Evidence map›Paper›PMID 18802461›Full record

ArticlePLoS genetics2008

Corona is required for higher-order assembly of transverse filaments into full-length synaptonemal complex in Drosophila oocytes.

Scott L Page, Radhika S Khetani, Cathleen M Lake, Rachel J Nielsen, Jennifer K Jeffress, William D Warren, Sharon E Bickel, R Scott Hawley

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

54 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Structure and function of the synaptonemal complex.The Journal of cell biology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Premeiotic pairing of homologous chromosomes duringProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. 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
  18. A Brief History ofGenes · 2022
    Review
  19. Article
  20. Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
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 2 countries.

Scott L PageComparative Genomics Centre, School of Pharmacy and Molecular Sciences, James Cook University, Townsville, Australia. scott.page@jcu.edu.au
Radhika S Khetani
Cathleen M Lake
Rachel J Nielsen
Jennifer K Jeffress
William D Warren
Sharon E Bickel
R Scott Hawley
Stowers Institute for Medical Research · USDartmouth College · USJames Cook University · AU

Funding

Regulation of Sister-Chromatid Cohesion in MeiosisR01GM059354 · NIGMS · DARTMOUTH COLLEGE · PI BICKEL, SHARON ELIZABETH · 2000 to 2024
$6.6M
NIGMS NIH HHS GM-59354NIGMS NIH HHS R01 GM059354
6 · The paper itself

Abstract

The synaptonemal complex (SC) is an intricate structure that forms between homologous chromosomes early during the meiotic prophase, where it mediates homolog pairing interactions and promotes the formation of genetic exchanges. In Drosophila melanogaster, C(3)G protein forms the transverse filaments (TFs) of the SC. The N termini of C(3)G homodimers localize to the Central Element (CE) of the SC, while the C-termini of C(3)G connect the TFs to the chromosomes via associations with the axial elements/lateral elements (AEs/LEs) of the SC. Here, we show that the Drosophila protein Corona (CONA) co-localizes with C(3)G in a mutually dependent fashion and is required for the polymerization of C(3)G into mature thread-like structures, in the context both of paired homologous chromosomes and of C(3)G polycomplexes that lack AEs/LEs. Although AEs assemble in cona oocytes, they exhibit defects that are characteristic of c(3)G mutant oocytes, including failure of AE alignment and synapsis. These results demonstrate that CONA, which does not contain a coiled coil domain, is required for the stable 'zippering' of TFs to form the central region of the Drosophila SC. We speculate that CONA's role in SC formation may be similar to that of the mammalian CE proteins SYCE2 and TEX12. However, the observation that AE alignment and pairing occurs in Tex12 and Syce2 mutant meiocytes but not in cona oocytes suggests that the SC plays a more critical role in the stable association of homologs in Drosophila than it does in mammalian cells.

Indexed as

AnimalsChromosomesDrosophila melanogasterDrosophila ProteinsMeiosisOocytesProtein TransportSynaptonemal ComplexC3G protein, Drosophilacona protein, DrosophilaDrosophila Proteins

Identifiers

PMID18802461
PMCPMC2529403
OpenAlexW2161536584

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.