ArticleProceedings of the National Academy of Sciences of the United States of America2005
Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 132 citations in OpenAlex.
- Differential proteomic analysis of abnormal intramyoplasmic aggregates in desminopathy.Journal of proteomics · 2013Trial
- Chaperone proteins protect against desmin fragment amyloid aggregation.Biophysical journal · 2026Article
- The myofibrillar myopathy-linked variant DES-p.T341P impairs desmin filament assembly.Molecular biology reports · 2026Article
- Identification and Functional Analysis of Dual Nuclear Localization Signals on Desmin.ACS omega · 2026Article
- Evaluation of aggrephagy markers in myofibrillar myopathies.Acta neuropathologica communications · 2025Article
- Functional impact of the head domain variants ofGenes & diseases · 2025Article
- Dominantly inherited muscle disorders: understanding their complexity and exploring therapeutic approaches.Disease models & mechanisms · 2024Review
- Desmin mutations impact the autophagy flux in C2C12 cell in mutation-specific manner.Cell and tissue research · 2023Article
- Article
- Structural and signaling proteins in the Z-disk and their role in cardiomyopathies.Frontiers in physiology · 2023Review
- The N-Terminal Part of the 1A Domain of Desmin Is a Hot Spot Region for Putative PathogenicCells · 2022Article
- Effects of Alexander disease-associated mutations on the assembly and organization of GFAP intermediate filaments.Molecular biology of the cell · 2022Article
- Genetic Insights into Primary Restrictive Cardiomyopathy.Journal of clinical medicine · 2022Review
- Case report: Whole-exome sequencing identifies a novelFrontiers in cardiovascular medicine · 2022Article
- The Desmin MutationBiomedicines · 2021Article
- Striated Preferentially Expressed Protein Kinase (SPEG) in Muscle Development, Function, and Disease.International journal of molecular sciences · 2021Review
- SPEG binds with desmin and its deficiency causes defects in triad and focal adhesion proteins.Human molecular genetics · 2021Article
- The Desmin (Genes · 2021Article
- The unified myofibrillar matrix for force generation in muscle.Nature communications · 2020Article
- Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Desmin is the major intermediate filament (IF) protein of muscle. Recently, mutations of the desmin gene have been reported to cause familial or sporadic forms of human skeletal, as well as cardiac, myopathy, termed desmin-related myopathy (DRM). The impact of any of these mutations on filament assembly and integration into the cytoskeletal network of myocytes is currently not understood, despite the fact that all cause the same histopathological defect, i.e., desmin aggregation. To gain more insight into the molecular basis of this process, we investigated how mutations within the alpha-helical rod domain of desmin affect both the assembly of the recombinant protein in vitro as well as the filament-forming capacity in cDNA-transfected cells. Whereas 6 of 14 mutants assemble into seemingly normal IFs in the test tube, the other mutants interfere with the assembly process at distinct stages, i.e., tetramer formation, unit-length filament (ULF) formation, filament elongation, and IF maturation. Correspondingly, the mutants with in vitro assembly defects yield dot-like aggregates in transfected cells, whereas the mutants that form IFs constitute a seemingly normal IF cytoskeleton in the cellular context. At present, it is entirely unclear why the latter mutant proteins also lead to aggregate formation in myocytes. Hence, these findings may be a starting point to dissect the contribution of the individual subdomains for desmin pathology and, eventually, the development of therapeutic interventions.
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