Tropomyosin and the steric mechanism of muscle regulation.
Contraction in all muscles must be precisely regulated and requisite control systems must be able to adjust to changes in physiological and myopathic stimuli. In this chapter, we outline the structural evidence for a steric mechanism that governs muscle activity. The mechanism involves calcium and myosin induced changes in the position of tropomyosin along actin-based thin filaments. This process either blocks or uncovers myosin crossbridge binding sites on actin and consequently regulates crossbridge cycling on thin filaments, the sliding of thin and thick filaments and muscle shortening and force production.
Lehman
William
W
Department of Physiology and Biophysics, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118, USA. wlehman@bu.edu
Craig
Roger
R
D008841:Actin Cytoskeleton / Q000737:chemistry; D000199:Actins / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D002118:Calcium / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008954:Models, Biological; D008958:Models, Molecular; D008968:Molecular Conformation; D009132:Muscles / Q000502:physiology*; D009218:Myosins / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D014335:Tropomyosin / Q000737:chemistry*
D000199:Actins; D014335:Tropomyosin; D000255:Adenosine Triphosphate; D009218:Myosins; D002118:Calcium