Evidence map›Paper›PMID 32285610›Full record

ArticleEMBO reports2020

PDS5 proteins regulate the length of axial elements and telomere integrity during male mouse meiosis.

Alberto Viera, Inés Berenguer, Miguel Ruiz-Torres, Rocío Gómez, Andrea Guajardo, José Luis Barbero, Ana Losada, José A Suja

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. The ubiquitin-proteasome system regulates meiotic chromosome organization.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Chromosome architecture and homologous recombination in meiosis.Frontiers in cell and developmental biology · 2022
    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 3 institutions in 1 country.

Alberto VieraUnidad de Biología Celular, Departamento de Biología, Facultad de Ciencias, Universidad Autónoma de Madrid, Madrid, Spain.ORCID 0000-0002-3602-4130
Inés BerenguerUnidad de Biología Celular, Departamento de Biología, Facultad de Ciencias, Universidad Autónoma de Madrid, Madrid, Spain.
Miguel Ruiz-TorresChromosome Dynamics Group, Centro Nacional de Investigaciones Oncológicas (CNIO), Madrid, Spain.
Rocío GómezUnidad de Biología Celular, Departamento de Biología, Facultad de Ciencias, Universidad Autónoma de Madrid, Madrid, Spain.
Andrea GuajardoUnidad de Biología Celular, Departamento de Biología, Facultad de Ciencias, Universidad Autónoma de Madrid, Madrid, Spain.
José Luis BarberoDepartamento de Biología Celular y Molecular, Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
Ana LosadaChromosome Dynamics Group, Centro Nacional de Investigaciones Oncológicas (CNIO), Madrid, Spain.ORCID 0000-0001-5251-3383
José A SujaUnidad de Biología Celular, Departamento de Biología, Facultad de Ciencias, Universidad Autónoma de Madrid, Madrid, Spain.ORCID 0000-0002-4266-795X
Universidad Autónoma de Madrid · ESSpanish National Cancer Research Centre · ESCentro de Investigaciones Biológicas Margarita Salas · ES

Funding

FEDERMinisterio de Economía y Competitividad (MEC) BFU2014-53681-PMinisterio de Economía y Competitividad (MEC) BFU2016-79841-RMinisterio de Economía y Competitividad (MEC) BFU2017-89408-R
6 · The paper itself

Abstract

Cohesin cofactors regulate the loading, maintenance, and release of cohesin complexes from chromosomes during mitosis but little is known on their role during vertebrate meiosis. One such cofactor is PDS5, which exists as two paralogs in somatic and germline cells, PDS5A and PDS5B, with unclear functions. Here, we have analyzed their distribution and functions in mouse spermatocytes. We show that simultaneous excision of Pds5A and Pds5B results in severe defects during early prophase I while their individual depletion does not, suggesting their functional redundancy. Shortened axial/lateral elements and a reduction of early recombination nodules are observed after the strong depletion of PDS5A/B proteins. Moreover, telomere integrity and their association to the nuclear envelope are severely compromised. As these defects occur without detectable reduction in chromosome-bound cohesin, we propose that the dynamic behavior of the complex, mediated by PDS5 proteins, is key for successful completion of meiotic prophase I.

Indexed as

MeiosisTelomereAnimalsCell Cycle ProteinsMaleMiceMitosisSpermatocytesSynaptonemal ComplexCell Cycle Proteinsaxial elementsmeiosismousePDS5telomeres

Identifiers

PMID32285610
PMCPMC7271656
OpenAlexW3015993049

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.