Key result
The sarcomeric cytoskeleton, including α-actinin and myomesin crosslinks, is essential for dissipating mechanical forces and maintaining sarcomere integrity during passive extension and active contraction.
Provides structural and biophysical insights into how sarcomeric cytoskeleton proteins maintain sarcomere integrity during muscle contraction.
Sarcomere cytoskeletal insights may inform cardiomyopathy mechanisms; extends experimental models but leaves open clinical translation.
Highly ordered organisation of striated muscle is the prerequisite for the fast and unidirectional development of force and motion during heart and skeletal muscle contraction. A group of proteins, summarised as the sarcomeric cytoskeleton, is essential for the ordered assembly of actin and myosin filaments into sarcomeres, by combining architectural, mechanical and signalling functions. This review discusses recent cell biological, biophysical and structural insight into the regulated assembly of sarcomeric cytoskeleton proteins and their roles in dissipating mechanical forces in order to maintain sarcomere integrity during passive extension and active contraction. α-Actinin crosslinks in the Z-disk show a pivot-and-rod structure that anchors both titin and actin filaments. In contrast, the myosin crosslinks formed by myomesin in the M-band are of a ball-and-spring type and may be crucial in providing stable yet elastic connections during active contractions, especially eccentric exercise.
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Gautel et al. (2016) conducted a review in Muscle contraction and sarcomere integrity. The sarcomeric cytoskeleton, including α-actinin and myomesin crosslinks, is essential for dissipating mechanical forces and maintaining sarcomere integrity during passive extension and active contraction.
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