Evidence map›Paper›PMID 20805487›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

The serine/arginine-rich protein SF2/ASF regulates protein sumoylation.

Federico Pelisch, Juan Gerez, Jimena Druker, Ignacio E Schor, Manuel J Muñoz, Guillermo Risso, Ezequiel Petrillo, Belinda J Westman, Angus I Lamond, Eduardo Arzt and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 67 citations in OpenAlex.

  1. SUMO conjugation to promoter-proximal sequence elements-associated proteins impacts on snRNA transcription.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. 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
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Regulation of SUMOylation on RNA metabolism in cancers.Frontiers in molecular biosciences · 2023
    Review
  9. Review
  10. Exploring the multifunctionality of SR proteins.Biochemical Society transactions · 2022
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. When SUMO met splicing.RNA biology · 2018
    Review
  17. 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

11 authors at 3 institutions in 2 countries.

Federico PelischLaboratorio de Fisiología, Biología Molecular, Instituto de Fisiología, Biología Molecular, Neurociencias, Consejo Nacional de Investigaciones Científicas y Técnicas, C1428EHA Buenos Aires, Argentina.
Juan Gerez
Jimena Druker
Ignacio E Schor
Manuel J Muñoz
Guillermo Risso
Ezequiel Petrillo
Belinda J Westman
Angus I Lamond
Eduardo Arzt
Anabella Srebrow
Fundación Ciencias Exactas y Naturales · ARUniversity of Buenos Aires · ARUniversity of Dundee · GB

Funding

Medical Research Council G0301131Wellcome Trust 073980
6 · The paper itself

Abstract

Protein modification by conjugation of small ubiquitin-related modifier (SUMO) is involved in diverse biological functions, such as transcription regulation, subcellular partitioning, stress response, DNA damage repair, and chromatin remodeling. Here, we show that the serine/arginine-rich protein SF2/ASF, a factor involved in splicing regulation and other RNA metabolism-related processes, is a regulator of the sumoylation pathway. The overexpression of this protein stimulates, but its knockdown inhibits SUMO conjugation. SF2/ASF interacts with Ubc9 and enhances sumoylation of specific substrates, sharing characteristics with already described SUMO E3 ligases. In addition, SF2/ASF interacts with the SUMO E3 ligase PIAS1 (protein inhibitor of activated STAT-1), regulating PIAS1-induced overall protein sumoylation. The RNA recognition motif 2 of SF2/ASF is necessary and sufficient for sumoylation enhancement. Moreover, SF2/ASF has a role in heat shock-induced sumoylation and promotes SUMO conjugation to RNA processing factors. These results add a component to the sumoylation pathway and a previously unexplored role for the multifunctional SR protein SF2/ASF.

Indexed as

Cell LineHeat-Shock ResponseHumansNuclear ProteinsProtein BindingRNA-Binding ProteinsRNA, Small InterferingSerine-Arginine Splicing FactorsSubstrate SpecificitySUMO-1 ProteinTumor Suppressor Protein p53Ubiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Nuclear ProteinsRNA-Binding ProteinsRNA, Small InterferingSerine-Arginine Splicing FactorsSUMO-1 ProteinTumor Suppressor Protein p53Ubiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9

Identifiers

PMID20805487
PMCPMC2941313
OpenAlexW2170520669

What OpenQuestion holds

Textmetadata
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.