Evidence map›Paper›PMID 21157427›Full record

ArticleThe EMBO journal2011

Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin.

Valerie Edmond, Elodie Moysan, Saadi Khochbin, Patrick Matthias, Christian Brambilla, Elisabeth Brambilla, Sylvie Gazzeri, Beatrice Eymin

Registry-linked trialAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT02853006 (Study on Fluids Associated to Lung Cancer, of the Ectopic Expression of Cancer Testis Gene and Mutation as Diagnostics and Prognosis Biomarkers), which is not on this map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
3.5field-weighted citation impact, top 7% 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.

NCT02853006 nacompletednot on this mapstarted 2015, after this paper: background citation

Study on Fluids Associated to Lung Cancer, of the Ectopic Expression of Cancer Testis Gene and Mutation as Diagnostics and Prognosis Biomarkers

TypeinterventionalSponsorUniversity Hospital, GrenobleRan2015 to 2020Enrolled31ConditionsLung CancerArmsBlood and respiratory fluids sampling, Biopsy, Excised tissues
3 · Its place in the literature

Who cites it

80 citing papers in PubMed, 135 citations in OpenAlex.

  1. Article
  2. Non-Enzymatic MGO-Glycation of SRSF2 Drives RNA Mis-Splicing.Journal of the American Chemical Society · 2026
    Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. U1-70K and U1A and tau pathogenesis in demented and non-demented individuals with Down syndrome.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Article
  9. Article
  10. Article
  11. Tumor-promoting effect and tumor immunity of SRSFs.Frontiers in cell and developmental biology · 2025
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. RNA splicing: a dual-edged sword for hepatocellular carcinoma.Medical oncology (Northwood, London, England) · 2022
    Review
  20. Review

20 more citing papers are in PubMed but not listed here.

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

8 authors at 5 institutions in 2 countries.

Valerie EdmondINSERM, U823, Equipe 2 Bases Moléculaires de la Progression des Cancers du Poumon, Institut Albert Bonniot, Grenoble, France.
Elodie Moysan
Saadi Khochbin
Patrick Matthias
Christian Brambilla
Elisabeth Brambilla
Sylvie Gazzeri
Beatrice Eymin
Inserm · FRUniversité Joseph Fourier · FRBiotechnologie et Signalisation Cellulaire · FRFriedrich Miescher Institute · CHInstitut pour l'avancée des biosciences · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SRSF2 is a serine/arginine-rich protein belonging to the family of SR proteins that are crucial regulators of constitutive and alternative pre-mRNA splicing. Although it is well known that phosphorylation inside RS domain controls activity of SR proteins, other post-translational modifications regulating SRSF2 functions have not been described to date. In this study, we provide the first evidence that the acetyltransferase Tip60 acetylates SRSF2 on its lysine 52 residue inside the RNA recognition motif, and promotes its proteasomal degradation. We also demonstrate that the deacetylase HDAC6 counters this acetylation and acts as a positive regulator of SRSF2 protein level. In addition, we show that Tip60 downregulates SRSF2 phosphorylation by inhibiting the nuclear translocation of both SRPK1 and SRPK2 kinases. Finally, we demonstrate that this acetylation/phosphorylation signalling network controls SRSF2 accumulation as well as caspase-8 pre-mRNA splicing in response to cisplatin and determines whether cells undergo apoptosis or G(2)/M cell cycle arrest. Taken together, these results unravel lysine acetylation as a crucial post-translational modification regulating SRSF2 protein level and activity in response to genotoxic stress.

Indexed as

AcetylationAlternative SplicingBlotting, WesternCaspase 8Cell CycleCell DifferentiationCell Line, TumorCisplatinDNA PrimersHistone AcetyltransferasesHistone Deacetylase 6Histone DeacetylasesHumansImmunoprecipitationLysineLysine Acetyltransferase 5Caspase 8CisplatinDNA PrimersHDAC6 protein, humanHistone AcetyltransferasesHistone Deacetylase 6Histone DeacetylasesKAT5 protein, humanLysineLysine Acetyltransferase 5Nuclear ProteinsOligonucleotidesRibonucleoproteinsRNA, Small InterferingSerine-Arginine Splicing FactorsSRSF2 protein, human

Identifiers

PMID21157427
PMCPMC3034009
OpenAlexW1802578251

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.