Review on the structural understanding of the 10S myosin II in the era of Cryo-electron microscopy

被引：0

作者：

Bharda A.V. ^{[1
]}

Jung H.S. ^{[1
]}

机构：

[1] Division of Chemistry & Biochemistry, Department of Biochemistry, College of Natural Sciences, Kangwon National University, Gangwon, Chuncheon

来源：

Applied Microscopy | 2022年 / 52卷 / 01期

基金：

新加坡国家研究基金会;

关键词：

Cryo-electron microscopy; High resolution studies; Molecular motor; Myosin; Smooth muscle myosin-II; Structural biology;

D O I：

10.1186/s42649-022-00078-x

中图分类号：

学科分类号：

摘要：

The compact smooth muscle 10S myosin II is a type of a monomer with folded tail and the heads bending back to interact with each other. This inactivated form is associated with regulatory and enzymatic activities affecting myosin processivity with actin filaments as well as ATPase activity. Phosphorylation by RLC can however, shuttle myosin from the inhibited 10S state to an activated 6S state, dictating the equilibrium. Multiple studies contributed by TEM have provided insights in the structural understanding of the 10S form. However, it is only recently that the true potential of Cryo-EM in deciphering the intramolecular interactions of 10S myosin state has been realized. This has led to an influx of new revelations on the 10S inactivation, unfolding mechanism and association in various diseases. This study reviews the gradual development in the structural interpretation of 10S species from TEM to Cryo-EM era. Furthermore, we discuss the utility of Cryo-EM in future myosin 10S studies and its contribution to human health. © 2022, The Author(s).

引用

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