C-terminal troponin-I residues trap tropomyosin in the muscle thin filament blocked-state.

ABSTRACT: Tropomyosin and troponin regulate muscle contraction by participating in a macromolecular scale steric-mechanism to control myosin-crossbridge - actin interactions and consequently contraction. At low-Ca²⁺, the C-terminal 30% of troponin subunit-I (TnI) is proposed to trap tropomyosin in a position on thin filaments that sterically interferes with myosin-binding, thus causing muscle relaxation. In contrast, at high-Ca²⁺, inhibition is released after the C-terminal domains dissociate from F-actin-tropomyosin as its component switch-peptide domain binds to the N-lobe of troponin-C (TnC). Recent, paradigm-shifting, cryo-EM reconstructions by the Namba group have revealed density attributed to TnI along cardiac muscle thin filaments at both low- and high-Ca²⁺ c

SUBMITTER: Lehman W 

PROVIDER: S-EPMC8026701 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature