Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers

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Standard

Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers. / Ochala, Julien; Gokhin, David S; Iwamoto, Hiroyuki; Fowler, Velia M.

I: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Bind 28, Nr. 1, 01.2014, s. 408-15.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Ochala, J, Gokhin, DS, Iwamoto, H & Fowler, VM 2014, 'Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers', FASEB journal : official publication of the Federation of American Societies for Experimental Biology, bind 28, nr. 1, s. 408-15. https://doi.org/10.1096/fj.13-239640

APA

Ochala, J., Gokhin, D. S., Iwamoto, H., & Fowler, V. M. (2014). Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 28(1), 408-15. https://doi.org/10.1096/fj.13-239640

Vancouver

Ochala J, Gokhin DS, Iwamoto H, Fowler VM. Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2014 jan.;28(1):408-15. https://doi.org/10.1096/fj.13-239640

Author

Ochala, Julien ; Gokhin, David S ; Iwamoto, Hiroyuki ; Fowler, Velia M. / Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers. I: FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2014 ; Bind 28, Nr. 1. s. 408-15.

Bibtex

@article{304eecc90129442ebc4653b3b8256728,
title = "Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers",
abstract = "In skeletal muscle, thick and thin filaments are arranged in a myofibrillar lattice. Tropomodulin 1 (Tmod1) is a pointed-end capping and tropomyosin-binding protein that controls thin-filament assembly, stability, and lengths. It remains unknown whether Tmods have other functional roles, such as regulating muscle contractility. To investigate this, we recorded and analyzed the mechanical properties and X-ray diffraction patterns of single membrane-permeabilized skeletal muscle fibers from mice lacking Tmod1. Results show that absence of Tmod1 and its replacement by Tmod3 and Tmod4 may impair initial tropomyosin movement over actin subunits during thin-filament activation, thus reducing both the fraction of actomyosin crossbridges in the strongly bound state (-29%) and fiber force-generating capacity (-31%). Therefore, Tmods are novel regulators of actomyosin crossbridge formation and muscle contractility, and future investigations and models of skeletal muscle force production must incorporate Tmods.",
keywords = "Actomyosin/chemistry, Animals, Mice, Mice, Knockout, Muscle Fibers, Skeletal/metabolism, Tropomodulin/genetics, X-Ray Diffraction",
author = "Julien Ochala and Gokhin, {David S} and Hiroyuki Iwamoto and Fowler, {Velia M}",
year = "2014",
month = jan,
doi = "10.1096/fj.13-239640",
language = "English",
volume = "28",
pages = "408--15",
journal = "F A S E B Journal",
issn = "0892-6638",
publisher = "Federation of American Societies for Experimental Biology",
number = "1",

}

RIS

TY - JOUR

T1 - Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers

AU - Ochala, Julien

AU - Gokhin, David S

AU - Iwamoto, Hiroyuki

AU - Fowler, Velia M

PY - 2014/1

Y1 - 2014/1

N2 - In skeletal muscle, thick and thin filaments are arranged in a myofibrillar lattice. Tropomodulin 1 (Tmod1) is a pointed-end capping and tropomyosin-binding protein that controls thin-filament assembly, stability, and lengths. It remains unknown whether Tmods have other functional roles, such as regulating muscle contractility. To investigate this, we recorded and analyzed the mechanical properties and X-ray diffraction patterns of single membrane-permeabilized skeletal muscle fibers from mice lacking Tmod1. Results show that absence of Tmod1 and its replacement by Tmod3 and Tmod4 may impair initial tropomyosin movement over actin subunits during thin-filament activation, thus reducing both the fraction of actomyosin crossbridges in the strongly bound state (-29%) and fiber force-generating capacity (-31%). Therefore, Tmods are novel regulators of actomyosin crossbridge formation and muscle contractility, and future investigations and models of skeletal muscle force production must incorporate Tmods.

AB - In skeletal muscle, thick and thin filaments are arranged in a myofibrillar lattice. Tropomodulin 1 (Tmod1) is a pointed-end capping and tropomyosin-binding protein that controls thin-filament assembly, stability, and lengths. It remains unknown whether Tmods have other functional roles, such as regulating muscle contractility. To investigate this, we recorded and analyzed the mechanical properties and X-ray diffraction patterns of single membrane-permeabilized skeletal muscle fibers from mice lacking Tmod1. Results show that absence of Tmod1 and its replacement by Tmod3 and Tmod4 may impair initial tropomyosin movement over actin subunits during thin-filament activation, thus reducing both the fraction of actomyosin crossbridges in the strongly bound state (-29%) and fiber force-generating capacity (-31%). Therefore, Tmods are novel regulators of actomyosin crossbridge formation and muscle contractility, and future investigations and models of skeletal muscle force production must incorporate Tmods.

KW - Actomyosin/chemistry

KW - Animals

KW - Mice

KW - Mice, Knockout

KW - Muscle Fibers, Skeletal/metabolism

KW - Tropomodulin/genetics

KW - X-Ray Diffraction

U2 - 10.1096/fj.13-239640

DO - 10.1096/fj.13-239640

M3 - Journal article

C2 - 24072783

VL - 28

SP - 408

EP - 415

JO - F A S E B Journal

JF - F A S E B Journal

SN - 0892-6638

IS - 1

ER -

ID: 240788733