Evidence map›Paper›PMID 29702642›Full record

ArticlePLoS biology2018

Polarization-resolved microscopy reveals a muscle myosin motor-independent mechanism of molecular actin ordering during sarcomere maturation.

Olivier Loison, Manuela Weitkunat, Aynur Kaya-Çopur, Camila Nascimento Alves, Till Matzat, Maria L Spletter, Stefan Luschnig, Sophie Brasselet, Pierre-François Lenne, Frank Schnorrer

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 73 citations in OpenAlex.

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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

10 authors at 4 institutions in 3 countries.

Olivier LoisonAix Marseille Université, CNRS, IBDM, Marseille, France.
Manuela WeitkunatMax Planck Institute of Biochemistry, Muscle Dynamics Group, Martinsried, Germany.
Aynur Kaya-ÇopurMax Planck Institute of Biochemistry, Muscle Dynamics Group, Martinsried, Germany.
Camila Nascimento AlvesMax Planck Institute of Biochemistry, Muscle Dynamics Group, Martinsried, Germany.
Till MatzatInstitute of Neurobiology and Cells-in-Motion Cluster of Excellence (EXC 1003 - CiM), University of Münster, Münster, Germany.
Maria L SpletterMax Planck Institute of Biochemistry, Muscle Dynamics Group, Martinsried, Germany.
Stefan LuschnigInstitute of Neurobiology and Cells-in-Motion Cluster of Excellence (EXC 1003 - CiM), University of Münster, Münster, Germany.
Sophie BrasseletAix Marseille Université, CNRS, Centrale Marseille, Institut Fresnel, Marseille, France.
Pierre-François LenneAix Marseille Université, CNRS, IBDM, Marseille, France.
Frank SchnorrerAix Marseille Université, CNRS, IBDM, Marseille, France.ORCID 0000-0002-9518-7263
Centre National de la Recherche Scientifique · FRMax Planck Institute of Biochemistry · DEUniversity of British Columbia · CAUniversity of Münster · DE

Funding

Resource Component: Acquisition, maintenance and distribution of Drosophila stocksP40OD018537 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Annette L. Parks · 2014 to 2026
$13.5M
NIH HHS P40 OD018537
6 · The paper itself

Abstract

Sarcomeres are stereotyped force-producing mini-machines of striated muscles. Each sarcomere contains a pseudocrystalline order of bipolar actin and myosin filaments, which are linked by titin filaments. During muscle development, these three filament types need to assemble into long periodic chains of sarcomeres called myofibrils. Initially, myofibrils contain immature sarcomeres, which gradually mature into their pseudocrystalline order. Despite the general importance, our understanding of myofibril assembly and sarcomere maturation in vivo is limited, in large part because determining the molecular order of protein components during muscle development remains challenging. Here, we applied polarization-resolved microscopy to determine the molecular order of actin during myofibrillogenesis in vivo. This method revealed that, concomitantly with mechanical tension buildup in the myotube, molecular actin order increases, preceding the formation of immature sarcomeres. Mechanistically, both muscle and nonmuscle myosin contribute to this actin order gain during early stages of myofibril assembly. Actin order continues to increase while myofibrils and sarcomeres mature. Muscle myosin motor activity is required for the regular and coordinated assembly of long myofibrils but not for the high actin order buildup during sarcomere maturation. This suggests that, in muscle, other actin-binding proteins are sufficient to locally bundle or cross-link actin into highly regular arrays.

Indexed as

Actin CytoskeletonActinsAnimalsBiomechanical PhenomenaConnectinDrosophila melanogasterFlight, AnimalMicroscopy, PolarizationMyofibrilsMyosinsPupaSarcomeresActinsConnectinMyosins

Identifiers

PMID29702642
PMCPMC5955565
OpenAlexW2800047565

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.