Journal
BIOPHYSICAL JOURNAL
Volume 108, Issue 1, Pages 10-13Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2014.11.1852
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Funding
- National Science Foundation [DMS-1413185]
- Hellman Fellowship
- Direct For Mathematical & Physical Scien
- Division Of Mathematical Sciences [1413185] Funding Source: National Science Foundation
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Although mutations in cardiac myosin binding protein-C (cMyBP-C) cause heart disease, its role in muscle contraction is not well understood. A mechanism remains elusive partly because the protein can have multiple effects, such as dual biphasic activation and inhibition observed in actin motility assays. Here we develop a mathematical model for the interaction of cMyBP-C with the contractile proteins actin and myosin and the regulatory protein tropomyosin. We use this model to show that a drag-activation-competition mechanism accurately describes actin motility measurements, while models lacking either drag or competition do not. These results suggest that complex effects can arise simply from cMyBP-C binding to actin.
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