ArticleFrontiers in molecular biosciences2014
Challenging muscle homeostasis uncovers novel chaperone interactions in Caenorhabditis elegans.
Article in Frontiers in molecular biosciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- Decoding Argonaute specificity: insights fromRNA (New York, N.Y.) · 2026Review
- Distinct impacts of human co-chaperone UNC45 paralogs on Drosophila muscle development and function.Journal of cell science · 2025Article
- Hetero-oligomerization of TDP-43 carboxy-terminal fragments with cellular proteins contributes to proteotoxicity.Communications biology · 2024Article
- Organismal Roles of Hsp90.Biomolecules · 2023Review
- Proteostasis and neurodegeneration: a closer look at autophagy in Alzheimer's disease.Frontiers in aging neuroscience · 2023Review
- Hsp90: From Cellular to Organismal Proteostasis.Cells · 2022Review
- UCS Chaperone Folding of the Myosin Head: A Function That Evolved before Animals and Fungi Diverged from a Common Ancestor More than a Billion Years Ago.Biomolecules · 2022Review
- Ageing induces tissue-specific transcriptomic changes in Caenorhabditis elegans.The EMBO journal · 2022Article
- HLH-1 Modulates Muscle Proteostasis DuringFrontiers in cell and developmental biology · 2022Article
- Maintaining proteostasis under mechanical stress.EMBO reports · 2021Review
- Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin.Nature communications · 2019Article
- The Molecular Chaperone HSP90 Promotes Notch Signaling in the Germline ofG3 (Bethesda, Md.) · 2018Article
- Uncoupling the Trade-Off between Somatic Proteostasis and Reproduction inFrontiers in molecular neuroscience · 2017Article
- A Differentiation Transcription Factor Establishes Muscle-Specific Proteostasis in Caenorhabditis elegans.PLoS genetics · 2016Article
- The struggle by Caenorhabditis elegans to maintain proteostasis during aging and disease.Biology direct · 2016Review
- A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel Cochaperone Aarsd1 Is Required for Muscle Differentiation.Molecular and cellular biology · 2016Article
- Still Heart Encodes a Structural HMT, SMYD1b, with Chaperone-Like Function during Fast Muscle Sarcomere Assembly.PloS one · 2015Article
- The Hsp90 ensemble: coordinated Hsp90-cochaperone complexes regulate diverse cellular processes.Nature structural & molecular biology · 2014Article
- Gene expression and functional analysis of Aha1a and Aha1b in stress response in zebrafish.Comparative biochemistry and physiology. Part B, Biochemistry & molecular biologyArticle
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Proteome stability is central to cellular function and the lifespan of an organism. This is apparent in muscle cells, where incorrect folding and assembly of the sarcomere contributes to disease and aging. Apart from the myosin-assembly factor UNC-45, the complete network of chaperones involved in assembly and maintenance of muscle tissue is currently unknown. To identify additional factors required for sarcomere quality control, we performed genetic screens based on suppressed or synthetic motility defects in Caenorhabditis elegans. In addition to ethyl methyl sulfonate-based mutagenesis, we employed RNAi-mediated knockdown of candidate chaperones in unc-45 temperature-sensitive mutants and screened for impaired movement at permissive conditions. This approach confirmed the cooperation between UNC-45 and Hsp90. Moreover, the screens identified three novel co-chaperones, CeHop (STI-1), CeAha1 (C01G10.8) and Cep23 (ZC395.10), required for muscle integrity. The specific identification of Hsp90 and Hsp90 co-chaperones highlights the physiological role of Hsp90 in myosin folding. Our work thus provides a clear example of how a combination of mild perturbations to the proteostasis network can uncover specific quality control modules.
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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.