ArticleProtein science : a publication of the Protein Society2021
Mutations in conserved residues of the myosin chaperone UNC-45 result in both reduced stability and chaperoning activity.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Distinct impacts of human co-chaperone UNC45 paralogs on Drosophila muscle development and function.Journal of cell science · 2025Article
- Hsf1 is essential for proteotoxic stress response in smyd1b-deficient embryos and fish survival under heat shock.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Optogenetic induction of mechanical muscle stress identifies myosin regulatory ubiquitin ligase NHL-1 in C. elegans.Nature communications · 2024Article
- The myosin chaperone UNC-45 has an important role in maintaining the structure and function of muscle sarcomeres during adult aging.Molecular biology of the cell · 2024Article
- SPR spectroscopic analysis of myosin binding to wild type and mutant UNC45B.microPublication biology · 2024Article
- 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
- Protein Quality Control at the Sarcomere: Titin Protection and Turnover and Implications for Disease Development.Frontiers in physiology · 2022Review
- Mutations in conserved residues of the myosin chaperone UNC-45 result in both reduced stability and chaperoning activity.Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Proper muscle development and function depend on myosin being properly folded and integrated into the thick filament structure. For this to occur the myosin chaperone UNC-45, or UNC-45B, must be present and able to chaperone myosin. Here we use a combination of in vivo C. elegans experiments and in vitro biophysical experiments to analyze the effects of six missense mutations in conserved regions of UNC-45/UNC-45B. We found that the phenotype of paralysis and disorganized thick filaments in 5/6 of the mutant nematode strains can likely be attributed to both reduced steady state UNC-45 protein levels and reduced chaperone activity. Interestingly, the biophysical assays performed on purified proteins show that all of the mutations result in reduced myosin chaperone activity but not overall protein stability. This suggests that these mutations only cause protein instability in the in vivo setting and that these conserved regions may be involved in UNC-45 protein stability/regulation via posttranslational modifications, protein-protein interactions, or some other unknown mechanism.
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