Protein arginylation of cytoskeletal proteins in the muscle: modifications modifying function

被引:10
|
作者
Rassier, Dilson E. [1 ]
Kashina, Anna [2 ]
机构
[1] McGill Univ, Dept Kinesiol & Phys Educ, Montreal, PQ H2W 1S4, Canada
[2] Univ Penn, Dept Biomed Sci, Philadelphia, PA 19104 USA
来源
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY | 2019年 / 316卷 / 05期
基金
加拿大健康研究院;
关键词
actin; arginylation; muscle; myosin; posttranslational modification; N-END RULE; POSTTRANSLATIONAL ARGINYLATION; MYOSIN SUBFRAGMENT-1; FORCE ENHANCEMENT; STRIATED-MUSCLE; TITIN; ACTIN; SKELETAL; PATHWAY; MECHANISM;
D O I
10.1152/ajpcell.00500.2018
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The cytoskeleton drives many essential processes in normal physiology, and its impairments underlie many diseases, including skeletal myopathies, cancer, and heart failure, that broadly affect developed countries worldwide. Cytoskeleton regulation is a field of investigation of rapidly emerging global importance and a new venue for the development of potential therapies. This review overviews our present understanding of the posttranslational regulation of the muscle cytoskeleton through arginylation, a tRNA-dependent addition of arginine to proteins mediated by arginyltransferase 1. We focus largely on arginylation-dependent regulation of striated muscles, shown to play critical roles in facilitating muscle integrity, contractility, regulation, and strength.
引用
收藏
页码:C668 / C677
页数:10
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