Evidence map›Paper›PMID 35178558›Full record

ArticleJournal of cell science2022

Emerin self-assembly and nucleoskeletal coupling regulate nuclear envelope mechanics against stress.

Anthony Fernandez, Markville Bautista, Liying Wu, Fabien Pinaud

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2022. 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
2.5field-weighted citation impact, top 10% 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, 31 citations in OpenAlex.

  1. Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  10. Mechanical Stress Triggers Premature Senescence in Cardiac Fibroblasts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  11. Review
  12. Article
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  15. The role of inner nuclear membrane protein emerin in myogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    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

4 authors at 1 institution in 1 country.

Anthony FernandezDepartment of Biological Sciences, University of Southern California, 1050 Childs Way, Los Angeles, CA 90089, USA.
Markville BautistaDepartment of Chemistry, University of Southern California, 1050 Childs Way, Los Angeles, CA 90089, USA.
Liying WuDepartment of Biological Sciences, University of Southern California, 1050 Childs Way, Los Angeles, CA 90089, USA.
Fabien PinaudDepartment of Biological Sciences, University of Southern California, 1050 Childs Way, Los Angeles, CA 90089, USA.ORCID 0000-0002-4272-3616
University of Southern California · US

Funding

Nanoscale organization and mechanotransduction of emerin at the nuclear envelope: Implication for Emery-Dreifuss Muscular DystrophyR21AR076514 · NIAMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PINAUD, FABIEN · 2020 to 2021
$394k
NIAMS NIH HHS R21 AR076514NIAMS NIH HHS R21AR076514NIH HHS R21AR076514
6 · The paper itself

Abstract

Emerin is an integral nuclear envelope protein that participates in the maintenance of nuclear shape. When mutated or absent, emerin causes X-linked Emery-Dreifuss muscular dystrophy (EDMD). To understand how emerin takes part in molecular --scaffolding at the nuclear envelope and helps protect the nucleus against mechanical stress, we established its nanoscale organization using single-molecule tracking and super-resolution microscopy. We show that emerin monomers form localized oligomeric nanoclusters stabilized by both lamin A/C and the SUN1-containing linker of nucleoskeleton and cytoskeleton (LINC) complex. Interactions of emerin with nuclear actin and BAF (also known as BANF1) additionally modulate its membrane mobility and its ability to oligomerize. In nuclei subjected to mechanical challenges, the mechanotransduction functions of emerin are coupled to changes in its oligomeric state, and the incremental self-assembly of emerin determines nuclear shape adaptation against mechanical forces. We also show that the abnormal nuclear envelope deformations induced by EDMD emerin mutants stem from improper formation of lamin A/C and LINC complex-stabilized emerin oligomers. These findings place emerin at the center of the molecular processes that regulate nuclear shape remodeling in response to mechanical challenges.

Indexed as

Muscular Dystrophy, Emery-DreifussNuclear EnvelopeHumansMechanotransduction, CellularMembrane ProteinsNuclear ProteinsemerinMembrane ProteinsNuclear ProteinsEmerinLaminopathyMechanobiologyNuclear envelopeSuper-resolution microscopy

Identifiers

PMID35178558
PMCPMC8995096
OpenAlexW4212841047

What OpenQuestion holds

Textmetadata
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.