ArticlePloS one2011
Downregulation of the Hsp90 system causes defects in muscle cells of Caenorhabditis elegans.
Article in PloS one, 2011. 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.
- Proteostasis and ageing dissidence.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Distinct impacts of human co-chaperone UNC45 paralogs on Drosophila muscle development and function.Journal of cell science · 2025Article
- Decreased Hsp90 activity protects against TDP-43 neurotoxicity in a C. elegans model of amyotrophic lateral sclerosis.PLoS genetics · 2024Article
- Optogenetic induction of mechanical muscle stress identifies myosin regulatory ubiquitin ligase NHL-1 in C. elegans.Nature communications · 2024Article
- Article
- Heat Shock Proteins: Important Helpers for the Development, Maintenance and Regeneration of Skeletal Muscles.Muscles (Basel, Switzerland) · 2023Review
- Regulation of TFEB nuclear localization by HSP90AA1 promotes autophagy and longevity.Autophagy · 2023Article
- Transcellular chaperone signaling is an intercellular stress-response distinct from the HSF-1-mediated heat shock response.PLoS biology · 2023Article
- Organismal Roles of Hsp90.Biomolecules · 2023Review
- A ubiquitin fusion reporter to monitor muscle proteostasis inmicroPublication biology · 2023Article
- Binding of the HSF-1 DNA-binding domain to multimeric C. elegans consensus HSEs is guided by cooperative interactions.Scientific reports · 2022Article
- Protein Quality Control at the Sarcomere: Titin Protection and Turnover and Implications for Disease Development.Frontiers in physiology · 2022Review
- Maintaining proteostasis under mechanical stress.EMBO reports · 2021Review
- hsp-90 and unc-45 depletion induce characteristic transcriptional signatures in coexpression cliques of C. elegans.Scientific reports · 2021Article
- Nitrosative Redox Homeostasis and Antioxidant Response Defense in DisusedAntioxidants (Basel, Switzerland) · 2021Article
- Article
- Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin.Nature communications · 2019Article
- Hsp90 Stabilizes SIRT1 Orthologs in Mammalian Cells andInternational journal of molecular sciences · 2018Article
- DAF-21/Hsp90 is required for C. elegans longevity by ensuring DAF-16/FOXO isoform A function.Scientific reports · 2018Article
- The Molecular Chaperone HSP90 Promotes Notch Signaling in the Germline ofG3 (Bethesda, Md.) · 2018Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ATP-dependent molecular chaperone Hsp90 is required for the activation of a variety of client proteins involved in various cellular processes. Despite the abundance of known client proteins, functions of Hsp90 in the organismal context are not fully explored. In Caenorhabditis elegans, Hsp90 (DAF-21) has been implicated in the regulation of the stress-resistant dauer state, in chemosensing and in gonad formation. In a C. elegans strain carrying a DAF-21 mutation with a lower ATP turnover, we observed motility defects. Similarly, a reduction of DAF-21 levels in wild type nematodes leads to reduced motility and induction of the muscular stress response. Furthermore, aggregates of the myosin MYO-3 are visible in muscle cells, if DAF-21 is depleted, implying a role of Hsp90 in the maintenance of muscle cell functionality. Similar defects can also be observed upon knockdown of the Hsp90-cochaperone UNC-45. In life nematodes YFP-DAF-21 localizes to the I-band and the M-line of the muscular ultrastructure, but the protein is not stably attached there. The Hsp90-cofactor UNC-45-CFP contrarily can be found in all bands of the nematode muscle ultrastructure and stably associates with the UNC-54 containing A-band. Thus, despite the physical interaction between DAF-21 and UNC-45, apparently the two proteins are not always localized to the same muscular structures. While UNC-45 can stably bind to myofilaments in the muscular ultrastructure, Hsp90 (DAF-21) appears to participate in the maintenance of muscle structures as a transiently associated diffusible factor.
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