Hutagalung Alex H, Landsverk Megan L, Price Maureen G, Epstein Henry F
Departments of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
J Cell Sci. 2002 Nov 1;115(Pt 21):3983-90. doi: 10.1242/jcs.00107.
The canonical UCS (UNC-45/Cro1/She4p) protein, Caenorhabditis elegans UNC-45, was one of the earliest molecules to be shown genetically to be necessary for sarcomere assembly. Genetic analyses of homologues in several fungal species indicate that the conserved UCS domain functionally interacts with conventional type II and unconventional type V myosins. In C. elegans and other invertebrate species, UNC-45 and its orthologues interact with both sarcomeric and non-sarcomeric myosins whereas, in vertebrates, there are two UNC-45 isoforms: a general cell (GC) and a striated muscle (SM) isoform. Although the mechanism of action of UCS proteins is unknown, recent biochemical studies suggest that they may act as molecular chaperones that facilitate the folding and/or maturation of myosin.
经典的UCS（UNC-45/Cro1/She4p）蛋白，即秀丽隐杆线虫的UNC-45，是最早通过遗传学方法证明对肌节组装必不可少的分子之一。对几种真菌物种中同源物的遗传分析表明，保守的UCS结构域在功能上与传统的II型和非传统的V型肌球蛋白相互作用。在秀丽隐杆线虫和其他无脊椎动物物种中，UNC-45及其直系同源物与肌节和非肌节肌球蛋白相互作用，而在脊椎动物中，有两种UNC-45亚型：一种是一般细胞（GC）亚型，另一种是横纹肌（SM）亚型。尽管UCS蛋白的作用机制尚不清楚，但最近的生化研究表明，它们可能作为分子伴侣促进肌球蛋白的折叠和/或成熟。
