Evidence map›Paper›PMID 29694890›Full record

ArticleCell reports2018

Infection Reveals a Modification of SIRT2 Critical for Chromatin Association.

Jorge M Pereira, Christine Chevalier, Thibault Chaze, Quentin Gianetto, Francis Impens, Mariette Matondo, Pascale Cossart, Mélanie A Hamon

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. The Sirtuin Network: Linking NADDiabetes/metabolism research and reviews · 2026
    Review
  3. PPM1B utilizes a trinuclear metal architecture for phosphatase activity.bioRxiv : the preprint server for biology · 2026
    Article
  4. Potential 14-3-3 binding sites in sirtuins reveal extended phosphosite-recognition modes.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  5. Review
  6. Article
  7. ThemBio · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. A secreted sirtuin fromScience advances · 2023
    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

8 authors at 2 institutions in 2 countries.

Jorge M PereiraInstitut Pasteur, Unité des Interactions Bactéries-Cellules, Paris, France; Institut National de la Santé et de la Recherche Médicale, U604, Paris, France; Institut National de la Recherche Agronomique, USC2020, Paris, France; Institut Pasteur, Chromatine et Infection G5, Paris, France.
Christine ChevalierInstitut Pasteur, Chromatine et Infection G5, Paris, France.
Thibault ChazeInstitut Pasteur, Unité de Spectrométrie de Masse Structurale et Protéomique, Paris, France.
Quentin GianettoInstitut Pasteur, Unité de Spectrométrie de Masse Structurale et Protéomique, Paris, France.
Francis ImpensInstitut Pasteur, Unité des Interactions Bactéries-Cellules, Paris, France; Institut National de la Santé et de la Recherche Médicale, U604, Paris, France; Institut National de la Recherche Agronomique, USC2020, Paris, France; Center for Medical Biotechnology, VIB, Ghent University, 9000 Ghent, Belgium.
Mariette MatondoInstitut Pasteur, Unité de Spectrométrie de Masse Structurale et Protéomique, Paris, France.
Pascale CossartInstitut Pasteur, Unité des Interactions Bactéries-Cellules, Paris, France; Institut National de la Santé et de la Recherche Médicale, U604, Paris, France; Institut National de la Recherche Agronomique, USC2020, Paris, France. Electronic address: pascale.cossart@pasteur.fr.
Mélanie A HamonInstitut Pasteur, Chromatine et Infection G5, Paris, France. Electronic address: melanie.hamon@pasteur.fr.
Institut Pasteur · FRInserm · FR

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Sirtuin 2 is a nicotinamide-adenine-dinucleotide-dependent deacetylase that regulates cell processes such as carcinogenesis, cell cycle, DNA damage, and infection. Subcellular localization of SIRT2 is crucial for its function but is poorly understood. Infection with the bacterial pathogen Listeria monocytogenes, which relocalizes SIRT2 from the cytoplasm to the chromatin, provides an ideal stimulus for the molecular study of this process. In this report, we provide a map of SIRT2 post-translational modification sites and focus on serine 25 phosphorylation. We show that infection specifically induces dephosphorylation of S25, an event essential for SIRT2 chromatin association. Furthermore, we identify a nuclear complex formed by the phosphatases PPM1A and PPM1B, with SIRT2 essential for controlling H3K18 deacetylation and SIRT2-mediated gene repression during infection and necessary for a productive Listeria infection. This study reveals a molecular mechanism regulating SIRT2 function and localization, paving the way for understanding other SIRT2-regulated cellular processes.

Indexed as

Listeria monocytogenesAnimalsChromatinHeLa CellsHumansListeriosisMiceMice, KnockoutPhosphorylationProtein Phosphatase 2CProtein Processing, Post-TranslationalSirtuin 2ChromatinPPM1A protein, humanPpm1a protein, mousePPM1B protein, humanPpm1b protein, mouseProtein Phosphatase 2CSIRT2 protein, humanSirt2 protein, mouseSirtuin 2chromatinH3K18histone acetylationinfectionListeria monocytogenesphosphorylationPPM1sirtuinsubcellular localization

Identifiers

PMID29694890
PMCPMC5946459
OpenAlexW2802630688

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.