Structural Biochemistry of Muscle Contraction.

IF 12.1 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Annual review of biochemistry Pub Date : 2023-06-20 DOI:10.1146/annurev-biochem-052521-042909
Zhexin Wang, Stefan Raunser
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引用次数: 3

Abstract

Muscles are essential for movement and heart function. Contraction and relaxation of muscles rely on the sliding of two types of filaments-the thin filament and the thick myosin filament. The thin filament is composed mainly of filamentous actin (F-actin), tropomyosin, and troponin. Additionally, several other proteins are involved in the contraction mechanism, and their malfunction can lead to diverse muscle diseases, such as cardiomyopathies. We review recent high-resolution structural data that explain the mechanism of action of muscle proteins at an unprecedented level of molecular detail. We focus on the molecular structures of the components of the thin and thick filaments and highlight the mechanisms underlying force generation through actin-myosin interactions, as well as Ca2+-dependent regulation via the dihydropyridine receptor, the ryanodine receptor, and troponin. We particularly emphasize the impact of cryo-electron microscopy and cryo-electron tomography in leading muscle research into a new era.

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肌肉收缩的结构生物化学。
肌肉对运动和心脏功能至关重要。肌肉的收缩和松弛依赖于两种纤维的滑动——细纤维和粗肌球蛋白纤维。细丝主要由丝状肌动蛋白(F-actin)、原肌球蛋白和肌钙蛋白组成。此外,其他几种蛋白质也参与收缩机制,它们的功能障碍可导致多种肌肉疾病,如心肌病。我们回顾了最近的高分辨率结构数据,这些数据在前所未有的分子细节水平上解释了肌肉蛋白的作用机制。我们专注于细纤维和粗纤维成分的分子结构,并强调通过肌动蛋白-肌球蛋白相互作用产生力的机制,以及通过二氢吡啶受体、红嘌呤受体和肌钙蛋白进行的Ca2+依赖性调节。我们特别强调低温电子显微镜和低温电子断层扫描在引领肌肉研究进入新时代的影响。
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来源期刊
Annual review of biochemistry
Annual review of biochemistry 生物-生化与分子生物学
CiteScore
33.90
自引率
0.00%
发文量
31
期刊介绍: The Annual Review of Biochemistry, in publication since 1932, sets the standard for review articles in biological chemistry and molecular biology. Since its inception, these volumes have served as an indispensable resource for both the practicing biochemist and students of biochemistry.
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