Yin Lei-Miao, Schnoor Michael, Jun Chang-Duk
Laboratory of Molecular Biology, Shanghai Research Institute of Acupuncture and Meridian, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Molecular Biomedicine, Center for Investigation and Advanced Studies of the National Polytechnic Institute (Cinvestav), Mexico City, Mexico.
Front Cell Dev Biol. 2020 May 14;8:342. doi: 10.3389/fcell.2020.00342. eCollection 2020.
The calponin homology (CH) domain is one of the most common modules in various actin-binding proteins and is characterized by an α-helical fold. The CH domain plays important regulatory roles in both cytoskeletal dynamics and signaling. The CH domain is required for stability and organization of the actin cytoskeleton, calcium mobilization and activation of downstream pathways. The CH domain has recently garnered increased attention due to its importance in the onset of different diseases, such as cancers and asthma. However, many roles of the CH domain in various protein functions and corresponding diseases are still unclear. Here, we review current knowledge about the structural features, interactome and related diseases of the CH domain.
钙调蛋白同源（CH）结构域是各种肌动蛋白结合蛋白中最常见的模块之一，其特征在于α-螺旋折叠。CH结构域在细胞骨架动力学和信号传导中均发挥重要的调节作用。肌动蛋白细胞骨架的稳定性和组织、钙动员以及下游途径的激活都需要CH结构域。由于CH结构域在诸如癌症和哮喘等不同疾病的发病过程中的重要性，它最近受到了越来越多的关注。然而，CH结构域在各种蛋白质功能和相应疾病中的许多作用仍不清楚。在此，我们综述了关于CH结构域的结构特征、相互作用组和相关疾病的现有知识。
