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Structure and Regulation of Cardiac and Skeletal Muscle Thin Filaments

  • Chapter
Molecular Control Mechanisms in Striated Muscle Contraction

Part of the book series: Advances in Muscle Research ((ADMR,volume 1))

Abstract

The biological production of force and movement can be understood only when it is considered as a molecular phenomenon, as has been recognized for many decades (Huxley, 1957). However, detailed molecular-scale investigations of this process had to await atomic resolution structures of the myosin molecular motor (Rayment et al., 1993). In striated muscles such as skeletal muscle and the heart, the primary regulation of myosin is by the reversible binding of Ca2+ to the thin filament. As was true for understanding myosin’s action, the understanding of myosin’s regulation requires detailed information about the structure of the relevant proteins: the thin filament and its components. These data are now increasingly available, thanks to the determined efforts of many investigators. Albeit incomplete, a molecular appreciation for how movement is controlled is now within reach. This review summarizes recent advances in the structures of actin, tropomyosin, troponin, and the assembled thin filament, focusing on how these results help explain the regulation of cardiac and skeletal muscle contraction, and on some of the questions that remain.

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  1. Departments of Internal Medicine and Biochemistry, The University of Iowa, Iowa City, Iowa, USA

    Larry S. Tobacman

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  1. University of Illinois at Chicago, Chicago, Illinois, USA

    R. John Solaro

  2. University of Wisconsin Medical School, Madison, Wisconsin, USA

    Richard L. Moss

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Tobacman, L.S. (2002). Structure and Regulation of Cardiac and Skeletal Muscle Thin Filaments. In: Solaro, R.J., Moss, R.L. (eds) Molecular Control Mechanisms in Striated Muscle Contraction. Advances in Muscle Research, vol 1. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-9926-9_4

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  • DOI: https://doi.org/10.1007/978-94-015-9926-9_4

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