Mechanics of myosin function in white muscle fibres of the dogfish, Scyliorhinus canicula

S. Park-Holohan; M. Linari; M. Reconditi; L. Fusi; E. Brunello; M. Irving; M. Dolfi; V. Lombardi; T. G. West; N. A. Curtin; R. C. Woledge; G. Piazzesi

doi:10.1113/jphysiol.2011.217133

Mechanics of myosin function in white muscle fibres of the dogfish, Scyliorhinus canicula

S. Park-Holohan, M. Linari, M. Reconditi, L. Fusi, E. Brunello, M. Irving, M. Dolfi, V. Lombardi, T. G. West, N. A. Curtin^*, R. C. Woledge, G. Piazzesi

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

14 Citations (Scopus)

Abstract

Key points Muscle force and shortening are generated by a structural change called the working stroke in myosin motor proteins that cross-link the myosin and actin filaments in muscle. Precise values for two key parameters of the myosin motor its mechanical stiffness and the size of the working stroke at low load were previously only available from one type of muscle in one species, fast twitch muscles of the frog, so it was not clear how generally applicable these values were. We show that in dogfish fast muscle the low-load working stroke is the same as in frog muscle, but the myosin motor stiffness is smaller. The results provide new insights into how the molecular properties of myosin motors in different muscle types and species may be adapted for different muscle functions.

Original language	English
Pages (from-to)	1973-1988
Number of pages	16
Journal	The Journal of Physiology
Volume	590
Issue number	8
DOIs	https://doi.org/10.1113/jphysiol.2011.217133
Publication status	Published - Apr 2012

Keywords

X-RAY-DIFFRACTION
VERTEBRATE STRIATED-MUSCLE
SKELETAL-MUSCLE
ENERGY-CONVERSION
FORCE GENERATION
SINUSOIDAL MOVEMENT
CROSSBRIDGE ACTION
WORKING STROKE
ACTIVE FORCE
RABBIT PSOAS

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10.1113/jphysiol.2011.217133

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@article{fad9c0c0b8b84699850e8b23afa52b99,

title = "Mechanics of myosin function in white muscle fibres of the dogfish, Scyliorhinus canicula",

abstract = "Key points Muscle force and shortening are generated by a structural change called the working stroke in myosin motor proteins that cross-link the myosin and actin filaments in muscle. Precise values for two key parameters of the myosin motor its mechanical stiffness and the size of the working stroke at low load were previously only available from one type of muscle in one species, fast twitch muscles of the frog, so it was not clear how generally applicable these values were. We show that in dogfish fast muscle the low-load working stroke is the same as in frog muscle, but the myosin motor stiffness is smaller. The results provide new insights into how the molecular properties of myosin motors in different muscle types and species may be adapted for different muscle functions.",

keywords = "X-RAY-DIFFRACTION, VERTEBRATE STRIATED-MUSCLE, SKELETAL-MUSCLE, ENERGY-CONVERSION, FORCE GENERATION, SINUSOIDAL MOVEMENT, CROSSBRIDGE ACTION, WORKING STROKE, ACTIVE FORCE, RABBIT PSOAS",

author = "S. Park-Holohan and M. Linari and M. Reconditi and L. Fusi and E. Brunello and M. Irving and M. Dolfi and V. Lombardi and West, {T. G.} and Curtin, {N. A.} and Woledge, {R. C.} and G. Piazzesi",

year = "2012",

month = apr,

doi = "10.1113/jphysiol.2011.217133",

language = "English",

volume = "590",

pages = "1973--1988",

journal = "The Journal of Physiology",

issn = "0022-3751",

publisher = "Wiley",

number = "8",

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TY - JOUR

T1 - Mechanics of myosin function in white muscle fibres of the dogfish, Scyliorhinus canicula

AU - Park-Holohan, S.

AU - Linari, M.

AU - Reconditi, M.

AU - Fusi, L.

AU - Brunello, E.

AU - Irving, M.

AU - Dolfi, M.

AU - Lombardi, V.

AU - West, T. G.

AU - Curtin, N. A.

AU - Woledge, R. C.

AU - Piazzesi, G.

PY - 2012/4

Y1 - 2012/4

N2 - Key points Muscle force and shortening are generated by a structural change called the working stroke in myosin motor proteins that cross-link the myosin and actin filaments in muscle. Precise values for two key parameters of the myosin motor its mechanical stiffness and the size of the working stroke at low load were previously only available from one type of muscle in one species, fast twitch muscles of the frog, so it was not clear how generally applicable these values were. We show that in dogfish fast muscle the low-load working stroke is the same as in frog muscle, but the myosin motor stiffness is smaller. The results provide new insights into how the molecular properties of myosin motors in different muscle types and species may be adapted for different muscle functions.

AB - Key points Muscle force and shortening are generated by a structural change called the working stroke in myosin motor proteins that cross-link the myosin and actin filaments in muscle. Precise values for two key parameters of the myosin motor its mechanical stiffness and the size of the working stroke at low load were previously only available from one type of muscle in one species, fast twitch muscles of the frog, so it was not clear how generally applicable these values were. We show that in dogfish fast muscle the low-load working stroke is the same as in frog muscle, but the myosin motor stiffness is smaller. The results provide new insights into how the molecular properties of myosin motors in different muscle types and species may be adapted for different muscle functions.

KW - X-RAY-DIFFRACTION

KW - VERTEBRATE STRIATED-MUSCLE

KW - SKELETAL-MUSCLE

KW - ENERGY-CONVERSION

KW - FORCE GENERATION

KW - SINUSOIDAL MOVEMENT

KW - CROSSBRIDGE ACTION

KW - WORKING STROKE

KW - ACTIVE FORCE

KW - RABBIT PSOAS

U2 - 10.1113/jphysiol.2011.217133

DO - 10.1113/jphysiol.2011.217133

M3 - Article

SN - 0022-3751

VL - 590

SP - 1973

EP - 1988

JO - The Journal of Physiology

JF - The Journal of Physiology

IS - 8

ER -

Mechanics of myosin function in white muscle fibres of the dogfish, Scyliorhinus canicula

Abstract

Keywords

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