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

doi:10.1074/jbc.M113.474346

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 journal › Article › peer-review

30 Scopus citations

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 language	English (US)
Pages (from-to)	21496-21505
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	288
Issue number	30
DOIs	https://doi.org/10.1074/jbc.M113.474346
State	Published - Jul 26 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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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.",

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AU - Bezold, Kristina L.

AU - Shaffer, Justin F.

AU - Khosa, Jaskiran K.

AU - Hoye, Elaine R.

AU - Harris, Samantha P.

PY - 2013/7/26

Y1 - 2013/7/26

N2 - 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.

AB - 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.

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

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