期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 108, 期 28, 页码 11423-11428出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1103216108
关键词
protein; sarcomere structure; thick filament structure; cardiac muscle regulation; cardiac disease
资金
- British Heart Foundation [PG/06/010]
- National Institutes of Health (NIH) [R01 AR034711, R01 GM030598, P01 HL059408]
- Howard Hughes Medical Institute (HHMI) [55005953]
- FONACIT (Fondo Nacional de Ciencia y Tecnologia)
- NIH [P41 RR-01081]
Myosin-binding protein C (MyBP-C) is a thick filament protein playing an essential role in muscle contraction, and MyBP-C mutations cause heart and skeletal muscle disease in millions worldwide. Despite its discovery 40 y ago, the mechanism of MyBP-C function remains unknown. In vitro studies suggest that MyBP-C could regulate contraction in a unique way-by bridging thick and thin filaments-but there has been no evidence for this in vivo. Here we use electron tomography of exceptionally well preserved muscle to demonstrate that MyBP-C does indeed bind to actin in intact muscle. This binding implies a physical mechanism for communicating the relative sliding between thick and thin filaments that does not involve myosin and which could modulate the contractile process.
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