Evidence map›Paper›PMID 34779515›Full record

ArticleThe EMBO journal2022

Exon-independent recruitment of SRSF1 is mediated by U1 snRNP stem-loop 3.

Andrew M Jobbins, Sébastien Campagne, Robert Weinmeister, Christian M Lucas, Alison R Gosliga, Antoine Clery, Li Chen, Lucy P Eperon, Mark J Hodson, Andrew J Hudson and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 39 citations in OpenAlex.

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  10. Tumor-promoting effect and tumor immunity of SRSFs.Frontiers in cell and developmental biology · 2025
    Review
  11. Article
  12. Review
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  16. SRSF1 interactome determined by proximity labeling reveals direct interaction with spliceosomal RNA helicase DDX23.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
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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

12 authors at 2 institutions in 2 countries.

Andrew M JobbinsLeicester Institute of Structural & Chemical Biology and Department of Molecular & Cell Biology, University of Leicester, Leicester, UK.ORCID 0000-0002-9174-1503
Sébastien CampagneInstitute of Biochemistry, ETH Zürich, Switzerland.ORCID 0000-0002-0094-4760
Robert WeinmeisterLeicester Institute of Structural & Chemical Biology and Department of Molecular & Cell Biology, University of Leicester, Leicester, UK.
Christian M LucasLeicester Institute of Structural & Chemical Biology and Department of Molecular & Cell Biology, University of Leicester, Leicester, UK.
Alison R GosligaLeicester Institute of Structural & Chemical Biology and Department of Molecular & Cell Biology, University of Leicester, Leicester, UK.
Antoine CleryInstitute of Biochemistry, ETH Zürich, Switzerland.
Li ChenLeicester Institute of Structural & Chemical Biology and Department of Molecular & Cell Biology, University of Leicester, Leicester, UK.
Lucy P EperonLeicester Institute of Structural & Chemical Biology and Department of Molecular & Cell Biology, University of Leicester, Leicester, UK.
Mark J HodsonLeicester Institute of Structural & Chemical Biology and Department of Molecular & Cell Biology, University of Leicester, Leicester, UK.
Andrew J HudsonLeicester Institute of Structural & Chemical Biology and Department of Chemistry, University of Leicester, Leicester, UK.
Frédéric H T AllainInstitute of Biochemistry, ETH Zürich, Switzerland.ORCID 0000-0002-2131-6237
Ian C EperonLeicester Institute of Structural & Chemical Biology and Department of Molecular & Cell Biology, University of Leicester, Leicester, UK.ORCID 0000-0002-4903-1911
University of Leicester · GBETH Zurich · CH

Funding

Biotechnology and Biological Sciences Research Council BB/T000627/1
6 · The paper itself

Abstract

SRSF1 protein and U1 snRNPs are closely connected splicing factors. They both stimulate exon inclusion, SRSF1 by binding to exonic splicing enhancer sequences (ESEs) and U1 snRNPs by binding to the downstream 5' splice site (SS), and both factors affect 5' SS selection. The binding of U1 snRNPs initiates spliceosome assembly, but SR proteins such as SRSF1 can in some cases substitute for it. The mechanistic basis of this relationship is poorly understood. We show here by single-molecule methods that a single molecule of SRSF1 can be recruited by a U1 snRNP. This reaction is independent of exon sequences and separate from the U1-independent process of binding to an ESE. Structural analysis and cross-linking data show that SRSF1 contacts U1 snRNA stem-loop 3, which is required for splicing. We suggest that the recruitment of SRSF1 to a U1 snRNP at a 5'SS is the basis for exon definition by U1 snRNP and might be one of the principal functions of U1 snRNPs in the core reactions of splicing in mammals.

Indexed as

Nucleic Acid ConformationExonsHeLa CellsHumansModels, BiologicalProtein BindingRibonucleoprotein, U1 Small NuclearRNA PrecursorsRNA, Small NuclearRNA Splice SitesSerine-Arginine Splicing FactorsRibonucleoprotein, U1 Small NuclearRNA PrecursorsRNA, Small NuclearRNA Splice SitesSerine-Arginine Splicing FactorsSRSF1 protein, humanU1 small nuclear RNAexon definitionRNA-protein interactionRNA splicingSRSF1U1 snRNP

Identifiers

PMID34779515
PMCPMC8724738
OpenAlexW3214218534

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.