Molecular basis of dimerization of initiator caspase was revealed by crystal structure of caspase-8 pro-domain
Molecular basis of dimerization of initiator caspase was revealed by crystal structure of caspase-8 pro-domain
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DOI：
10.1038/s41418-018-0200-x
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发表时间：
2019-07-01
影响因子：
12.4
通讯作者：
Park, Hyun Ho
中科院分区：
文献类型：
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作者：
Park, Hyun Ho
装配死亡诱导信号复合体(DISC)以激活启动子caspase是受体介导的细胞凋亡信号转导的关键步骤。许多含有死亡效应结构域(DED)的蛋白质参与了视盘的组装和控制。光盘的主要成分之一caspase-8含有DED和DED介导的二聚反应，而光盘中的寡聚作用对于该启动子caspase的激活是至关重要的。人们对DED介导的二聚化和寡聚化进行了深入的研究，但还没有给出明确的答案，也存在许多有争议的争论。在此，我们结合结晶学研究，提出了caspase-8串联DED二聚化新工艺。
The assembly of death-inducing signaling complex (DISC) for activation of initiator caspase is a key step for the receptor-mediated apoptosis signaling. Many death effector domain (DED)-containing proteins are involved in DISC assembly and controlling. One of the main DISC component, caspase-8, contains DED and DED-mediated dimerization and oligomerization in the DISC is critical for the activation of this initiator caspase. There have been intensive studies to understand DED-mediated dimerization and oligomerization for the DISC assembly but no clear answer has been provided and there are many controversial arguments. Here, we suggested novel dimerization process of tandem DED of caspase-8 with crystallographic study.