Posttranslational Arginylation Regulates Striated Muscle Function

被引：8

作者：

Leite, Felipe de Souza ^{[1
]}

Kashina, Anna ^{[2
]}

Rassier, Dilson E. ^{[1
]}

机构：

[1] McGill Univ, Dept Kinesiol & Phys Educ Phys & Physiol, 475 Pine Ave W,Room 308, Montreal, PQ H2W 1S4, Canada

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

来源：

EXERCISE AND SPORT SCIENCES REVIEWS | 2016年 / 44卷 / 03期

基金：

美国国家卫生研究院; 加拿大健康研究院;

关键词：

myosin; actin; titin; arginylation; posttranslational modification; BINDING PROTEIN-C; SARCOMERIC Z-DISK; ALPHA-ACTININ; MYOSIN; TITIN; TRANSFERASE; DOMAIN; HEART; CYTOSKELETON; EXPRESSION;

D O I：

10.1249/JES.0000000000000079

中图分类号：

Q4 [生理学];

学科分类号：

071003 ;

摘要：

In this article, we propose the hypothesis that the posttranslational arginylation of proteins, a process catalyzed by the enzyme arginyl-tRNA-transferase, regulates active and passive force generation in striated muscles. Specifically, we propose that proteins essential for muscle contraction and force production are regulated by arginylation, including myosin heavy chain, troponin, actin, and titin filaments.

引用

页码：98 / 103

页数：6

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