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

Whitten, Andrew E., Jeffries, Cy M., Harris, Samantha P. and Trewhella, Jill (2008) Cardiac myosin-binding protein C decorates F-actin: Implications for cardiac function. National Academy of Sciences. Proceedings, 105 47: 18360-18365. doi:10.1073/pnas.0808903105

Author Whitten, Andrew E.
Jeffries, Cy M.
Harris, Samantha P.
Trewhella, Jill
Title Cardiac myosin-binding protein C decorates F-actin: Implications for cardiac function
Journal name National Academy of Sciences. Proceedings   Check publisher's open access policy
ISSN 0027-8424
Publication date 2008-11-25
Sub-type Article (original research)
DOI 10.1073/pnas.0808903105
Open Access Status Not Open Access
Volume 105
Issue 47
Start page 18360
End page 18365
Total pages 6
Place of publication Washington, D.C., U.S.A.
Publisher National Academy of Sciences of the U.S.
Language eng
Subject 0601 Biochemistry and Cell Biology
Formatted 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.
© 2008 by The National Academy of Sciences of the USA
Keyword Familial hypertrophic cardiomypathy
C protein
Neutron contrast variation
Muscle regulation
Small-angle scattering
Q-Index Code C1
Q-Index Status Provisional Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 66 times in Thomson Reuters Web of Science Article | Citations
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Created: Fri, 19 Feb 2010, 21:45:58 EST by Sue Green on behalf of Institute for Molecular Bioscience