Cardiac myosin-binding protein C decorates F-actin: Implications for cardiac function

Andrew E. Whitten, Cy M. Jeffries, Samantha P. Harris, Jill Trewhella

Research output: Contribution to journalArticle

90 Scopus citations

Abstract

Cardiac myosin-binding protein C (cMyBP-C) is an accessory protein of striated muscle sarcomeres that is vital for maintaining regular heart function. Its 4 N-terminal regulatory domains, C0-C1-m-C2 (C0C2), influence actin and myosin interactions, the basic contractile proteins of muscle. Using neutron contrast variation data, we have determined that C0C2 forms a repeating assembly with filamentous actin, where the C0 and C1 domains of C0C2 attach near the DNase I-binding loop and subdomain 1 of adjacent actin monomers. Direct interactions between the N terminus of cMyBP-C and actin thereby provide a mechanism to modulate the contractile cycle by affecting the regulatory state of the thin filament and its ability to interact with myosin.

Original languageEnglish (US)
Pages (from-to)18360-18365
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume105
Issue number47
DOIs
StatePublished - Nov 25 2008
Externally publishedYes

Keywords

  • C protein
  • Familial hypertrophic cardiomypathy
  • Muscle regulation
  • Neutron contrast variation
  • Small-angle scattering

ASJC Scopus subject areas

  • General

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