The chaperones UNC-45B and Hsp90 reversibly regulate the actin translocation function of sarcomeric myosin, potentially preventing premature powerstrokes during sarcomere assembly.
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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Nicholls et al. (2014) studied this question.
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