Evidence map›Paper›PMID 29878125›Full record

ArticleHuman molecular genetics2018

Cofilin-1 phosphorylation catalyzed by ERK1/2 alters cardiac actin dynamics in dilated cardiomyopathy caused by lamin A/C gene mutation.

Maria Chatzifrangkeskou, David Yadin, Thibaut Marais, Solenne Chardonnet, Mathilde Cohen-Tannoudji, Nathalie Mougenot, Alain Schmitt, Silvia Crasto, Elisa Di Pasquale, Coline Macquart and 11 more

Open access · bronzeAbstract read
In one paragraph

Article in Human molecular genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.6field-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

53 citing papers in PubMed, 62 citations in OpenAlex.

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  12. G protein regulation by RGS proteins in the pathophysiology of dilated cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2025
    Review
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  14. Nuclear envelope budding inhibition slows down progerin-induced aging process.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

21 authors at 10 institutions in 4 countries.

Maria ChatzifrangkeskouSorbonne Université, UPMC Paris 06, INSERM UMRS974, Center of Research in Myology, F-75013 Paris, France.
David YadinInstitute for Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.
Thibaut MaraisSorbonne Université, UPMC Paris 06, INSERM UMRS974, Center of Research in Myology, F-75013 Paris, France.
Solenne ChardonnetSorbonne Université, UPMC Paris 06, INSERM, UMS29 Omique, F-75013 Paris, France.
Mathilde Cohen-TannoudjiSorbonne Université, UPMC Paris 06, INSERM UMRS974, Center of Research in Myology, F-75013 Paris, France.
Nathalie MougenotSorbonne Université, UPMC Paris 06, INSERM, UMS28 Phénotypage du Petit Animal, Paris F-75013, France.
Alain SchmittInstitut Cochin, INSERM U1016-CNRS UMR 8104, Université Paris Descartes-Sorbonne Paris Cité, Paris F-75014, France.
Silvia CrastoIstituto Clinico Humanitas IRCCS, Milan, Italy.
Elisa Di PasqualeIstituto Clinico Humanitas IRCCS, Milan, Italy.
Coline MacquartSorbonne Université, UPMC Paris 06, INSERM UMRS974, Center of Research in Myology, F-75013 Paris, France.
Yannick TanguySorbonne Université, UPMC Paris 06, INSERM UMRS974, Center of Research in Myology, F-75013 Paris, France.
Imen JebenianiFaculté de Médecine La Timone, Université Aix-Marseille, INSERM UMR910, Marseille 13005, France.
Michel PucéatFaculté de Médecine La Timone, Université Aix-Marseille, INSERM UMR910, Marseille 13005, France.
Blanca Morales RodriguezSorbonne Université, UPMC Paris 06, INSERM UMRS974, Center of Research in Myology, F-75013 Paris, France.
Wolfgang H GoldmannDepartment of Physics, Friedrich-Alexander-University of Erlangen-Nuremberg, 91054 Erlangen, Germany.
Matteo Dal FerroCardiovascular Department, Ospedali Riuniti and University of Trieste, Trieste, Italy.
Maria-Grazia BiferiSorbonne Université, UPMC Paris 06, INSERM UMRS974, Center of Research in Myology, F-75013 Paris, France.
Petra KnausInstitute for Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.
Gisèle BonneSorbonne Université, UPMC Paris 06, INSERM UMRS974, Center of Research in Myology, F-75013 Paris, France.
Howard J WormanDepartment of Medicine.
Antoine MuchirSorbonne Université, UPMC Paris 06, INSERM UMRS974, Center of Research in Myology, F-75013 Paris, France.
Inserm · FRCentre de Recherche en MyologieUniversité Paris Cité · FRFreie Universität Berlin · DEInstitute of Genetic and Biomedical Research · ITSorbonne Université · FRAix-Marseille Université · FRColumbia University · USFriedrich-Alexander-Universität Erlangen-Nürnberg · DEUniversity of Trieste · IT

Funding

Pathogenesis of Emery-Dreifuss Muscular DystrophyR01AR048997 · NIAMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI WORMAN, HOWARD J · 2003 to 2024
$7.1M
NIAMS NIH HHS R01 AR048997
6 · The paper itself

Abstract

Hyper-activation of extracellular signal-regulated kinase (ERK) 1/2 contributes to heart dysfunction in cardiomyopathy caused by mutations in the lamin A/C gene (LMNA cardiomyopathy). The mechanism of how this affects cardiac function is unknown. We show that active phosphorylated ERK1/2 directly binds to and catalyzes the phosphorylation of the actin depolymerizing factor cofilin-1 on Thr25. Cofilin-1 becomes active and disassembles actin filaments in a large array of cellular and animal models of LMNA cardiomyopathy. In vivo expression of cofilin-1, phosphorylated on Thr25 by endogenous ERK1/2 signaling, leads to alterations in left ventricular function and cardiac actin. These results demonstrate a novel role for cofilin-1 on actin dynamics in cardiac muscle and provide a rationale on how increased ERK1/2 signaling leads to LMNA cardiomyopathy.

Indexed as

MutationActinsAdolescentAdultAnimalsCardiomyopathy, DilatedCase-Control StudiesCofilin 1FemaleHeartHumansLamin Type AMaleMiceMiddle AgedMitogen-Activated Protein Kinase 1ActinsCofilin 1Lamin Type AMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3

Identifiers

PMID29878125
PMCPMC6097156
OpenAlexW2805295001

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.