粗脉脉孢菌
劈理(地质)
异基因识别
细胞生物学
上睑下垂
生物物理学
二聚体
生物
化学
生物化学
基因
突变体
古生物学
断裂(地质)
细胞凋亡
有机化学
程序性细胞死亡
主要组织相容性复合体
作者
Yueyue Li,Yueyue Li,Yanjie Hou,Qi Sun,Qi Sun,Huan Zeng,Huan Zeng,Meng Fang,Meng Fang,Tian Xia,Qun He,Feng Shao,Feng Shao,Feng Shao,Feng Shao,Feng Shao,Feng Shao,Jingjin Ding,Jingjin Ding,Jingjin Ding
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2024-04-25
标识
DOI:10.1126/science.adm9190
摘要
Gasdermins (GSDMs) are pore-forming proteins that execute pyroptosis for immune defense. GSDMs are two-domain proteins, activated by proteolytic removal of the inhibitory domain. Here we report two types of cleavage-independent GSDM activation. First, Tricho GSDM, a pore-forming-domain-only protein from the basal metazoan Trichoplax adhaerens , is a disulfides-linked autoinhibited dimer, activated by reduction of the disulfides. Cryo–electron microscopy (cryo-EM) structure illustrates assembly mechanism for the 44-mer Tricho GSDM pore. Second, RCD-1-1/RCD-1-2, encoded by polymorphic rcd-1 in filamentous fungus Neurospora crassa , are also pore-forming-domain-only GSDMs. RCD-1-1 and RCD-1-2, when encountering each other, form pores and cause pyroptosis, underlying allorecognition in Neurospora . Cryo-EM structure reveals a pore of 11 RCD-1-1/RCD-1-2 heterodimers and heterodimerization-triggered pore assembly mechanism. This study shows mechanistic diversities in GSDM activation and indicates versatile functions of GSDMs.
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