The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans.

ABSTRACT: 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 filaments. Loss-of-function mutations in Caenorhabditis elegans UNC-45 lead to decreased muscle myosin accumulation and defective thick filament 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 i

SUBMITTER: Landsverk ML 

PROVIDER: S-EPMC2064129 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature