期刊
ELIFE
卷 10, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.68211
关键词
-
类别
资金
- Medical Research Council [MR/R01700X/1]
- Diamond Light Source [SM21316-1]
- British Heart Foundation [FS/17/3/32604]
- Wellcome Trust [210464/Z/18/Z]
- Royal Society [210464/Z/18/Z]
- Wellcome Trust [210464/Z/18/Z] Funding Source: Wellcome Trust
- MRC [MR/R01700X/1] Funding Source: UKRI
The study revealed a sequence of structural changes during muscle activation, including thin filament activation, disruption of the helical array of myosin motors, release of myosin motor domains from the folded conformation, and actin attachment. Physiological force generation in skeletal muscle twitch response is limited by incomplete activation of the thick filament and rapid inactivation of both filaments.
Time-resolved X-ray diffraction of isolated fast-twitch muscles of mice was used to show how structural changes in the myosin-containing thick filaments contribute to the regulation of muscle contraction, extending the previous focus on regulation by the actin-containing thin filaments. This study shows that muscle activation involves the following sequence of structural changes: thin filament activation, disruption of the helical array of myosin motors characteristic of resting muscle, release of myosin motor domains from the folded conformation on the filament backbone, and actin attachment. Physiological force generation in the 'twitch' response of skeletal muscle to single action potential stimulation is limited by incomplete activation of the thick filament and the rapid inactivation of both filaments. Muscle relaxation after repetitive stimulation is accompanied by a complete recovery of the folded motor conformation on the filament backbone but by incomplete reformation of the helical array, revealing a structural basis for post-tetanic potentiation in isolated muscles.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据