ArticleHuman molecular genetics2013
Myopathic lamin mutations impair nuclear stability in cells and tissue and disrupt nucleo-cytoskeletal coupling.
Article in Human molecular genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.
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Who cites it
112 citing papers in PubMed, 175 citations in OpenAlex.
- Nuclear mechanobiology: a brief history and five unresolved questions.Nucleus (Austin, Tex.) · 2026Article
- An Unbiased Drug Screen in a Drosophila Model ofInternational journal of molecular sciences · 2026Article
- A-type lamins anchor emerin at the inner nuclear membrane via two independent binding sites.The Journal of biological chemistry · 2026Article
- Polarization increases nuclear stiffness in macrophages despite reduction in lamin A/C levels.npj biological physics and mechanics · 2026Article
- Interplay between microtubule interactome, myonuclei mechanotransduction, and positioning in myopathies.Nucleus (Austin, Tex.) · 2025Review
- Microtubule forces drive nuclear damage in LMNA cardiomyopathy.Nature cardiovascular research · 2025Article
- Review
- Review
- Aging and Altered Gravity: A Cellular Perspective.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Review
- Lamin variants cause cardiac arrhythmogenicity in Drosophila.Disease models & mechanisms · 2025Article
- Rare Variation in LMNA Underlies Polycystic Ovary Syndrome Pathogenesis in 2 Independent Cohorts.The Journal of clinical endocrinology and metabolism · 2025Article
- Viscoelastic extracellular matrix enhances epigenetic remodeling and cellular plasticity.Nature communications · 2025Article
- A genetic variant inScience advances · 2025Article
- Micro-Scale Topography Triggers Dynamic 3D Nuclear Deformations.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Role of Nuclear Lamins in the Regulation of the Genome: Focus on CardioLaminopathy.Sub-cellular biochemistry · 2025Review
- Dominantly inherited muscle disorders: understanding their complexity and exploring therapeutic approaches.Disease models & mechanisms · 2024Review
- N-terminal tags impair the ability of lamin A to provide structural support to the nucleus.Journal of cell science · 2024Article
- Blood flow-bearing physical forces, endothelial glycocalyx, and liver enzyme mobilization: A hypothesis.The Journal of general physiology · 2024Review
- PIGB maintains nuclear lamina organization in skeletal muscle of Drosophila.The Journal of cell biology · 2024Article
- Heterologous expression ofMolecular biology of the cell · 2024Article
52 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 7 institutions in 4 countries.
Funding
Abstract
Lamins are intermediate filament proteins that assemble into a meshwork underneath the inner nuclear membrane, the nuclear lamina. Mutations in the LMNA gene, encoding lamins A and C, cause a variety of diseases collectively called laminopathies. The disease mechanism for these diverse conditions is not well understood. Since lamins A and C are fundamental determinants of nuclear structure and stability, we tested whether defects in nuclear mechanics could contribute to the disease development, especially in laminopathies affecting mechanically stressed tissue such as muscle. Using skin fibroblasts from laminopathy patients and lamin A/C-deficient mouse embryonic fibroblasts stably expressing a broad panel of laminopathic lamin A mutations, we found that several mutations associated with muscular dystrophy and dilated cardiomyopathy resulted in more deformable nuclei; in contrast, lamin mutants responsible for diseases without muscular phenotypes did not alter nuclear deformability. We confirmed our results in intact muscle tissue, demonstrating that nuclei of transgenic Drosophila melanogaster muscle expressing myopathic lamin mutations deformed more under applied strain than controls. In vivo and in vitro studies indicated that the loss of nuclear stiffness resulted from impaired assembly of mutant lamins into the nuclear lamina. Although only a subset of lamin mutations associated with muscular diseases caused increased nuclear deformability, almost all mutations tested had defects in force transmission between the nucleus and cytoskeleton. In conclusion, our results indicate that although defective nuclear stability may play a role in the development of muscle diseases, other factors, such as impaired nucleo-cytoskeletal coupling, likely contribute to the muscle phenotype.
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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.