Death-effector filaments: novel cytoplasmic structures that recruit caspases and trigger apoptosis.
Death-effector filaments: novel cytoplasmic structures that recruit caspases and trigger apoptosis.
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DOI：
10.1083/jcb.141.5.1243
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发表时间：
1998-06-01
期刊：
影响因子：
--
通讯作者：
Lenardo MJ
中科院分区：
文献类型：
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作者：
Siegel RM;Martin DA;Zheng L;Ng SY;Bertin J;Cohen J;Lenardo MJ
死亡效应结构域(DED)是一个关键的蛋白质相互作用结构域，它将caspase招募到与肿瘤坏死因子受体超家族成员的复合体中。也可以通过表达某些含有DED的蛋白来诱导细胞凋亡，而不需要表面受体的交联性。使用绿色荧光蛋白检测活细胞中含有DED的蛋白，我们发现这些蛋白通过形成新的细胞质细丝来招募和激活caspase酶原，从而导致细胞凋亡。这些细丝的形成，我们称之为死亡效应细丝，被病毒抗凋亡含DED蛋白的共表达所阻止，但不被bcl2家族蛋白所阻止。因此，死亡效应丝的形成允许细胞内受调控的凋亡信号复合体的组装，这些复合体可以独立于质膜上的受体启动或放大凋亡刺激。
The death-effector domain (DED) is a critical protein interaction domain that recruits caspases into complexes with members of the TNF-receptor superfamily. Apoptosis can also be induced by expressing certain DED-containing proteins without surface receptor cross-linking. Using Green Fluorescent Protein to examine DED-containing proteins in living cells, we show that these proteins cause apoptosis by forming novel cytoplasmic filaments that recruit and activate pro-caspase zymogens. Formation of these filaments, which we term death-effector filaments, was blocked by coexpression of viral antiapoptotic DED-containing proteins, but not by bcl-2 family proteins. Thus, formation of death-effector filaments allows a regulated intracellular assembly of apoptosis-signaling complexes that can initiate or amplify apoptotic stimuli independently of receptors at the plasma membrane.