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Published online
doi:10.1083/jcb.200607084
The Journal of Cell Biology, Vol. 177, No. 2, 205-210
The Rockefeller University Press, 0021-9525 $30.00
© Landsverk et al.
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The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans



Megan L. Landsverk1,2, Shumin Li1, Alex H. Hutagalung2, Ayaz Najafov1, Thorsten Hoppe3, José M. Barral1, and Henry F. Epstein1

1 Department of Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX 77555
2 The Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030
3 Centre for Molecular Neurobiology, University of Hamburg, 20251 Hamburg, Germany

Correspondence to Henry F. Epstein: hepstein{at}utmb.edu

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 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.

M.L. Landsverk and S. Li contributed equally to this paper.

A.H. Hutagalung's present address is Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520.

Abbreviations used in this paper: Lof, loss-of-function; MHC, myosin heavy chain; UCS, UNC-45/Cro1p/She4p(Dim1p) domain; UPS, ubiquitin/proteasome system; Ya, young adult.


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