Abstract：
Gasdermins are membrane pore-forming proteins that cause pyroptosis, an inflammatory cell death in which cells burst and release cytokines, chemokines, and other host alarm signals, such as ATP and HMGB1, which recruit and activate immune cells at sites of infection and danger. There are five gasdermins in humans - gasdermins A to E. Pyroptosis was first described in myeloid cells and mucosal epithelia, which express gasdermin D and activate it when cytosolic sensors of invasive infection or tissue damage assemble into large macromolecular structures, called inflammasomes. Inflammasomes recruit and activate inflammatory caspases (caspase 1, 4, 5, and 11), which cut gasdermin D to remove an inhibitory C-terminal domain, allowing the N-terminal domain to bind to membrane acidic lipids and oligomerize into pores. Recent studies have identified inflammasome-independent proteolytic pathways that activate gasdermin D and the other gasdermins. Here, we review inflammasome-independent pyroptosis pathways and what is known about their role in normal physiology and disease.
摘要：
Gasdermins是膜孔形成蛋白，会引起焦亡，细胞破裂并释放细胞因子的炎性细胞死亡，趋化因子,和其他主机报警信号，例如ATP和HMGB1，它们在感染和危险部位募集和激活免疫细胞。在人类中有五种gasdermins-gasderminsA到E。表达gasderminD并在侵入性感染或组织损伤的细胞溶质传感器组装成大的大分子结构时激活它，叫做炎性体。炎性体募集并激活炎性胱天蛋白酶（胱天蛋白酶1、4、5和11），切割gasderminD以去除抑制性C末端结构域，允许N端结构域与膜酸性脂质结合并寡聚化入孔中。最近的研究已经确定了不依赖炎性体的蛋白水解途径，该途径激活了gasderminD和其他gasdermins。这里,我们回顾了不依赖炎性体的焦亡通路以及它们在正常生理和疾病中的作用。
