MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclX(L) and initiates cell death
MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclX(L) and initiates cell death
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DOI：
10.1073/pnas.94.21.11333
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发表时间：
1997-10-14
影响因子：
11.1
通讯作者：
Hood, L
中科院分区：
文献类型：
--
作者：
Han, DKM;Chaudhary, PM;Hood, L
蛋白水解半胱天冬酶级联的激活已被确定为不同生物系统中细胞凋亡的最终共同途径。我们已经分离出一个基因，称为MRIT，其具有与FLICE（MACH）的整体序列同源性，FLICE（MACH）是一种大的前结构域半胱天冬酶，其将肿瘤坏死因子受体家族的死亡结构域受体的聚集复合物与下游半胱天冬酶连接。然而，与FLICE不同，MRIT的C-末端结构域缺乏半胱天冬酶催化共有序列QAC（R/Q）G。尽管如此，MRIT激活caspase依赖性死亡，使用酵母双杂交试验，我们证明MRIT与具有大小前结构域的caspase相关此外，MRIT在哺乳动物细胞中同时且独立地与BclX（L）和FLICE相互作用，因此，MRIT是一种哺乳动物蛋白，同时与半胱天冬酶和Bcl-2家族成员相互作用。
Activation of the cascade of proteolytic caspases has been identified as the final common pathway of apoptosis in diverse biological systems. We have isolated a gene, termed MRIT, that possesses overall sequence homology to FLICE (MACH), a large prodomain caspase that links the aggregated complex of the death domain receptors of the tumor necrosis factor receptor family to downstream caspases, However, unlike FLICE, the C-terminal domain of MRIT lacks the caspase catalytic consensus sequence QAC(R/Q)G. Nonetheless MRIT activates caspase dependent death, Using yeast two-hybrid assays, we demonstrate that MRIT associates with caspases possessing large and small prodomains (FLICE, and CPP32/YAMA), as well as with the adaptor molecule FADD, In addition, MRIT simultaneously and independently interacts with BclX(L) and FLICE in mammalian cells, Thus, MRIT is a mammalian protein that interacts simultaneously with both caspases and a Bcl-2 family member.