Abstract
While the strength of contraction in our muscles is activated by the frequency of action potentials in its efferent nerves, this chapter is concerned with the way in which calcium ions released by the transverse-tubule system regulate contraction via the thin filament. Each strand of the actin double helix is regulated by overlapping tropomyosin-troponin units, and theories of thin-filament Ca2+-regulation have evolved from seven-site regulation by independent Tm-Tn units switching between two states (the original steric blocking model) or three states (blocked, closed and open), to models with end-to-end Tm interactions. Recent structural studies point to an alternative model in which Tm-Tn protomers join to form a continuous flexible chain (CFC). This chapter presents a quantitative version of the chain model, in which myosin binding in the absence of calcium is blocked by TnI bound to actin. Calcium binding to TnC releases TnI, which allows the chain to make angular Brownian fluctuations about the closed state, from which myosin binding pushes the chain out to a local open state. These models have been tested by solution experiments.
Keywords
Cooperation is the best form of regulation. anon.
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Aitchison Smith, D. (2018). Models of Thin-Filament Regulation. In: The Sliding-Filament Theory of Muscle Contraction. Springer, Cham. https://doi.org/10.1007/978-3-030-03526-6_7
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