Myosin chaperones

被引：26

作者：

Hellerschmied, Doris ^{[1
]}

Clausen, Tim ^{[1
]}

机构：

[1] Res Inst Mol Pathol, A-1030 Vienna, Austria

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2014年 / 25卷

基金：

奥地利科学基金会;

关键词：

UCS-DOMAIN PROTEIN; SKELETAL-MUSCLES; BUDDING YEAST; UNC-45; COLOCALIZES; REGULATOR; FILAMENT; HOMOLOG; HSP90A;

D O I：

10.1016/j.sbi.2013.11.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The folding and assembly of myosin motor proteins is essential for most movement processes at the cellular, but also at the organism level. Importantly, myosins, which represent a very diverse family of proteins, require the activity of general and specialized folding factors to develop their full motor function. The activities of the myosin-specific UCS (UNC-45/Cro1/She4) chaperones range from assisting acto-myosin dependent transport processes to scaffolding multi-subunit chaperone complexes, which are required to assemble myofilaments. Recent structure-function studies revealed the structural organization of TPR (tetratricopeptide repeat)-containing and TPR-less UCS chaperones. The observed structural differences seem to reflect the specialized and remarkably versatile working mechanisms of myosin-directed chaperones, as will be discussed in this review.

引用

收藏

页码：9 / 15

页数：7

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