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Structural Biochemistry of Muscle Contraction.

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Muscles are essential for movement and heart function. Contraction and relaxation of muscles relies on the sliding of two types of filaments-the thin filament and the thick myosin filament. The… Click to show full abstract

Muscles are essential for movement and heart function. Contraction and relaxation of muscles relies 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. Expected final online publication date for the Annual Review of Biochemistry, Volume 92 is June 2023. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

Keywords: structural biochemistry; biochemistry muscle; muscle; muscle contraction; biochemistry

Journal Title: Annual review of biochemistry
Year Published: 2023

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