Evidence map›Paper›PMID 30559341›Full record

ArticleNature communications2018

Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1.

James M Dunce, Amy E Milburn, Manickam Gurusaran, Irene da Cruz, Lee T Sen, Ricardo Benavente, Owen R Davies

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Meiotic telomeres of vole B chromosomes: shelterin and associated proteins provide a link to the nuclear envelope.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Kinetic analysis of synaptonemal complex dynamics during meiosis of yeastFrontiers in cell and developmental biology · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Meiotic Chromosome Dynamics in Zebrafish.Frontiers in cell and developmental biology · 2021
    Review
  19. Article
  20. 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

7 authors at 2 institutions in 2 countries.

James M DunceInstitute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK.
Amy E MilburnInstitute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK.
Manickam GurusaranInstitute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK.
Irene da CruzDepartment of Cell and Developmental Biology, Biocenter, University of Würzburg, D-97074, Würzburg, Germany.
Lee T SenInstitute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK.
Ricardo BenaventeDepartment of Cell and Developmental Biology, Biocenter, University of Würzburg, D-97074, Würzburg, Germany. benavente@biozentrum.uni-wuerzburg.de.
Owen R DaviesInstitute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK. owen.davies@newcastle.ac.uk.ORCID http://orcid.org/0000-0002-3806-5403
Newcastle University · GBUniversity of Würzburg · DE

Funding

Wellcome Trust
6 · The paper itself

Abstract

Meiotic chromosomes undergo rapid prophase movements, which are thought to facilitate the formation of inter-homologue recombination intermediates that underlie synapsis, crossing over and segregation. The meiotic telomere complex (MAJIN, TERB1, TERB2) tethers telomere ends to the nuclear envelope and transmits cytoskeletal forces via the LINC complex to drive these rapid movements. Here, we report the molecular architecture of the meiotic telomere complex through the crystal structure of MAJIN-TERB2, together with light and X-ray scattering studies of wider complexes. The MAJIN-TERB2 2:2 hetero-tetramer binds strongly to DNA and is tethered through long flexible linkers to the inner nuclear membrane and two TRF1-binding 1:1 TERB2-TERB1 complexes. Our complementary structured illumination microscopy studies and biochemical findings reveal a telomere attachment mechanism in which MAJIN-TERB2-TERB1 recruits telomere-bound TRF1, which is then displaced during pachytene, allowing MAJIN-TERB2-TERB1 to bind telomeric DNA and form a mature attachment plate.

Indexed as

Apoptosis Regulatory ProteinsCarrier ProteinsCell Cycle ProteinsCell LineCrystallography, X-RayDNA-Binding ProteinsHumansMeiosisMultiprotein ComplexesMyosinsNuclear EnvelopeNuclear ProteinsProtein FoldingTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1Apoptosis Regulatory ProteinsCarrier ProteinsCell Cycle ProteinsDNA-Binding ProteinsMultiprotein ComplexesMYO18A protein, humanMyosinsNuclear ProteinsTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1TERB1 protein, humanTERB2 protein, human

Identifiers

PMID30559341
PMCPMC6297230
OpenAlexW2904152911

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.