation before the next round of splicing. Here, we show that a previously uncharacterized protein TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation. We provide evidence that TSSC4 associates with U5 snRNP chaperones, U5 snRNP and the U5/PRPF19 particle. Specifically, TSSC4 interacts with U5-specific proteins PRPF8, EFTUD2 and SNRNP200. We also identified TSSC4 domains critical for the interaction with U5 snRNP and the PRPF19 complex, as well as for TSSC4 function in tri-snRNP assembly. TSSC4 emerges as a specific chaperone that acts in U5 snRNP de novo biogenesis as well as post-splicing recycling.

Indexed as

DNA Repair EnzymesDown-RegulationHeLa CellsHumansNuclear ProteinsPeptide Elongation FactorsProtein DomainsProtein Interaction Domains and MotifsRecombinant Fusion ProteinsRibonucleoproteins, Small NuclearRibonucleoprotein, U5 Small NuclearRNA-Binding ProteinsRNA SplicingRNA Splicing FactorsSpliceosomesTranscription FactorsDNA Repair EnzymesEFTUD2 protein, humanNuclear ProteinsPeptide Elongation FactorsPRPF19 protein, humanPRPF6 protein, humanPRPF8 protein, humanRecombinant Fusion ProteinsRibonucleoproteins, Small NuclearRibonucleoprotein, U5 Small NuclearRNA-Binding ProteinsRNA Splicing FactorsSNRNP200 protein, humanTranscription FactorsTSSC4 protein, humanTumor Suppressor Proteins

Identifiers

PMID34131137
PMCPMC8206348
OpenAlexW3166626292

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.