ArticleJournal of cell science2011
The desmin coil 1B mutation K190A impairs nebulin Z-disc assembly and destabilizes actin thin filaments.
Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Novel truncating Desmin mutation Arg150Stop disrupts structural integrity and cellular homeostasis by formation of persistent aggregate-like structure.Cell death discovery · 2026Article
- Coordinated Bone-Muscle Axis Association in South China Carp (Foods (Basel, Switzerland) · 2026Article
- Common and Key Differential Pathogenic Pathways in Desminopathy and Titinopathy.International journal of medical sciences · 2024Article
- Expression profile and bioinformatics analysis of circRNA and its associated ceRNA networks in longissimus dorsi from Lufeng cattle and Leiqiong cattle.BMC genomics · 2023Article
- Nucleus Mechanosensing in Cardiomyocytes.International journal of molecular sciences · 2023Review
- Synchrony of sarcomeric movement regulates left ventricular pump function in the in vivo beating mouse heart.The Journal of general physiology · 2021Article
- Real-Time In Vivo Imaging of Mouse Left Ventricle Reveals Fluctuating Movements of the Intercalated Discs.Nanomaterials (Basel, Switzerland) · 2020Article
- Intermediate filaments in cardiomyopathy.Biophysical reviews · 2018Review
- Type III Intermediate Filaments Desmin, Glial Fibrillary Acidic Protein (GFAP), Vimentin, and Peripherin.Cold Spring Harbor perspectives in biology · 2017Review
- Nebulette is a powerful cytolinker organizing desmin and actin in mouse hearts.Molecular biology of the cell · 2016Article
- Review
- Nebulin, a multi-functional giant.The Journal of experimental biology · 2016Review
- Desmin related disease: a matter of cell survival failure.Current opinion in cell biology · 2015Review
- Z-disc-associated, alternatively spliced, PDZ motif-containing protein (ZASP) mutations in the actin-binding domain cause disruption of skeletal muscle actin filaments in myofibrillar myopathy.The Journal of biological chemistry · 2014Article
- Μyospryn: a multifunctional desmin-associated protein.Histochemistry and cell biology · 2013Review
- Nebulin binding impedes mutant desmin filament assembly.Molecular biology of the cell · 2013Article
- The sarcomeric protein nebulin: another multifunctional giant in charge of muscle strength optimization.Frontiers in physiology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Desmin intermediate filaments intimately surround myofibrils in vertebrate muscle forming a mesh-like filament network. Desmin attaches to sarcomeres through its high-affinity association with nebulin, a giant F-actin binding protein that co-extends along the length of actin thin filaments. Here, we further investigated the functional significance of the association of desmin and nebulin in cultured primary myocytes to address the hypothesis that this association is key in integrating myofibrils to the intermediate filament network. Surprisingly, we identified eight peptides along the length of desmin that are capable of binding to C-terminal modules 160-170 in nebulin. In this study, we identified a targeted mutation (K190A) in the desmin coil 1B region that results in its reduced binding with the nebulin C-terminal modules. Using immunofluorescence microscopy and quantitative analysis, we demonstrate that expression of the mutant desmin K190A in primary myocytes results in a significant reduction in assembled endogenous nebulin and desmin at the Z-disc. Non-uniform actin filaments were markedly prevalent in myocytes expressing GFP-tagged desmin K190A, suggesting that the near-crystalline organization of actin filaments in striated muscle depends on a stable interaction between desmin and nebulin. All together, these data are consistent with a model in which Z-disc-associated nebulin interacts with desmin through multiple sites to provide efficient stability to satisfy the dynamic contractile activity of myocytes.
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