Key result
Review details less-characterized sarcomere proteins like titin and obscurin in striated muscle contraction.
This review highlights the structural and regulatory roles of lesser-characterized myofilaments in striated muscle contraction.
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Synthesizes roles of understudied myofilaments in contraction; extends basic insight but leaves clinical translation open.
Striated cardiac and skeletal muscles play very different roles in the body, but they are similar at the molecular level. In particular, contraction, regardless of the type of muscle, is a precise and complex process involving the integral protein myofilaments and their associated regulatory components. The smallest functional unit of muscle contraction is the sarcomere. Within the sarcomere can be found a sophisticated ensemble of proteins associated with the thick filaments (myosin, myosin binding protein-C, titin, and obscurin) and thin myofilaments (actin, troponin, tropomyosin, nebulin, and nebulette). These parallel thick and thin filaments slide across one another, pulling the two ends of the sarcomere together to regulate contraction. More specifically, the regulation of both timing and force of contraction is accomplished through an intricate network of intra- and interfilament interactions belonging to each myofilament. This review introduces the sarcomere proteins involved in striated muscle contraction and places greater emphasis on the more recently identified and less well-characterized myofilaments: cardiac myosin binding protein-C, titin, nebulin, and obscurin.
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Lin et al. (2017) conducted a review in Striated muscle contraction. This review details sarcomere proteins in striated muscle contraction, emphasizing less well-characterized myofilaments like cardiac myosin binding protein-C, titin, nebulin, and obscurin.
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