Department of Pharmacy, College of Pharmacy, Chung‑Ang University, Seoul 06974, Republic of Korea.
Int J Mol Med. 2019 Mar;43(3):1119-1127. doi: 10.3892/ijmm.2019.4060. Epub 2019 Jan 11.
The caspase recruitment domain (CARD), a well‑known protein interaction module, belongs to the death domain (DD) superfamily, which includes DDs, death effector domains, and pyrin domains. The DD superfamily mediates the protein interactions necessary for apoptosis and immune cell signaling pathways. Among these domains, the CARD has been studied extensively as it mediates important cellular signaling events that are associated with various human diseases including cancer, neuro‑degenerative diseases and immune disorders. Homo‑type and hetero‑type CARD‑CARD interactions mediate the formation of large signaling complexes, including caspase‑activating complexes and downstream signaling complexes. The present review summarizes and discusses the results of structural studies of various CARDs and their complexes. These studies shed light on the mechanisms that control the assembly and disassembly of signaling complexes and provide an improved understanding of cellular signaling processes.
半胱氨酸天冬氨酸蛋白酶募集结构域(CARD)是一种众所周知的蛋白质相互作用模块,属于死亡结构域(DD)超家族,该超家族包括 DD、死亡效应结构域和 pyrin 结构域。DD 超家族介导凋亡和免疫细胞信号通路所需的蛋白质相互作用。在这些结构域中,CARD 已被广泛研究,因为它介导与各种人类疾病相关的重要细胞信号事件,包括癌症、神经退行性疾病和免疫紊乱。同型和异型 CARD-CARD 相互作用介导大型信号复合物的形成,包括半胱天冬酶激活复合物和下游信号复合物。本综述总结和讨论了各种 CARD 及其复合物的结构研究结果。这些研究揭示了控制信号复合物组装和拆卸的机制,并提供了对细胞信号过程的更好理解。