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Updated: Apr 27, 2026

Myo-mechanical Analysis of Isolated Skeletal Muscle
Published on: February 22, 2011
Arginylation of myosin heavy chain regulates skeletal muscle strength
Anabelle S Cornachione1, Felipe S Leite1, Junling Wang2
1Department of Kinesiology and Physical Education, Physics and Physiology, McGill University, Montreal, QC H2W 1S4, Canada.
Abstract:
Protein arginylation is a posttranslational modification with an emerging global role in the regulation of actin cytoskeleton. To test the role of arginylation in the skeletal muscle, we generated a mouse model with Ate1 deletion driven by the skeletal muscle-specific creatine kinase (Ckmm) promoter. Ckmm-Ate1 mice were viable and outwardly normal; however, their skeletal muscle strength was significantly reduced in comparison to controls. Mass spectrometry of isolated skeletal myofibrils showed a limited set of proteins, including myosin heavy chain, arginylated on specific sites. Atomic force microscopy measurements of contractile strength in individual myofibrils and isolated myosin filaments from these mice showed a significant reduction of contractile forces, which, in the case of myosin filaments, could be fully rescued by rearginylation with purified Ate1. Our results demonstrate that arginylation regulates force production in muscle and exerts a direct effect on muscle strength through arginylation of myosin.
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