Chaperone-mediated reversible inhibition of the sarcomeric myosin power stroke

•The chaperone UNC-45B is involved in myosin folding and associates with thick filaments.•UNC-45B inhibits the ability of myosin to translocate actin.•This effect inhibits the power stroke but not the myosin ATPase.•The co-chaperone Hsp90 alleviates the inhibitory effect, interacting with the UNC-45...

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Bibliographic Details
Published in:FEBS letters 2014-11, Vol.588 (21), p.3977-3981
Main Authors: Nicholls, Paul, Bujalowski, Paul J., Epstein, Henry F., Boehning, Darren F., Barral, José M., Oberhauser, Andres F.
Format: Article
Language:English
Subjects:
Actin-translocation
Actins - metabolism
Adenosine Triphosphatases - metabolism
Animals
Chaperone
Hsp90
HSP90 Heat-Shock Proteins - metabolism
Humans
Intracellular Signaling Peptides and Proteins - chemistry
Intracellular Signaling Peptides and Proteins - metabolism
Mice
Movement
Myosins - metabolism
Protein Structure, Tertiary
Rabbits
Sarcomeres - metabolism
UNC-45
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Summary:•The chaperone UNC-45B is involved in myosin folding and associates with thick filaments.•UNC-45B inhibits the ability of myosin to translocate actin.•This effect inhibits the power stroke but not the myosin ATPase.•The co-chaperone Hsp90 alleviates the inhibitory effect, interacting with the UNC-45B TPR domain. 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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2014.09.013