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Chaperone‐mediated reversible inhibition of the sarcomeric myosin power stroke
Author(s) -
Nicholls Paul,
Bujalowski Paul J.,
Epstein Henry F.,
Boehning Darren F.,
Barral José M.,
Oberhauser Andres F.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.09.013
Subject(s) - myosin , sarcomere , chaperone (clinical) , actin , microbiology and biotechnology , myosin head , chemistry , biology , myosin light chain kinase , myocyte , medicine , pathology
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.