Evidence map›Paper›PMID 27098914›Full record

ArticleGenetics2016

Nuclear Envelope Retention of LINC Complexes Is Promoted by SUN-1 Oligomerization in the Caenorhabditis elegans Germ Line.

Anahita Daryabeigi, Alexander Woglar, Antoine Baudrimont, Nicola Silva, Dimitra Paouneskou, Cornelia Vesely, Manuel Rauter, Alexandra Penkner, Michael Jantsch, Verena Jantsch

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. A chromodomain protein mediates heterochromatin-directed piRNA expression.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. Article
  7. 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

10 authors at 4 institutions in 1 country.

Anahita DaryabeigiDepartment of Chromosome Biology, Max F. Perutz Laboratories, Vienna Biocenter, University of Vienna, 1030, Austria.
Alexander WoglarDepartment of Chromosome Biology, Max F. Perutz Laboratories, Vienna Biocenter, University of Vienna, 1030, Austria.
Antoine BaudrimontDepartment of Chromosome Biology, Max F. Perutz Laboratories, Vienna Biocenter, University of Vienna, 1030, Austria.
Nicola SilvaDepartment of Chromosome Biology, Max F. Perutz Laboratories, Vienna Biocenter, University of Vienna, 1030, Austria.
Dimitra PaouneskouDepartment of Chromosome Biology, Max F. Perutz Laboratories, Vienna Biocenter, University of Vienna, 1030, Austria.
Cornelia VeselyCenter for Anatomy and Cell Biology, Department of Cell and Developmental Biology, Medical University of Vienna, 1090, Austria.
Manuel RauterDepartment of Chromosome Biology, Max F. Perutz Laboratories, Vienna Biocenter, University of Vienna, 1030, Austria.
Alexandra PenknerDepartment of Chromosome Biology, Max F. Perutz Laboratories, Vienna Biocenter, University of Vienna, 1030, Austria.
Michael JantschCenter for Anatomy and Cell Biology, Department of Cell and Developmental Biology, Medical University of Vienna, 1090, Austria.
Verena JantschDepartment of Chromosome Biology, Max F. Perutz Laboratories, Vienna Biocenter, University of Vienna, 1030, Austria verena.jantsch@univie.ac.at.
Max Perutz Labs · ATUniversity of Vienna · ATMedical University of Vienna · ATVienna Biocenter · AT

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Ann E. Rougvie · 2012 to 2026
$7.5M
Austrian Science Fund FWF P 23638Austrian Science Fund FWF P 26882NIH HHS P40 OD010440
6 · The paper itself

Abstract

SUN (Sad1 and UNC-84) and KASH (Klarsicht, ANC-1, and Syne homology) proteins are constituents of the inner and outer nuclear membranes. They interact in the perinuclear space via C-terminal SUN-KASH domains to form the linker of nucleoskeleton and cytoskeleton (LINC) complex thereby bridging the nuclear envelope. LINC complexes mediate numerous biological processes by connecting chromatin with the cytoplasmic force-generating machinery. Here we show that the coiled-coil domains of SUN-1 are required for oligomerization and retention of the protein in the nuclear envelope, especially at later stages of female gametogenesis. Consistently, deletion of the coiled-coil domain makes SUN-1 sensitive to unilateral force exposure across the nuclear membrane. Premature loss of SUN-1 from the nuclear envelope leads to embryonic death due to loss of centrosome-nuclear envelope attachment. However, in contrast to previous notions we can show that the coiled-coil domain is dispensable for functional LINC complex formation, exemplified by successful chromosome sorting and synapsis in meiotic prophase I in its absence.

Indexed as

Protein MultimerizationAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell Cycle ProteinsFemaleMeiosisNuclear EnvelopeNuclear ProteinsOogoniaProtein BindingProtein DomainsReceptors, Cytoplasmic and NuclearCaenorhabditis elegans ProteinsCell Cycle ProteinsKDP-1 protein, C elegansNuclear ProteinsReceptors, Cytoplasmic and Nuclearsun-1 protein, C elegansCaenorhabditis elegansLINC complexmeiosisoocyte formation

Identifiers

PMID27098914
PMCPMC4896190
OpenAlexW2336813029

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.