期刊
FEBS LETTERS
卷 588, 期 21, 页码 3977-3981出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2014.09.013
关键词
Chaperone; UNC-45; Actin-translocation; Hsp90
资金
- American Heart Foundation (AHA) [13GRNT17290006]
- National Institutes of Health/National Institute on Aging [P30AG024832]
- Jeane B. Kempner Fellowship Foundation
- Ida and Cecil M. Green Endowment at the University of Texas Medical Branch
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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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