ArticleScientific reports2018
Characterization of human small heat shock protein HSPB1 α-crystallin domain localized mutants associated with hereditary motor neuron diseases.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 40 citations in OpenAlex.
- Neuropathy-Associated HSPB1 Mutant Impairs Neuronal Mechanoadaptation and Axonal Regeneration.Cells · 2026Article
- Polymorphisms in Necroptosis Pathway Genes: Novel Prognostic Markers for Multiple Myeloma Treatment Outcomes.International journal of molecular sciences · 2025Article
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- Identification of Novel CSF-Derived miRNAs in Treated Paediatric Onset Spinal Muscular Atrophy: An Exploratory Study.Pharmaceutics · 2023Article
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- Human HspB1, HspB3, HspB5 and HspB8: Shaping these disease factors during vertebrate evolution.Cell stress & chaperones · 2022Article
- The role of BAG3 in dilated cardiomyopathy and its association with Charcot-Marie-Tooth disease type 2.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2022Review
- Autologous treatment for ALS with implication for broad neuroprotection.Translational neurodegeneration · 2022Article
- A molecular view of amyotrophic lateral sclerosis through the lens of interaction network modules.PloS one · 2022Article
- Insights Into the Role of Heat Shock Protein 27 in the Development of Neurodegeneration.Frontiers in molecular neuroscience · 2022Review
- Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.Nature communications · 2021Article
- The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70.Scientific reports · 2021Article
- Article
- A weakened interface in the P182L variant of HSP27 associated with severe Charcot-Marie-Tooth neuropathy causes aberrant binding to interacting proteins.The EMBO journal · 2021Article
- Impaired Mitochondrial Mobility in Charcot-Marie-Tooth Disease.Frontiers in cell and developmental biology · 2021Article
- Mutations in HspB1 and hereditary neuropathies.Cell stress & chaperones · 2020Review
- Small heat-shock proteins and their role in mechanical stress.Cell stress & chaperones · 2020Review
- The Heterooligomerization of Human Small Heat Shock Proteins Is Controlled by Conserved Motif Located in the N-Terminal Domain.International journal of molecular sciences · 2020Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Congenital mutations in human small heat shock protein HSPB1 (HSP27) have been linked to Charcot-Marie-Tooth disease, a commonly occurring peripheral neuropathy. Understanding the molecular mechanism of such mutations is indispensable towards developing future therapies for this currently incurable disorder. Here we describe the physico-chemical properties of the autosomal dominant HSPB1 mutants R127W, S135F and R136W. Despite having a nominal effect on thermal stability, the three mutations induce dramatic changes to quaternary structure. At high concentrations or under crowding conditions, the mutants form assemblies that are approximately two times larger than those formed by the wild-type protein. At low concentrations, the mutants have a higher propensity to dissociate into small oligomers, while the dissociation of R127W and R135F mutants is enhanced by MAPKAP kinase-2 mediated phosphorylation. Specific differences are observed in the ability to form hetero-oligomers with the homologue HSPB6 (HSP20). For wild-type HSPB1 this only occurs at or above physiological temperature, whereas the R127W and S135F mutants form hetero-oligomers with HSPB6 at 4 °C, and the R136W mutant fails to form hetero-oligomers. Combined, the results suggest that the disease-related mutations of HSPB1 modify its self-assembly and interaction with partner proteins thus affecting normal functioning of HSPB1 in the cell.
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