Evidence map›Paper›PMID 32152320›Full record

ArticleNature communications2020

Histone variant H3.3 residue S31 is essential for Xenopus gastrulation regardless of the deposition pathway.

David Sitbon, Ekaterina Boyarchuk, Florent Dingli, Damarys Loew, Geneviève Almouzni

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  11. Dinochromosome Heterotermini with Telosomal Anchorages.International journal of molecular sciences · 2024
    Article
  12. Review
  13. Review
  14. Article
  15. Reduced histone gene copy number disruptsbioRxiv : the preprint server for biology · 2023
    Article
  16. Article
  17. Article
  18. Epigenomic dynamics of early Xenopus Embryos.Development, growth & differentiation · 2022
    Review
  19. Review
  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

5 authors at 2 institutions in 1 country.

David Sitbon *Institut Curie, PSL Research University, CNRS, Sorbonne Université, Nuclear Dynamics Unit, Equipe Labellisée Ligue contre le Cancer, 26 rue d'Ulm, 75005, Paris, France.ORCID http://orcid.org/0000-0002-4131-8520
Ekaterina Boyarchuk *Institut Curie, PSL Research University, CNRS, Sorbonne Université, Nuclear Dynamics Unit, Equipe Labellisée Ligue contre le Cancer, 26 rue d'Ulm, 75005, Paris, France.ORCID http://orcid.org/0000-0002-7691-6547
Florent DingliInstitut Curie, PSL Research University, Centre de Recherche, Mass Spectrometry and Proteomics Facility (LSMP), 26 rue d'Ulm, Paris, 75248, Cedex 05, France.ORCID http://orcid.org/0000-0002-7715-2446
Damarys LoewInstitut Curie, PSL Research University, Centre de Recherche, Mass Spectrometry and Proteomics Facility (LSMP), 26 rue d'Ulm, Paris, 75248, Cedex 05, France.ORCID http://orcid.org/0000-0002-9111-8842
Geneviève AlmouzniInstitut Curie, PSL Research University, CNRS, Sorbonne Université, Nuclear Dynamics Unit, Equipe Labellisée Ligue contre le Cancer, 26 rue d'Ulm, 75005, Paris, France. genevieve.almouzni@curie.fr.ORCID http://orcid.org/0000-0001-5570-0723
Centre National de la Recherche Scientifique · FRUniversité Paris Sciences et Lettres · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vertebrates exhibit specific requirements for replicative H3 and non-replicative H3.3 variants during development. To disentangle whether this involves distinct modes of deposition or unique functions once incorporated into chromatin, we combined studies in Xenopus early development with chromatin assays. Here we investigate the extent to which H3.3 mutated at residues that differ from H3.2 rescue developmental defects caused by H3.3 depletion. Regardless of the deposition pathway, only variants at residue 31-a serine that can become phosphorylated-failed to rescue endogenous H3.3 depletion. Although an alanine substitution fails to rescue H3.3 depletion, a phospho-mimic aspartate residue at position 31 rescues H3.3 function. To explore mechanisms involving H3.3 S31 phosphorylation, we identified factors attracted or repulsed by the presence of aspartate at position 31, along with modifications on neighboring residues. We propose that serine 31-phosphorylated H3.3 acts as a signaling module that stimulates the acetylation of K27, providing a chromatin state permissive to the embryonic development program.

Indexed as

Amino Acid SequenceAnimalsChromatinGastrulationHistonesPhosphorylationSequence Analysis, ProteinSerineXenopus laevisChromatinHistonesSerine

Identifiers

PMID32152320
PMCPMC7062693
OpenAlexW3010477184

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.