Evidence map›Paper›PMID 26598615›Full record

ArticleThe Journal of cell biology2015

The synaptonemal complex is assembled by a polySUMOylation-driven feedback mechanism in yeast.

Wing-Kit Leung, Neil Humphryes, Negar Afshar, Bilge Argunhan, Yaroslav Terentyev, Tomomi Tsubouchi, Hideo Tsubouchi

Abstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Structure and function of the synaptonemal complex.The Journal of cell biology · 2026
    Review
  3. Article
  4. Article
  5. Genetic control of meiosis surveillance mechanisms in mammals.Frontiers in cell and developmental biology · 2023
    Review
  6. Kinetic analysis of synaptonemal complex dynamics during meiosis of yeastFrontiers in cell and developmental biology · 2023
    Article
  7. Polycomb group (PcG) proteins prevent the assembly of abnormal synaptonemal complex structures during meiosis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. SCFLife science alliance · 2021
    Article
  14. Article
  15. Regulation of Meiotic Prophase One in Mammalian Oocytes.Frontiers in cell and developmental biology · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Wing-Kit LeungGenome Damage and Stability Centre, Life Sciences, University of Sussex, Brighton BN19RQ, England, UK.
Neil HumphryesGenome Damage and Stability Centre, Life Sciences, University of Sussex, Brighton BN19RQ, England, UK.
Negar AfsharGenome Damage and Stability Centre, Life Sciences, University of Sussex, Brighton BN19RQ, England, UK.
Bilge ArgunhanGenome Damage and Stability Centre, Life Sciences, University of Sussex, Brighton BN19RQ, England, UK.
Yaroslav TerentyevGenome Damage and Stability Centre, Life Sciences, University of Sussex, Brighton BN19RQ, England, UK.
Tomomi TsubouchiNational Institute for Basic Biology, National Institutes of Natural Sciences, Myodaiji, Okazaki, Aichi 444-8585, Japan.
Hideo TsubouchiGenome Damage and Stability Centre, Life Sciences, University of Sussex, Brighton BN19RQ, England, UK.

Funding

Biotechnology and Biological Sciences Research Council BB/I009159/1Medical Research Council
6 · The paper itself

Abstract

During meiotic prophase I, proteinaceous structures called synaptonemal complexes (SCs) connect homologous chromosomes along their lengths via polymeric arrays of transverse filaments (TFs). Thus, control of TF polymerization is central to SC formation. Using budding yeast, we show that efficiency of TF polymerization closely correlates with the extent of SUMO conjugation to Ecm11, a component of SCs. HyperSUMOylation of Ecm11 leads to highly aggregative TFs, causing frequent assembly of extrachromosomal structures. In contrast, hypoSUMOylation leads to discontinuous, fragmented SCs, indicative of defective TF polymerization. We further show that the N terminus of the yeast TF, Zip1, serves as an activator for Ecm11 SUMOylation. Coexpression of the Zip1 N terminus and Gmc2, a binding partner of Ecm11, is sufficient to induce robust polySUMOylation of Ecm11 in nonmeiotic cells. Because TF assembly is mediated through N-terminal head-to-head associations, our results suggest that mutual activation between TF assembly and Ecm11 polySUMOylation acts as a positive feedback loop that underpins SC assembly.

Indexed as

SumoylationCell Cycle ProteinsEndopeptidasesFeedback, PhysiologicalFungal ProteinsNuclear ProteinsProtein Interaction Domains and MotifsProtein MultimerizationSaccharomycetalesSynaptonemal ComplexCell Cycle ProteinsEndopeptidasesFungal ProteinsNuclear Proteins

Identifiers

PMID26598615
PMCPMC4657171

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.