Evidence map›Paper›PMID 24586196›Full record

ArticlePLoS genetics2014

DAAM is required for thin filament formation and Sarcomerogenesis during muscle development in Drosophila.

Imre Molnár, Ede Migh, Szilárd Szikora, Tibor Kalmár, Attila G Végh, Ferenc Deák, Szilvia Barkó, Beáta Bugyi, Zacharias Orfanos, János Kovács and 5 more

Abstract read
In one paragraph

Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
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

33 citing papers in PubMed.

  1. Review
  2. Article
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  7. Review
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  13. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review
  14. Article
  15. Article
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  17. 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

15 authors.

Imre MolnárInstitute of Genetics, Biological Research Centre HAS, Szeged, Hungary.
Ede MighInstitute of Genetics, Biological Research Centre HAS, Szeged, Hungary.
Szilárd SzikoraInstitute of Genetics, Biological Research Centre HAS, Szeged, Hungary.
Tibor KalmárInstitute of Genetics, Biological Research Centre HAS, Szeged, Hungary.
Attila G VéghInstitute of Biophysics, Biological Research Centre HAS, Szeged, Hungary.
Ferenc DeákInstitute of Biochemistry, Biological Research Centre HAS, Szeged, Hungary.
Szilvia BarkóUniversity of Pécs, Department of Biophysics, Pécs, Hungary.
Beáta BugyiUniversity of Pécs, Department of Biophysics, Pécs, Hungary.
Zacharias OrfanosDepartment of Biology, University of York, York, United Kingdom.
János KovácsDepartment of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary.
Gábor JuhászDepartment of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary.
György VáróInstitute of Biophysics, Biological Research Centre HAS, Szeged, Hungary.
Miklós NyitraiUniversity of Pécs, Department of Biophysics, Pécs, Hungary ; Hungarian Academy of Sciences, Office for Subsidized Research Units, Budapest, Hungary.
John SparrowDepartment of Biology, University of York, York, United Kingdom.
József MihályInstitute of Genetics, Biological Research Centre HAS, Szeged, Hungary.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During muscle development, myosin and actin containing filaments assemble into the highly organized sarcomeric structure critical for muscle function. Although sarcomerogenesis clearly involves the de novo formation of actin filaments, this process remained poorly understood. Here we show that mouse and Drosophila members of the DAAM formin family are sarcomere-associated actin assembly factors enriched at the Z-disc and M-band. Analysis of dDAAM mutants revealed a pivotal role in myofibrillogenesis of larval somatic muscles, indirect flight muscles and the heart. We found that loss of dDAAM function results in multiple defects in sarcomere development including thin and thick filament disorganization, Z-disc and M-band formation, and a near complete absence of the myofibrillar lattice. Collectively, our data suggest that dDAAM is required for the initial assembly of thin filaments, and subsequently it promotes filament elongation by assembling short actin polymers that anneal to the pointed end of the growing filaments, and by antagonizing the capping protein Tropomodulin.

Indexed as

Actin CytoskeletonActinsAdaptor Proteins, Signal TransducingAnimalsCell DifferentiationDrosophila melanogasterDrosophila ProteinsGene Expression Regulation, DevelopmentalMiceMuscle DevelopmentMyocardiumMyofibrilsMyosinsSarcomeresActinsAdaptor Proteins, Signal TransducingDAAM protein, DrosophilaDrosophila ProteinsMyosins

Identifiers

PMID24586196
PMCPMC3937221

What OpenQuestion holds

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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.