Molecular consequences of the myopathy-related D286G mutation on actin function

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Standard

Molecular consequences of the myopathy-related D286G mutation on actin function. / Fan, Jun; Chan, Chun; McNamara, Elyshia L.; Nowak, Kristen J.; Iwamoto, Hiroyuki; Ochala, Julien.

I: Frontiers in Physiology, Bind 9, 1756, 01.12.2018.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Fan, J, Chan, C, McNamara, EL, Nowak, KJ, Iwamoto, H & Ochala, J 2018, 'Molecular consequences of the myopathy-related D286G mutation on actin function', Frontiers in Physiology, bind 9, 1756. https://doi.org/10.3389/fphys.2018.01756

APA

Fan, J., Chan, C., McNamara, E. L., Nowak, K. J., Iwamoto, H., & Ochala, J. (2018). Molecular consequences of the myopathy-related D286G mutation on actin function. Frontiers in Physiology, 9, [1756]. https://doi.org/10.3389/fphys.2018.01756

Vancouver

Fan J, Chan C, McNamara EL, Nowak KJ, Iwamoto H, Ochala J. Molecular consequences of the myopathy-related D286G mutation on actin function. Frontiers in Physiology. 2018 dec. 1;9. 1756. https://doi.org/10.3389/fphys.2018.01756

Author

Fan, Jun ; Chan, Chun ; McNamara, Elyshia L. ; Nowak, Kristen J. ; Iwamoto, Hiroyuki ; Ochala, Julien. / Molecular consequences of the myopathy-related D286G mutation on actin function. I: Frontiers in Physiology. 2018 ; Bind 9.

Bibtex

@article{dbf6b0808be84020821f533b35ebb9ae,
title = "Molecular consequences of the myopathy-related D286G mutation on actin function",
abstract = "Myopathies are notably associated with mutations in genes encoding proteins known to be essential for the force production of skeletal muscle fibers, such as skeletal alpha-actin. The exact molecular mechanisms by which these specific defects induce myopathic phenotypes remain unclear. Hence, in the present study, to better understand actin dysfunction, we conducted a molecular dynamic simulation together with ex vivo experiments of the specific muscle disease-causing actin mutation, D286G located in the actin-actin interface. Our computational study showed that D286G impairs the flexural rigidity of actin filaments. However, upon activation, D286G did not have any direct consequences on actin filament extension. Hence, D286G may alter the structure of actin filaments but, when expressed together with normal actin molecules, it may only have minor effects on the ex vivo mechanics of actin filaments upon skeletal muscle fiber contraction.",
keywords = "Actin mechanics, Actin mutation, Muscle fiber, Muscle force, Myopathy",
author = "Jun Fan and Chun Chan and McNamara, {Elyshia L.} and Nowak, {Kristen J.} and Hiroyuki Iwamoto and Julien Ochala",
year = "2018",
month = dec,
day = "1",
doi = "10.3389/fphys.2018.01756",
language = "English",
volume = "9",
journal = "Frontiers in Physiology",
issn = "1664-042X",
publisher = "Frontiers Media S.A.",

}

RIS

TY - JOUR

T1 - Molecular consequences of the myopathy-related D286G mutation on actin function

AU - Fan, Jun

AU - Chan, Chun

AU - McNamara, Elyshia L.

AU - Nowak, Kristen J.

AU - Iwamoto, Hiroyuki

AU - Ochala, Julien

PY - 2018/12/1

Y1 - 2018/12/1

N2 - Myopathies are notably associated with mutations in genes encoding proteins known to be essential for the force production of skeletal muscle fibers, such as skeletal alpha-actin. The exact molecular mechanisms by which these specific defects induce myopathic phenotypes remain unclear. Hence, in the present study, to better understand actin dysfunction, we conducted a molecular dynamic simulation together with ex vivo experiments of the specific muscle disease-causing actin mutation, D286G located in the actin-actin interface. Our computational study showed that D286G impairs the flexural rigidity of actin filaments. However, upon activation, D286G did not have any direct consequences on actin filament extension. Hence, D286G may alter the structure of actin filaments but, when expressed together with normal actin molecules, it may only have minor effects on the ex vivo mechanics of actin filaments upon skeletal muscle fiber contraction.

AB - Myopathies are notably associated with mutations in genes encoding proteins known to be essential for the force production of skeletal muscle fibers, such as skeletal alpha-actin. The exact molecular mechanisms by which these specific defects induce myopathic phenotypes remain unclear. Hence, in the present study, to better understand actin dysfunction, we conducted a molecular dynamic simulation together with ex vivo experiments of the specific muscle disease-causing actin mutation, D286G located in the actin-actin interface. Our computational study showed that D286G impairs the flexural rigidity of actin filaments. However, upon activation, D286G did not have any direct consequences on actin filament extension. Hence, D286G may alter the structure of actin filaments but, when expressed together with normal actin molecules, it may only have minor effects on the ex vivo mechanics of actin filaments upon skeletal muscle fiber contraction.

KW - Actin mechanics

KW - Actin mutation

KW - Muscle fiber

KW - Muscle force

KW - Myopathy

UR - http://www.scopus.com/inward/record.url?scp=85076846728&partnerID=8YFLogxK

U2 - 10.3389/fphys.2018.01756

DO - 10.3389/fphys.2018.01756

M3 - Journal article

AN - SCOPUS:85076846728

VL - 9

JO - Frontiers in Physiology

JF - Frontiers in Physiology

SN - 1664-042X

M1 - 1756

ER -

ID: 245661849