Evidence map›Paper›PMID 34197600›Full record

ArticleNucleic acids research2021

The synaptonemal complex central region modulates crossover pathways and feedback control of meiotic double-strand break formation.

Min-Su Lee, Mika T Higashide, Hyungseok Choi, Ke Li, Soogil Hong, Kangseok Lee, Akira Shinohara, Miki Shinohara, Keun P Kim

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

30 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure and function of the synaptonemal complex.The Journal of cell biology · 2026
    Review
  4. bioRxiv : the preprint server for biology · 2026
    Article
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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

9 authors at 2 institutions in 2 countries.

Min-Su LeeDepartment of Life Science, Chung-Ang University, Seoul 06974, South Korea.
Mika T HigashideInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan.
Hyungseok ChoiDepartment of Life Science, Chung-Ang University, Seoul 06974, South Korea.
Ke LiInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan.
Soogil HongDepartment of Life Science, Chung-Ang University, Seoul 06974, South Korea.
Kangseok LeeDepartment of Life Science, Chung-Ang University, Seoul 06974, South Korea.
Akira ShinoharaInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan.
Miki ShinoharaInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan.
Keun P KimDepartment of Life Science, Chung-Ang University, Seoul 06974, South Korea.ORCID 0000-0002-5973-8259
Chung-Ang University · KRProtein Research Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The synaptonemal complex (SC) is a proteinaceous structure that mediates homolog engagement and genetic recombination during meiosis. In budding yeast, Zip-Mer-Msh (ZMM) proteins promote crossover (CO) formation and initiate SC formation. During SC elongation, the SUMOylated SC component Ecm11 and the Ecm11-interacting protein Gmc2 facilitate the polymerization of Zip1, an SC central region component. Through physical recombination, cytological, and genetic analyses, we found that ecm11 and gmc2 mutants exhibit chromosome-specific defects in meiotic recombination. CO frequencies on a short chromosome (chromosome III) were reduced, whereas CO and non-crossover frequencies on a long chromosome (chromosome VII) were elevated. Further, in ecm11 and gmc2 mutants, more double-strand breaks (DSBs) were formed on a long chromosome during late prophase I, implying that the Ecm11-Gmc2 (EG) complex is involved in the homeostatic regulation of DSB formation. The EG complex may participate in joint molecule (JM) processing and/or double-Holliday junction resolution for ZMM-dependent CO-designated recombination. Absence of the EG complex ameliorated the JM-processing defect in zmm mutants, suggesting a role for the EG complex in suppressing ZMM-independent recombination. Our results suggest that the SC central region functions as a compartment for sequestering recombination-associated proteins to regulate meiosis specificity during recombination.

Indexed as

Crossing Over, GeneticDNA Breaks, Double-StrandedCell Cycle ProteinsChromosomes, FungalDNA-Binding ProteinsDNA ReplicationEndonucleasesFeedback, PhysiologicalGene DeletionMeiosisRecombination, GeneticSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSynaptonemal ComplexTemperatureTranscription FactorsCell Cycle ProteinsDNA-Binding ProteinsEcm11 protein, S cerevisiaeEndonucleasesMUS81 protein, S cerevisiaeNDT80 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitin-Protein LigasesZip3 protein, S cerevisiae

Identifiers

PMID34197600
PMCPMC8287913
OpenAlexW3176424860

What OpenQuestion holds

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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.