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• W2893130223 abstract "Muscle contraction relies on interaction between myosin-based thick filaments and actin-based thin filaments. Myosin binding protein C (MyBP-C) is a key regulator of actomyosin interactions. Recent studies established that the N'-terminal domains (NTDs) of MyBP-C can either activate or inhibit thin filaments, but the mechanism of their collective action is poorly understood. Cardiac MyBP-C (cMyBP-C) harbors an extra NTD, which is absent in skeletal isoforms of MyBP-C, and its role in regulation of cardiac contraction is unknown. Here we show that the first two domains of human cMyPB-C (i.e., C0 and C1) cooperate to activate the thin filament. We demonstrate that C1 interacts with tropomyosin via a positively charged loop and that this interaction, stabilized by the C0 domain, is required for thin filament activation by cMyBP-C. Our data reveal a mechanism by which cMyBP-C can modulate cardiac contraction and demonstrate a function of the C0 domain." @default.
• W2893130223 created "2018-10-05" @default.
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• W2893130223 date "2018-12-01" @default.
• W2893130223 modified "2023-10-13" @default.
• W2893130223 title "N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament" @default.
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• W2893130223 doi "https://doi.org/10.1016/j.str.2018.08.007" @default.
• W2893130223 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6281772" @default.
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