What is it about?
The control scheme for lengthdependent activation (LDA), a fundamental, striated muscle property where submaximal contraction is improved at longer compared to shorter lengths, is poorly understood. We demonstrate that 50% titin cleavage in passive sarcomeres attenuates all measured structural markers of LDA for thick (e.g., myosin) and thin (e.g., actin, troponin) filaments, as well as a functionally required thick-thin filament bridge in the A-band. These culminate to attenuate LDA in contracting fibers. The identified regulatory role of titin to LDA structural features is critical to the future study of many myo- and cardiomyopathies, of which LDA impairment is a hallmark.
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Why is it important?
The identified regulatory role of titin to muscle function and performance is critical to the future study of many myo- and cardiomyopathies.
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This page is a summary of: Titin force in muscle cells alters lattice order, thick and thin filament protein formation, Proceedings of the National Academy of Sciences, November 2022, Proceedings of the National Academy of Sciences, DOI: 10.1073/pnas.2209441119.
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