Evidence map›Paper›PMID 27307582›Full record

ArticleMolecular biology of the cell2016

Nucleus-dependent sarcomere assembly is mediated by the LINC complex.

Alexander L Auld, Eric S Folker

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Biphasic regulation of myogenesis by ALDH2, aldosterone, and oxidative stress.Pflugers Archiv : European journal of physiology · 2026
    Article
  2. Article
  3. FHODs: Nuclear tethered formins for nuclear mechanotransduction.Frontiers in cell and developmental biology · 2023
    Review
  4. Sarcomere maturation: function acquisition, molecular mechanism, and interplay with other organelles.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Review
  5. Nuclear movement in multinucleated cells.Development (Cambridge, England) · 2022
    Review
  6. Article
  7. Cells · 2021
    Article
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  11. Review
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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

2 authors at 1 institution in 2 countries.

Alexander L AuldDepartment of Biology, Boston College, Chestnut Hill, MA 02467.
Eric S FolkerDepartment of Biology, Boston College, Chestnut Hill, MA 02467 eric.folker@bc.edu.
Boston College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two defining characteristics of muscle cells are the many precisely positioned nuclei and the linearly arranged sarcomeres, yet the relationship between these two features is not known. We show that nuclear positioning precedes sarcomere formation. Furthermore, ZASP-GFP, a Z-line protein, colocalizes with F-actin in puncta at the cytoplasmic face of nuclei before sarcomere assembly. In embryos with mispositioned nuclei, ZASP-GFP is still recruited to the nuclei before its incorporation into sarcomeres. Furthermore, the first sarcomeres appear in positions close to the nuclei, regardless of nuclear position. These data suggest that the interaction between sarcomere proteins and nuclei is not dependent on properly positioned nuclei. Mechanistically, ZASP-GFP localization to the cytoplasmic face of the nucleus did require the linker of nucleoskeleton and cytoskeleton (LINC) complex. Muscle-specific depletion of klarsicht (nesprin) or klariod (SUN) blocked the recruitment of ZASP-GFP to the nucleus during the early stages of sarcomere assembly. As a result, sarcomeres were poorly formed and the general myofibril network was less stable, incomplete, and/or torn. These data suggest that the nucleus, through the LINC complex, is crucial for the proper assembly and stability of the sarcomere network.

Indexed as

Actin CytoskeletonActinsAnimalsCarrier ProteinsCell NucleusCytoskeletonDrosophilaDrosophila ProteinsLIM Domain ProteinsMembrane Transport ProteinsMicrofilament ProteinsMicrotubulesMyofibrilsNerve Tissue ProteinsNuclear MatrixNuclear ProteinsActinsCarrier ProteinsDrosophila Proteinsklar protein, DrosophilaLIM Domain ProteinsMembrane Transport ProteinsMicrofilament ProteinsNerve Tissue ProteinsNuclear ProteinsZasp52 protein, Drosophila

Identifiers

PMID27307582
PMCPMC4966977
OpenAlexW2443440841

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.