A gain-of-function mutation in the M-domain of cardiac myosin-binding protein-C increases binding to actin

Kristina L. Bezold, Justin F. Shaffer, Jaskiran K. Khosa, Elaine R. Hoye, Samantha P. Harris

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Background: Cardiac myosin-binding protein C (cMyBP-C) regulates heart muscle contraction by influencing actomyosin interactions. Results: Amino acids within the tri-helix bundle of the M-domain contribute to the functional effects of cMyBP-C. Conclusion: Amino acids outside of phosphorylation sites influence function of the M-domain. Significance: The tri-helix bundle is important to the regulatory role of cMyBP-C, likely through actin-binding interactions.

Original languageEnglish (US)
Pages (from-to)21496-21505
Number of pages10
JournalJournal of Biological Chemistry
Volume288
Issue number30
DOIs
StatePublished - Jul 26 2013

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Cardiac Myosins
Actins
Amino Acids
Actomyosin
Mutation
Phosphorylation
Muscle Contraction
Muscle
Myocardium
myosin-binding protein C

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

A gain-of-function mutation in the M-domain of cardiac myosin-binding protein-C increases binding to actin. / Bezold, Kristina L.; Shaffer, Justin F.; Khosa, Jaskiran K.; Hoye, Elaine R.; Harris, Samantha P.

In: Journal of Biological Chemistry, Vol. 288, No. 30, 26.07.2013, p. 21496-21505.

Research output: Contribution to journalArticle

Bezold, Kristina L. ; Shaffer, Justin F. ; Khosa, Jaskiran K. ; Hoye, Elaine R. ; Harris, Samantha P. / A gain-of-function mutation in the M-domain of cardiac myosin-binding protein-C increases binding to actin. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 30. pp. 21496-21505.
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