ArticleMolecular biology of the cell2004
Desmin aggregate formation by R120G alphaB-crystallin is caused by altered filament interactions and is dependent upon network status in cells.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 104 citations in OpenAlex.
- CryAB-driven amyloidogenesis iniScience · 2026Article
- Molecular Insights into Central Core Disease: Proteomic Signatures and Potential Therapeutic Biomarkers in RYR1 I4895T Mice.International journal of molecular sciences · 2025Article
- TANGO2 binds crystallin alpha B and its loss causes desminopathy.Nature communications · 2025Article
- Article
- 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
- The J Domain of Sacsin Disrupts Intermediate Filament Assembly.International journal of molecular sciences · 2022Article
- A novel dominant mutation in CRYAB gene leading to a severe phenotype with childhood onset.Molecular genetics & genomic medicine · 2020Article
- Molecular Chaperones and Proteolytic Machineries Regulate Protein Homeostasis In Aging Cells.Cells · 2020Review
- Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results.International journal of molecular sciences · 2020Review
- Review
- Drosophila Hsp67Bc hot-spot variants alter muscle structure and function.Cellular and molecular life sciences : CMLS · 2018Article
- Assembly Kinetics of Vimentin Tetramers to Unit-Length Filaments: A Stopped-Flow Study.Biophysical journal · 2018Article
- The growing world of small heat shock proteins: from structure to functions.Cell stress & chaperones · 2017Review
- αB-crystallin is a sensor for assembly intermediates and for the subunit topology of desmin intermediate filaments.Cell stress & chaperones · 2017Article
- Interaction of small heat shock proteins with light component of neurofilaments (NFL).Cell stress & chaperones · 2017Article
- A novel dominant D109ABBA clinical · 2017Article
- The Human 343delT HSPB5 Chaperone Associated with Early-onset Skeletal Myopathy Causes Defects in Protein Solubility.The Journal of biological chemistry · 2016Article
- Myofibrillar disruption and RNA-binding protein aggregation in a mouse model of limb-girdle muscular dystrophy 1D.Human molecular genetics · 2015Article
- Intermediate Filaments Play a Pivotal Role in Regulating Cell Architecture and Function.The Journal of biological chemistry · 2015Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The R120G mutation in alphaB-crystallin causes desmin-related myopathy. There have been a number of mechanisms proposed to explain the disease process, from altered protein processing to loss of chaperone function. Here, we show that the mutation alters the in vitro binding characteristics of alphaB-crystallin for desmin filaments. The apparent dissociation constant of R120G alphaB-crystallin was decreased while the binding capacity was increased significantly and as a result, desmin filaments aggregated. These data suggest that the characteristic desmin aggregates seen as part of the disease histopathology can be caused by a direct, but altered interaction of R120G alphaB-crystallin with desmin filaments. Transfection studies show that desmin networks in different cell backgrounds are not equally affected. Desmin networks are most vulnerable when they are being made de novo and not when they are already established. Our data also clearly demonstrate the beneficial role of wild-type alphaB-crystallin in the formation of desmin filament networks. Collectively, our data suggest that R120G alphaB-crystallin directly promotes desmin filament aggregation, although this gain of a function can be repressed by some cell situations. Such circumstances in muscle could explain the late onset characteristic of the myopathies caused by mutations in alphaB-crystallin.
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Registered trials
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.