Evidence map›Paper›PMID 34433058›Full record

ArticleCell reports2021

The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies.

Nicolas Vignier, Maria Chatzifrangkeskou, Luca Pinton, Hugo Wioland, Thibaut Marais, Mégane Lemaitre, Caroline Le Dour, Cécile Peccate, Déborah Cardoso, Alain Schmitt and 12 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Preclinical Advances of Therapies for Laminopathies.Journal of clinical medicine · 2021
    Review
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

22 authors at 10 institutions in 3 countries.

Nicolas VignierSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Maria ChatzifrangkeskouSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Luca PintonDepartment of Cell and Developmental Biology, University College London, London, UK; Randall Centre for Cell and Molecular Biophysics, King's College London, London, UK.
Hugo WiolandUniversité de Paris, CNRS, Institut Jacques Monod, 75013 Paris, France.
Thibaut MaraisSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Mégane LemaitreSorbonne Université, UMS28, Phénotypage du Petit Animal, Paris, France.
Caroline Le DourSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Cécile PeccateSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Déborah CardosoSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Alain SchmittUniversité de Paris, INSERM, CNRS, Institut Cochin, 75005 Paris, France.
Wei WuDepartment of Medicine, Vagelos College of Physicians and Surgeons, Columbia University, New York, NY, USA; Department of Pathology and Cell Biology, Vagelos College of Physicians and Surgeons, Columbia University, New York, NY, USA.
Maria-Grazia BiferiSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Naïra NaouarSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Coline MacquartSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Maud BeuvinSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Valérie DecostreSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Gisèle BonneSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
Guillaume Romet-LemonneUniversité de Paris, CNRS, Institut Jacques Monod, 75013 Paris, France.
Howard J WormanDepartment of Medicine, Vagelos College of Physicians and Surgeons, Columbia University, New York, NY, USA; Department of Pathology and Cell Biology, Vagelos College of Physicians and Surgeons, Columbia University, New York, NY, USA.
Francesco Saverio TedescoDepartment of Cell and Developmental Biology, University College London, London, UK; Dubowitz Neuromuscular Centre, UCL Great Ormond Street Institute of Child Health and Great Ormond Street Hospital for Children, London, UK; The Francis Crick Institute, London, UK.
Antoine JégouUniversité de Paris, CNRS, Institut Jacques Monod, 75013 Paris, France.
Antoine MuchirSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France. Electronic address: a.muchir@institut-myologie.org.
Institut de Myologie · FRCentre de Recherche en MyologieSorbonne Université · FRColumbia University · USInstitut Jacques Monod · FRGreat Ormond Street Hospital · GBInserm · FRUMS Phénotypage du petit animalUniversité Paris Cité · FRUniversity College London · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

Cofilins are important for the regulation of the actin cytoskeleton, sarcomere organization, and force production. The role of cofilin-1, the non-muscle-specific isoform, in muscle function remains unclear. Mutations in LMNA encoding A-type lamins, intermediate filament proteins of the nuclear envelope, cause autosomal Emery-Dreifuss muscular dystrophy (EDMD). Here, we report increased cofilin-1 expression in LMNA mutant muscle cells caused by the inability of proteasome degradation, suggesting a protective role by ERK1/2. It is known that phosphorylated ERK1/2 directly binds to and catalyzes phosphorylation of the actin-depolymerizing factor cofilin-1 on Thr25. In vivo ectopic expression of cofilin-1, as well as its phosphorylated form on Thr25, impairs sarcomere structure and force generation. These findings present a mechanism that provides insight into the molecular pathogenesis of muscular dystrophies caused by LMNA mutations.

Indexed as

Actin CytoskeletonAdolescentAdultAnimalsCell LineChildCofilin 1DestrinHumansLaminopathiesLamin Type AMaleMiceMice, Inbred C57BLMice, KnockoutMitogen-Activated Protein Kinase 1Cofilin 1DestrinDSTN protein, humanLamin Type ALMNA protein, humanMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3cofilin-1ERK1/2 signalingmuscular dystrophysarcomeric organizationskeletal muscle

Identifiers

PMID34433058
PMCPMC8411111
OpenAlexW3195329627

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.