Severe protein aggregate myopathy in a knockout mouse model points to an essential role of cofilin2 in sarcomeric actin exchange and muscle maintenance

Mutations in the human actin depolymerizing factor cofilin2 result in an autosomal dominant form of nemaline myopathy. Here, we report on the targeted ablation of murine cofilin2, which leads to a severe skeletal muscle specific phenotype within the first two weeks after birth. Apart from skeletal m...

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Published inEuropean journal of cell biology Vol. 93; no. 5-6; pp. 252 - 266
Main Authors Gurniak, Christine B., Chevessier, Frédéric, Jokwitz, Melanie, Jönsson, Friederike, Perlas, Emerald, Richter, Hendrik, Matern, Gabi, Boyl, Pietro Pilo, Chaponnier, Christine, Fürst, Dieter, Schröder, Rolf, Witke, Walter
Format Journal Article
LanguageEnglish
Published Germany Elsevier GmbH 01.05.2014
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Abstract Mutations in the human actin depolymerizing factor cofilin2 result in an autosomal dominant form of nemaline myopathy. Here, we report on the targeted ablation of murine cofilin2, which leads to a severe skeletal muscle specific phenotype within the first two weeks after birth. Apart from skeletal muscle, cofilin2 is also expressed in heart and CNS, however the pathology was restricted to skeletal muscle. The two close family members of cofilin2 – ADF and cofilin1 – were co-expressed in muscle, but unable to compensate for the loss of cofilin2. While primary myofibril assembly and muscle development were unaffected in cofilin2 mutant mice, progressive muscle degeneration was observed between postnatal days 3 and 7. Muscle pathology was characterized by sarcoplasmic protein aggregates, fiber size disproportion, mitochondrial abnormalities and internal nuclei. The observed muscle pathology differed from nemaline myopathy, but showed combined features of actin-associated myopathy and myofibrillar myopathy. In cofilin2 mutant mice, the postnatal expression pattern and turnover of sarcomeric α-actin isoforms were altered. Levels of smooth muscle α-actin were increased and remained high in developing muscles, suggesting that cofilin2 plays a crucial role during the exchange of α-actin isoforms during the early postnatal remodeling of the sarcomere.
AbstractList Mutations in the human actin depolymerizing factor cofilin2 result in an autosomal dominant form of nemaline myopathy. Here, we report on the targeted ablation of murine cofilin2, which leads to a severe skeletal muscle specific phenotype within the first two weeks after birth. Apart from skeletal muscle, cofilin2 is also expressed in heart and CNS, however the pathology was restricted to skeletal muscle. The two close family members of cofilin2 - ADF and cofilin1 - were co-expressed in muscle, but unable to compensate for the loss of cofilin2. While primary myofibril assembly and muscle development were unaffected in cofilin2 mutant mice, progressive muscle degeneration was observed between postnatal days 3 and 7. Muscle pathology was characterized by sarcoplasmic protein aggregates, fiber size disproportion, mitochondrial abnormalities and internal nuclei. The observed muscle pathology differed from nemaline myopathy, but showed combined features of actin-associated myopathy and myofibrillar myopathy. In cofilin2 mutant mice, the postnatal expression pattern and turnover of sarcomeric α-actin isoforms were altered. Levels of smooth muscle α-actin were increased and remained high in developing muscles, suggesting that cofilin2 plays a crucial role during the exchange of α-actin isoforms during the early postnatal remodeling of the sarcomere.
Author Boyl, Pietro Pilo
Schröder, Rolf
Gurniak, Christine B.
Perlas, Emerald
Fürst, Dieter
Chevessier, Frédéric
Jokwitz, Melanie
Matern, Gabi
Chaponnier, Christine
Jönsson, Friederike
Richter, Hendrik
Witke, Walter
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  organization: University of Bonn, Institute of Genetics, Cell Migration Unit, Germany
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  surname: Chevessier
  fullname: Chevessier, Frédéric
  organization: University of Erlangen, Institute of Neuropathology, Germany
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  organization: University of Bonn, Institute of Genetics, Cell Migration Unit, Germany
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  surname: Jönsson
  fullname: Jönsson, Friederike
  organization: Institut Pasteur, Département d’Immunologie, Laboratoire Anticorps en Thérapie et Pathologie, Inserm, U.760, 75015 Paris, France
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  organization: University of Bonn, Institute of Cellular and Molecular Botany, Germany
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  organization: University of Bonn, Institute of Genetics, Cell Migration Unit, Germany
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  organization: University of Bonn, Institute of Genetics, Cell Migration Unit, Germany
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  organization: University of Geneva, Department of Pathology and Immunology, Switzerland
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  surname: Fürst
  fullname: Fürst, Dieter
  organization: University of Bonn, Institute of Cell Biology, Germany
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  surname: Schröder
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  surname: Witke
  fullname: Witke, Walter
  email: w.witke@uni-bonn.de
  organization: University of Bonn, Institute of Genetics, Cell Migration Unit, Germany
BackLink https://www.ncbi.nlm.nih.gov/pubmed/24598388$$D View this record in MEDLINE/PubMed
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Issue 5-6
Keywords Muscle development
Sarcomere structure
Cofilin2
Protein aggregate myopathy
Actin isoform exchange
Language English
License Copyright © 2014 Elsevier GmbH. All rights reserved.
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Snippet Mutations in the human actin depolymerizing factor cofilin2 result in an autosomal dominant form of nemaline myopathy. Here, we report on the targeted ablation...
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SubjectTerms Actin isoform exchange
Actins - metabolism
Animals
Brain - metabolism
Cofilin 2 - genetics
Cofilin 2 - metabolism
Cofilin2
Cytoskeleton - genetics
Cytoskeleton - pathology
Mice, Inbred C57BL
Mice, Knockout
Muscle Development
Muscle, Skeletal - growth & development
Muscle, Skeletal - metabolism
Muscle, Skeletal - pathology
Muscle, Smooth - growth & development
Muscle, Smooth - metabolism
Muscular Diseases - genetics
Muscular Diseases - pathology
Myocardium - metabolism
Organ Specificity
Protein aggregate myopathy
Protein Aggregates - genetics
Sarcomere structure
Sarcomeres - metabolism
Title Severe protein aggregate myopathy in a knockout mouse model points to an essential role of cofilin2 in sarcomeric actin exchange and muscle maintenance
URI https://dx.doi.org/10.1016/j.ejcb.2014.01.007
https://www.ncbi.nlm.nih.gov/pubmed/24598388
https://search.proquest.com/docview/1548635625
Volume 93
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