Evidence map›Paper›PMID 31107865›Full record

ArticlePLoS genetics2019

The E3 ubiquitin ligase Sina regulates the assembly and disassembly of the synaptonemal complex in Drosophila females.

Stacie E Hughes, Elizabeth Hemenway, Fengli Guo, Kexi Yi, Zulin Yu, R Scott Hawley

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Make it or break it: Protein homeostasis in the synaptonemal complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. The deubiquitinase Usp7 inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. 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
  7. Article
  8. Article
  9. Review
  10. Article
  11. Coordinating Proliferation, Polarity, and Cell Fate in theFrontiers in cell and developmental biology · 2020
    Review
  12. Article
  13. 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

6 authors at 1 institution in 1 country.

Stacie E HughesStowers Institute for Medical Research, Kansas City, Missouri, United States of America.ORCID 0000-0002-0992-1231
Elizabeth HemenwayStowers Institute for Medical Research, Kansas City, Missouri, United States of America.
Fengli GuoStowers Institute for Medical Research, Kansas City, Missouri, United States of America.
Kexi YiStowers Institute for Medical Research, Kansas City, Missouri, United States of America.
Zulin YuStowers Institute for Medical Research, Kansas City, Missouri, United States of America.
R Scott HawleyStowers Institute for Medical Research, Kansas City, Missouri, United States of America.ORCID 0000-0002-6478-0494
Stowers Institute for Medical Research · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During early meiotic prophase, homologous chromosomes are connected along their entire lengths by a proteinaceous tripartite structure known as the synaptonemal complex (SC). Although the components that comprise the SC are predominantly studied in this canonical ribbon-like structure, they can also polymerize into repeated structures known as polycomplexes. We find that in Drosophila oocytes, the ability of SC components to assemble into canonical tripartite SC requires the E3 ubiquitin ligase Seven in absentia (Sina). In sina mutant oocytes, SC components assemble into large rod-like polycomplexes instead of proper SC. Thus, the wild-type Sina protein inhibits the polymerization of SC components, including those of the lateral element, into polycomplexes. These polycomplexes persist into meiotic stages when canonical SC has been disassembled, indicating that Sina also plays a role in controlling SC disassembly. Polycomplexes induced by loss-of-function sina mutations associate with centromeres, sites of double-strand breaks, and cohesins. Perhaps as a consequence of these associations, centromere clustering is defective and crossing over is reduced. These results suggest that while features of the polycomplexes can be recognized as SC by other components of the meiotic nucleus, polycomplexes nonetheless fail to execute core functions of canonical SC.

Indexed as

AnimalsCell Cycle ProteinsCell NucleusCentromereChromosomal Proteins, Non-HistoneChromosome PairingCohesinsCytoskeletal ProteinsDrosophila melanogasterDrosophila ProteinsFemaleMeiosisNuclear ProteinsOocytesSeven in Absentia ProteinsSynaptonemal ComplexCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsCytoskeletal ProteinsDrosophila ProteinsNuclear ProteinsSeven in Absentia ProteinsUbiquitin-Protein Ligases

Identifiers

PMID31107865
PMCPMC6544331
OpenAlexW2946231207

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.