Evidence map›Paper›PMID 31664178›Full record

ArticleScientific reports2019

Actomyosin contractility scales with myoblast elongation and enhances differentiation through YAP nuclear export.

Céline Bruyère, Marie Versaevel, Danahe Mohammed, Laura Alaimo, Marine Luciano, Eléonore Vercruysse, Sylvain Gabriele

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 72 citations in OpenAlex.

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  20. Mechanics and functional consequences of nuclear deformations.Nature reviews. Molecular cell biology · 2022
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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

7 authors at 1 institution in 1 country.

Céline BruyèreUniversity of Mons, Laboratory for Complex Fluids and Interfaces, Mechanobiology and Soft Matter group, Research Institute for Biosciences, Place du Parc, 20, B-7000, Mons, Belgium.
Marie VersaevelUniversity of Mons, Laboratory for Complex Fluids and Interfaces, Mechanobiology and Soft Matter group, Research Institute for Biosciences, Place du Parc, 20, B-7000, Mons, Belgium.
Danahe MohammedUniversity of Mons, Laboratory for Complex Fluids and Interfaces, Mechanobiology and Soft Matter group, Research Institute for Biosciences, Place du Parc, 20, B-7000, Mons, Belgium.
Laura AlaimoUniversity of Mons, Laboratory for Complex Fluids and Interfaces, Mechanobiology and Soft Matter group, Research Institute for Biosciences, Place du Parc, 20, B-7000, Mons, Belgium.
Marine LucianoUniversity of Mons, Laboratory for Complex Fluids and Interfaces, Mechanobiology and Soft Matter group, Research Institute for Biosciences, Place du Parc, 20, B-7000, Mons, Belgium.
Eléonore VercruysseUniversity of Mons, Laboratory for Complex Fluids and Interfaces, Mechanobiology and Soft Matter group, Research Institute for Biosciences, Place du Parc, 20, B-7000, Mons, Belgium.
Sylvain GabrieleUniversity of Mons, Laboratory for Complex Fluids and Interfaces, Mechanobiology and Soft Matter group, Research Institute for Biosciences, Place du Parc, 20, B-7000, Mons, Belgium. sylvain.gabriele@umons.ac.be.
University of Mons · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Skeletal muscle fibers are formed by the fusion of mononucleated myoblasts into long linear myotubes, which differentiate and reorganize into multinucleated myofibers that assemble in bundles to form skeletal muscles. This fundamental process requires the elongation of myoblasts into a bipolar shape, although a complete understanding of the mechanisms governing skeletal muscle fusion is lacking. To address this question, we consider cell aspect ratio, actomyosin contractility and the Hippo pathway member YAP as potential regulators of the fusion of myoblasts into myotubes. Using fibronectin micropatterns of different geometries and traction force microscopy, we investigated how myoblast elongation affects actomyosin contractility. Our findings indicate that cell elongation enhances actomyosin contractility in myoblasts, which regulate their actin network to their spreading area. Interestingly, we found that the contractility of cell pairs increased after their fusion and raise on elongated morphologies. Furthermore, our findings indicate that myoblast elongation modulates nuclear orientation and triggers cytoplasmic localization of YAP, increasing evidence that YAP is a key regulator of mechanotransduction in myoblasts. Taken together, our findings support a mechanical model where actomyosin contractility scales with myoblast elongation and enhances the differentiation of myoblasts into myotubes through YAP nuclear export.

Indexed as

ActinsActomyosinAdaptor Proteins, Signal TransducingAnimalsCell Cycle ProteinsCell DifferentiationCell NucleusCell ShapeCell SizeFibronectinsHippo Signaling PathwayMiceMuscle ContractionMuscle Fibers, SkeletalMyoblastsProtein Serine-Threonine KinasesActinsActomyosinAdaptor Proteins, Signal TransducingCell Cycle ProteinsFibronectinsProtein Serine-Threonine KinasesYap1 protein, mouseYAP-Signaling Proteins

Identifiers

PMID31664178
PMCPMC6820726
OpenAlexW2982342780

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.