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

15 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Cardiac Myosins
Actins
Contractile Proteins
Tropomyosin
Myosins
Muscle Contraction
Protein Binding
Heart Diseases
Proteins
Theoretical Models
Mutation
myosin-binding protein C

ASJC Scopus subject areas

  • Biophysics

Cite this

Effects of cardiac myosin binding protein-C on actin motility are explained with a drag-activation-competition model. / Walcott, Sam; Docken, Steffen; Harris, Samantha P.

In: Biophysical Journal, Vol. 108, No. 1, 06.01.2015, p. 10-13.

Research output: Contribution to journalArticle

Walcott, Sam ; Docken, Steffen ; Harris, Samantha P. / Effects of cardiac myosin binding protein-C on actin motility are explained with a drag-activation-competition model. In: Biophysical Journal. 2015 ; Vol. 108, No. 1. pp. 10-13.
@article{4e0414e0404b43bc915f018bd2d5c786,
title = "Effects of cardiac myosin binding protein-C on actin motility are explained with a drag-activation-competition model",
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.",
author = "Sam Walcott and Steffen Docken and Harris, {Samantha P.}",
year = "2015",
month = "1",
day = "6",
doi = "10.1016/j.bpj.2014.11.1852",
language = "English (US)",
volume = "108",
pages = "10--13",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "1",

}

TY - JOUR

T1 - Effects of cardiac myosin binding protein-C on actin motility are explained with a drag-activation-competition model

AU - Walcott, Sam

AU - Docken, Steffen

AU - Harris, Samantha P.

PY - 2015/1/6

Y1 - 2015/1/6

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84921024869&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84921024869&partnerID=8YFLogxK

U2 - 10.1016/j.bpj.2014.11.1852

DO - 10.1016/j.bpj.2014.11.1852

M3 - Article

C2 - 25564844

AN - SCOPUS:84921024869

VL - 108

SP - 10

EP - 13

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 1

ER -