Evidence map›Paper›PMID 29440262›Full record

ArticleGenes & development2018

A meiotic XPF-ERCC1-like complex recognizes joint molecule recombination intermediates to promote crossover formation.

Arnaud De Muyt, Alexandra Pyatnitskaya, Jessica Andréani, Lepakshi Ranjha, Claire Ramus, Raphaëlle Laureau, Ambra Fernandez-Vega, Daniel Holoch, Elodie Girard, Jérome Govin and 5 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
–field-weighted citation impact
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

69 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Structure and function of the synaptonemal complex.The Journal of cell biology · 2026
    Review
  6. Article
  7. Ufd2p promotes efficient crossover formation by destabilizing Top2p during meiosis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. HEIP1 orchestrates pro-crossover protein activity during mammalian meiosis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

9 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

15 authors at 5 institutions in 2 countries.

Arnaud De MuytUMR3244, Centre Nationnal de la Recherche Scientifique (CNRS), Institut Curie, PSL (Paris Sciences and Letters) Research University, 75005 Paris, France.
Alexandra PyatnitskayaUMR3244, Centre Nationnal de la Recherche Scientifique (CNRS), Institut Curie, PSL (Paris Sciences and Letters) Research University, 75005 Paris, France.
Jessica AndréaniInstitut de Biologie Intégrative de la Cellule (I2BC), Institut de biologie et de technologies de Saclay (iBiTec-S), Commissariat à l'Énergie Atomique et aux Énergies Alternatives (CEA), UMR9198, CNRS, Université Paris-Sud, 91190 Gif-sur-Yvette, France.
Lepakshi RanjhaInstitute for Research in Biomedicine, Università della Svizzera italiana, 6500 Bellinzona, Switzerland.
Claire RamusUniversity of Grenoble Alpes, CEA, Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Biosciences et Biotechnologies de Grenoble (BIG-BGE), 38000 Grenoble, France.
Raphaëlle LaureauUMR3244, Centre Nationnal de la Recherche Scientifique (CNRS), Institut Curie, PSL (Paris Sciences and Letters) Research University, 75005 Paris, France.
Ambra Fernandez-VegaUMR3244, Centre Nationnal de la Recherche Scientifique (CNRS), Institut Curie, PSL (Paris Sciences and Letters) Research University, 75005 Paris, France.
Daniel HolochUniversité Pierre et Marie Curie (UPMC), 75005 Paris, France.
Elodie GirardInstitut Curie, PSL Research University, Mines ParisTech, U900, INSERM, 75005 Paris, France.
Jérome GovinUniversity of Grenoble Alpes, CEA, Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Biosciences et Biotechnologies de Grenoble (BIG-BGE), 38000 Grenoble, France.
Raphaël MargueronUniversité Pierre et Marie Curie (UPMC), 75005 Paris, France.
Yohann CoutéUniversity of Grenoble Alpes, CEA, Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Biosciences et Biotechnologies de Grenoble (BIG-BGE), 38000 Grenoble, France.
Petr CejkaInstitute for Research in Biomedicine, Università della Svizzera italiana, 6500 Bellinzona, Switzerland.
Raphaël GuéroisInstitut de Biologie Intégrative de la Cellule (I2BC), Institut de biologie et de technologies de Saclay (iBiTec-S), Commissariat à l'Énergie Atomique et aux Énergies Alternatives (CEA), UMR9198, CNRS, Université Paris-Sud, 91190 Gif-sur-Yvette, France.
Valérie BordeUMR3244, Centre Nationnal de la Recherche Scientifique (CNRS), Institut Curie, PSL (Paris Sciences and Letters) Research University, 75005 Paris, France.
Centre National de la Recherche Scientifique · FRInserm · FRUniversité Paris-Sud · FRBoard of the Swiss Federal Institutes of Technology · CHUniversità della Svizzera italiana · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Meiotic crossover formation requires the stabilization of early recombination intermediates by a set of proteins and occurs within the environment of the chromosome axis, a structure important for the regulation of meiotic recombination events. The molecular mechanisms underlying and connecting crossover recombination and axis localization are elusive. Here, we identified the ZZS (Zip2-Zip4-Spo16) complex, required for crossover formation, which carries two distinct activities: one provided by Zip4, which acts as hub through physical interactions with components of the chromosome axis and the crossover machinery, and the other carried by Zip2 and Spo16, which preferentially bind branched DNA molecules in vitro. We found that Zip2 and Spo16 share structural similarities to the structure-specific XPF-ERCC1 nuclease, although it lacks endonuclease activity. The XPF domain of Zip2 is required for crossover formation, suggesting that, together with Spo16, it has a noncatalytic DNA recognition function. Our results suggest that the ZZS complex shepherds recombination intermediates toward crossovers as a dynamic structural module that connects recombination events to the chromosome axis. The identification of the ZZS complex improves our understanding of the various activities required for crossover implementation and is likely applicable to other organisms, including mammals.

Indexed as

Crossing Over, GeneticChromosomal Proteins, Non-HistoneChromosomes, FungalDNADNA-Binding ProteinsDNA Breaks, Double-StrandedEndodeoxyribonucleasesMeiosisMicrotubule-Associated ProteinsProtein DomainsSaccharomyces cerevisiae ProteinsChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsEndodeoxyribonucleasesMicrotubule-Associated ProteinsSaccharomyces cerevisiae ProteinsSpo16 protein, S cerevisiaeSpo22 protein, S cerevisiaeZip2 protein, S cerevisiaecrossoverhomologous recombinationmeiosissynaptonemal complexXPF–ERCC1Zip2–Zip4–Spo16 complex

Identifiers

PMID29440262
PMCPMC5859969
OpenAlexW2787874420

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.