Evidence map›Paper›PMID 36635604›Full record

ArticleNature structural & molecular biology2023

Structural maturation of SYCP1-mediated meiotic chromosome synapsis by SYCE3.

James H Crichton, James M Dunce, Orla M Dunne, Lucy J Salmon, Paul S Devenney, Jennifer Lawson, Ian R Adams, Owen R Davies

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure and function of the synaptonemal complex.The Journal of cell biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Computational Tools for the Analysis of Meiotic Prophase I Images.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. 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 5 institutions in 2 countries.

James H Crichton *MRC Human Genetics Unit, MRC Institute of Genetics and Cancer, University of Edinburgh, Edinburgh, UK.
James M Dunce *Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, UK.
Orla M DunneBiosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, UK.
Lucy J SalmonBiosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, UK.
Paul S DevenneyMRC Human Genetics Unit, MRC Institute of Genetics and Cancer, University of Edinburgh, Edinburgh, UK.
Jennifer LawsonMRC Human Genetics Unit, MRC Institute of Genetics and Cancer, University of Edinburgh, Edinburgh, UK.
Ian R AdamsMRC Human Genetics Unit, MRC Institute of Genetics and Cancer, University of Edinburgh, Edinburgh, UK. Ian.Adams@ed.ac.uk.ORCID 0000-0001-8838-1271
Owen R DaviesBiosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, UK. Owen.Davies@ed.ac.uk.ORCID 0000-0002-3806-5403
Institute of Genetics and Cancer · GBNewcastle University · GBUniversity of Cambridge · GBVienna Biocenter · ATWellcome Centre for Cell Biology · GB

Funding

Medical Research Council MC_UU_00007/6NIDCD NIH HHS L30 DC008431Wellcome Trust 219413
6 · The paper itself

Abstract

In meiosis, a supramolecular protein structure, the synaptonemal complex (SC), assembles between homologous chromosomes to facilitate their recombination. Mammalian SC formation is thought to involve hierarchical zipper-like assembly of an SYCP1 protein lattice that recruits stabilizing central element (CE) proteins as it extends. Here we combine biochemical approaches with separation-of-function mutagenesis in mice to show that, rather than stabilizing the SYCP1 lattice, the CE protein SYCE3 actively remodels this structure during synapsis. We find that SYCP1 tetramers undergo conformational change into 2:1 heterotrimers on SYCE3 binding, removing their assembly interfaces and disrupting the SYCP1 lattice. SYCE3 then establishes a new lattice by its self-assembly mimicking the role of the disrupted interface in tethering together SYCP1 dimers. SYCE3 also interacts with CE complexes SYCE1-SIX6OS1 and SYCE2-TEX12, providing a mechanism for their recruitment. Thus, SYCE3 remodels the SYCP1 lattice into a CE-binding integrated SYCP1-SYCE3 lattice to achieve long-range synapsis by a mature SC.

Indexed as

Chromosome PairingSynaptonemal ComplexAnimalsCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsMammalsMeiosisMiceNuclear ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsNuclear ProteinsSYCE2 protein, mouseSyce3 protein, mouseSycp1 protein, mouse

Identifiers

PMID36635604
PMCPMC7614228
OpenAlexW4315707269

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.