Journal
JOURNAL OF CELL BIOLOGY
Volume 177, Issue 2, Pages 205-210Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200607084
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Funding
- NIAMS NIH HHS [R01AR050051, R01 AR050051] Funding Source: Medline
- NIA NIH HHS [P30 AG024832] Funding Source: Medline
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Myosin motors are central to diverse cellular processes in eukaryotes. Homologues of the myosin chaperone UNC-45 have been implicated in the assembly and function of myosin-containing structures in organisms from fungi to humans. In muscle, the assembly of sarcomeric myosin is regulated to produce stable, uniform thick. laments. Loss-of-function mutations in Caenorhabditis elegans UNC-45 lead to decreased muscle myosin accumulation and defective thick. lament assembly, resulting in paralyzed animals. We report that transgenic worms overexpressing UNC-45 also display defects in myosin assembly, with decreased myosin content and a mild paralysis phenotype. We find that the reduced myosin accumulation is the result of degradation through the ubiquitin/proteasome system. Partial proteasome inhibition is able to restore myosin protein and worm motility to nearly wild-type levels. These findings suggest a mechanism in which UNC-45-related proteins may contribute to the degradation of myosin in conditions such as heart failure and muscle wasting.
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