Arginylation of Myosin Heavy Chain Regulates Skeletal Muscle Strength

被引：25

作者：

Comachione, Anabelle S. ^{[1
]}

Leite, Felipe S. ^{[1
]}

Wang, Junling ^{[2
]}

Leu, Nicolae A. ^{[2
]}

Kalganov, Albert ^{[1
]}

Volgin, Denys ^{[2
]}

Han, Xuemei ^{[3
]}

Xu, Tao ^{[3
]}

Cheng, Yu-Shu ^{[1
]}

Yates, John R. R., III ^{[3
]}

Rassier, Dilson E. ^{[1
]}

Kashina, Anna ^{[2
]}

机构：

[1] McGill Univ, Dept Kinesiol & Phys Educ Phys & Physiol, Montreal, PQ H2W 1S4, Canada

[2] Univ Penn, Sch Vet Med, Dept Anim Biol, Philadelphia, PA 19104 USA

[3] Scripps Res Inst, La Jolla, CA 92037 USA

来源：

CELL REPORTS | 2014年 / 8卷 / 02期

基金：

加拿大健康研究院;

关键词：

MYOFIBRILS; FORCE; HEART; CONTRACTILITY; PROTEINS;

D O I：

10.1016/j.celrep.2014.06.019

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页码：469 / 475

页数：7

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