Myofilaments: Movers and Rulers of the Sarcomere. Compr Physiol 2017 Mar 16;7(2):675-692
Date
03/24/2017Pubmed ID
28333386DOI
10.1002/cphy.c160026Scopus ID
2-s2.0-85021039448 (requires institutional sign-in at Scopus site) 25 CitationsAbstract
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. © 2017 American Physiological Society. Compr Physiol 7:675-692, 2017.
Author List
Lin BL, Song T, Sadayappan SAuthor
Brian L. Lin PhD Assistant Professor in the Cell Biology, Neurobiology and Anatomy department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ConnectinHumans
Muscle Contraction
Muscle Proteins
Muscle, Skeletal
Myofibrils
Rho Guanine Nucleotide Exchange Factors
Sarcomeres
Troponin
