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Vignier N, Chatzifrangkeskou M, Pinton L, et al. The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies. Cell Rep. 2021;36(8):109601doi: 10.1016/j.celrep.2021.109601.
Vignier, N., Chatzifrangkeskou, M., Pinton, L., Wioland, H., Marais, T., Lemaitre, M., Le Dour, C., Peccate, C., Cardoso, D., Schmitt, A., Wu, W., Biferi, M. G., Naouar, N., Macquart, C., Beuvin, M., Decostre, V., Bonne, G., Romet-Lemonne, G., Worman, H. J., Tedesco, F. S., Jégou, A., & Muchir, A. (2021). The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies. Cell reports, 36(8), 109601. https://doi.org/10.1016/j.celrep.2021.109601
Vignier, Nicolas, et al. "The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies." Cell reports vol. 36,8 (2021): 109601. doi: https://doi.org/10.1016/j.celrep.2021.109601
Vignier N, Chatzifrangkeskou M, Pinton L, Wioland H, Marais T, Lemaitre M, Le Dour C, Peccate C, Cardoso D, Schmitt A, Wu W, Biferi MG, Naouar N, Macquart C, Beuvin M, Decostre V, Bonne G, Romet-Lemonne G, Worman HJ, Tedesco FS, Jégou A, Muchir A. The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies. Cell Rep. 2021 Aug 24;36(8):109601. doi: 10.1016/j.celrep.2021.109601. PMID: 34433058; PMCID: PMC8411111.
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Cell Rep. 2021 Aug 24;36(8):109601. doi: 10.1016/j.celrep.2021.109601.

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

Cell reports

Nicolas Vignier, Maria Chatzifrangkeskou, Luca Pinton, Hugo Wioland, Thibaut Marais, Mégane Lemaitre, Caroline Le Dour, Cécile Peccate, Déborah Cardoso, Alain Schmitt, Wei Wu, Maria-Grazia Biferi, Naïra Naouar, Coline Macquart, Maud Beuvin, Valérie Decostre, Gisèle Bonne, Guillaume Romet-Lemonne, Howard J Worman, Francesco Saverio Tedesco, Antoine Jégou, Antoine Muchir

Affiliations

  1. Sorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.
  2. Department of Cell and Developmental Biology, University College London, London, UK; Randall Centre for Cell and Molecular Biophysics, King's College London, London, UK.
  3. Université de Paris, CNRS, Institut Jacques Monod, 75013 Paris, France.
  4. Sorbonne Université, UMS28, Phénotypage du Petit Animal, Paris, France.
  5. Université de Paris, INSERM, CNRS, Institut Cochin, 75005 Paris, France.
  6. Department 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.
  7. Department 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.
  8. Sorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France. Electronic address: [email protected].

PMID: 34433058 PMCID: PMC8411111 DOI: 10.1016/j.celrep.2021.109601

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.

Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.

Keywords: ERK1/2 signaling; cofilin-1; muscular dystrophy; sarcomeric organization; skeletal muscle

Conflict of interest statement

Declaration of interests H.J.W. is on the scientific advisory board and owns equity in AlloMek Therapeutics. The remaining authors declare no competing interests.

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