Evidence map›Paper›PMID 18592385›Full record

ArticleChromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology2008

In human pachytene spermatocytes, SUMO protein is restricted to the constitutive heterochromatin.

Catherine Metzler-Guillemain, Danielle Depetris, Judith J Luciani, Cecile Mignon-Ravix, Michael J Mitchell, Marie-Genevieve Mattei

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In one paragraph

Article in Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Review
  3. SIRT1: A Key Player in Male Reproduction.Life (Basel, Switzerland) · 2022
    Review
  4. Programmed DNA Elimination in Vertebrates.Annual review of animal biosciences · 2021
    Review
  5. The role of SUMOylation during development.Biochemical Society transactions · 2020
    Review
  6. Review
  7. Article
  8. Cross-talk between sumoylation and phosphorylation in mouse spermatocytes.Biochemical and biophysical research communications · 2017
    Article
  9. Article
  10. Wrestling with Chromosomes: The Roles of SUMO During Meiosis.Advances in experimental medicine and biology · 2017
    Review
  11. Article
  12. Review
  13. Review
  14. Emerging roles of the SUMO pathway in development.Cellular and molecular life sciences : CMLS · 2011
    Review
  15. Article
  16. 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

6 authors at 1 institution in 1 country.

Catherine Metzler-GuillemainINSERM U910, Faculté de Médecine, 27 Boulevard Jean Moulin, Marseille, France.
Danielle Depetris
Judith J Luciani
Cecile Mignon-Ravix
Michael J Mitchell
Marie-Genevieve Mattei
Inserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMO-1, a ubiquitin-like protein, is covalently bound to many proteins, leading to chromatin inactivation and transcriptional repression. The high concentration of SUMO-1 on the XY body in rodents suggests that this protein has an important role in facultative heterochromatin organization. In human, the precise role of SUMO in chromatin/heterochromatin organization remains to be defined. Here we describe the SUMO-1 distribution, during human male meiosis, in relation to the formation of the different types of heterochromatin. We show that, during late pachynema, SUMO-1 appears on the constitutive heterochromatin, but is excluded from the XY body facultative heterochromatin. At the SUMO-1 labelled areas, the presence of HP1alpha protein, as well as of trimethylated H3-K9 and H4-K20 histone modifications, supports a role for SUMO-1 in constitutive heterochromatin organization. We also establish that, on the constitutive heterochromatin, H4-K20me3 staining progressively decreases as SUMO-1 staining increases, suggesting that core histone(s), and histone H4 in particular, are direct targets for sumoylation. Our results also suggest that, in the context of global histone H4 hyperacetylation that precedes the histone-to-protamine transition at postmeiotic stages of spermatogenesis, histone H4 sumoylation may represent an important epigenetic marker replacing methylation on the constitutive heterochromatin.

Indexed as

Pachytene StageChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneChromosome PairingHeterochromatinHistonesHumansIn Situ Hybridization, FluorescenceMaleSpermatocytesSUMO-1 ProteinCBX5 protein, humanChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneHeterochromatinHistonesSUMO-1 Protein

Identifiers

PMID18592385
OpenAlexW2050735681

What OpenQuestion holds

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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.