The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies
Summary: 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 nucl...
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| Format: | Article |
| Language: | English |
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Elsevier
2021-08-01
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| Series: | Cell Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124721010391 |
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Article |
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DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
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 |
| spellingShingle |
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 The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies Cell Reports cofilin-1 ERK1/2 signaling muscular dystrophy skeletal muscle sarcomeric organization |
| author_facet |
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 |
| author_sort |
Nicolas Vignier |
| title |
The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies |
| title_short |
The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies |
| title_full |
The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies |
| title_fullStr |
The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies |
| title_full_unstemmed |
The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies |
| title_sort |
non-muscle adf/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies |
| publisher |
Elsevier |
| series |
Cell Reports |
| issn |
2211-1247 |
| publishDate |
2021-08-01 |
| description |
Summary: 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. |
| topic |
cofilin-1 ERK1/2 signaling muscular dystrophy skeletal muscle sarcomeric organization |
| url |
http://www.sciencedirect.com/science/article/pii/S2211124721010391 |
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doaj-c556bebb8808453e8abeba29fd9a8cdb2021-08-26T04:33:26ZengElsevierCell Reports2211-12472021-08-01368109601The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathiesNicolas Vignier0Maria Chatzifrangkeskou1Luca Pinton2Hugo Wioland3Thibaut Marais4Mégane Lemaitre5Caroline Le Dour6Cécile Peccate7Déborah Cardoso8Alain Schmitt9Wei Wu10Maria-Grazia Biferi11Naïra Naouar12Coline Macquart13Maud Beuvin14Valérie Decostre15Gisèle Bonne16Guillaume Romet-Lemonne17Howard J. Worman18Francesco Saverio Tedesco19Antoine Jégou20Antoine Muchir21Sorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceDepartment of Cell and Developmental Biology, University College London, London, UK; Randall Centre for Cell and Molecular Biophysics, King’s College London, London, UKUniversité de Paris, CNRS, Institut Jacques Monod, 75013 Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceSorbonne Université, UMS28, Phénotypage du Petit Animal, Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceUniversité de Paris, INSERM, CNRS, Institut Cochin, 75005 Paris, FranceDepartment 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, USASorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, FranceUniversité de Paris, CNRS, Institut Jacques Monod, 75013 Paris, FranceDepartment 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, USADepartment 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, UKUniversité de Paris, CNRS, Institut Jacques Monod, 75013 Paris, FranceSorbonne Université, INSERM, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France; Corresponding authorSummary: 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.http://www.sciencedirect.com/science/article/pii/S2211124721010391cofilin-1ERK1/2 signalingmuscular dystrophyskeletal musclesarcomeric organization |