Evidence map›Paper›PMID 26420826›Full record

ArticleNucleic acids research2015

Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins.

Angela Crisci, Flore Raleff, Ivona Bagdiul, Monika Raabe, Henning Urlaub, Jean-Christophe Rain, Angela Krämer

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

35 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Sustainable integrative cell biology: CENP-C is guilty by association.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Journal of Cancer · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. DHX15 is involved in SUGP1-mediated RNA missplicing by mutant SF3B1 in cancer.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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 4 institutions in 3 countries.

Angela CrisciDepartment of Cell Biology, Faculty of Sciences, University of Geneva, CH-1211 Geneva 4, Switzerland.
Flore RaleffDepartment of Cell Biology, Faculty of Sciences, University of Geneva, CH-1211 Geneva 4, Switzerland.
Ivona BagdiulDepartment of Cell Biology, Faculty of Sciences, University of Geneva, CH-1211 Geneva 4, Switzerland.
Monika RaabeBioanalytical Mass Spectrometry, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.
Henning UrlaubBioanalytical Mass Spectrometry, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany Bioanalytics, Institute for Clinical Chemistry, University Medical Center Göttingen, D-37075 Göttingen, Germany.
Jean-Christophe RainHybrigenics Services, F-75014 Paris, France.
Angela KrämerDepartment of Cell Biology, Faculty of Sciences, University of Geneva, CH-1211 Geneva 4, Switzerland angela.kraemer@unige.ch.
University of Geneva · CHHybrigenics (France) · FRMax Planck Institute for Biophysical Chemistry · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Splicing factor 1 (SF1) recognizes the branch point sequence (BPS) at the 3' splice site during the formation of early complex E, thereby pre-bulging the BPS adenosine, thought to facilitate subsequent base-pairing of the U2 snRNA with the BPS. The 65-kDa subunit of U2 snRNP auxiliary factor (U2AF65) interacts with SF1 and was shown to recruit the U2 snRNP to the spliceosome. Co-immunoprecipitation experiments of SF1-interacting proteins from HeLa cell extracts shown here are consistent with the presence of SF1 in early splicing complexes. Surprisingly almost all U2 snRNP proteins were found associated with SF1. Yeast two-hybrid screens identified two SURP domain-containing U2 snRNP proteins as partners of SF1. A short, evolutionarily conserved region of SF1 interacts with the SURP domains, stressing their role in protein-protein interactions. A reduction of A complex formation in SF1-depleted extracts could be rescued with recombinant SF1 containing the SURP-interaction domain, but only partial rescue was observed with SF1 lacking this sequence. Thus, SF1 can initially recruit the U2 snRNP to the spliceosome during E complex formation, whereas U2AF65 may stabilize the association of the U2 snRNP with the spliceosome at later times. In addition, these findings may have implications for alternative splicing decisions.

Indexed as

DNA-Binding ProteinsHeLa CellsHumansMembrane ProteinsNuclear ProteinsProtein BindingProtein Interaction Domains and MotifsRibonucleoproteinsRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA Splicing FactorsSpliceosomesSplicing Factor U2AFTranscription FactorsCHERP protein, humanDNA-Binding ProteinsMembrane ProteinsNuclear ProteinsRibonucleoproteinsRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA Splicing FactorsSF1 protein, humanSFSWAP protein, humansplicing factor 3aSplicing Factor U2AFTranscription FactorsU2AF2 protein, human

Identifiers

PMID26420826
PMCPMC4666396
OpenAlexW1660832822

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.