Effects of cardiac myosin binding protein-C on actin motility are explained with a drag-activation-competition model

Sam Walcott, Steffen Docken, Samantha P. Harris

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)10-13
Number of pages4
JournalBiophysical Journal
Volume108
Issue number1
DOIs
StatePublished - Jan 6 2015

ASJC Scopus subject areas

  • Biophysics

Fingerprint Dive into the research topics of 'Effects of cardiac myosin binding protein-C on actin motility are explained with a drag-activation-competition model'. Together they form a unique fingerprint.

  • Cite this