Chaperone-mediated reversible inhibition of the sarcomeric myosin power stroke |
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| Authors: | Paul Nicholls,Paul J. Bujalowski,Henry F. Epstein,Darren F. Boehning,José M. Barral,Andres F. Oberhauser |
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| Affiliation: | 1. Department of Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX, United States;2. Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, United States;3. Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX, United States;4. Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, TX, United States |
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| Abstract: | Molecular chaperones are required for successful folding and assembly of sarcomeric myosin in skeletal and cardiac muscle. Here, we show that the chaperone UNC-45B inhibits the actin translocation function of myosin. Further, we show that Hsp90, another chaperone involved in sarcomere development, allows the myosin to resume actin translocation. These previously unknown activities may play a key role in sarcomere development, preventing untimely myosin powerstrokes from disrupting the precise alignment of the sarcomere until it has formed completely. |
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| Keywords: | Chaperone UNC-45 Actin-translocation Hsp90 |
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