CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP.
CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP.
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发表时间：
1997-02
期刊：
影响因子：
11.2
通讯作者：
Manzoor Ahmad;S. Srinivasula;Lijuan Wang;R. Talanian;G. Litwack;T. Fernandes‐Alnemri;E. Alnemri
中科院分区：
文献类型：
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作者：
Manzoor Ahmad;S. Srinivasula;Lijuan Wang;R. Talanian;G. Litwack;T. Fernandes‐Alnemri;E. Alnemri
FADD/MORT1 is a death domain (DD)-containing adaptor/signaling molecule that interacts with the intracellular DD of FAS/APO-I (CD95) and tumor necrosis factor receptor 1 and the prodomain of caspase-8 (Mch5/MACH/FLICE). FADD engagement of caspase-8 presumably activates this caspase and leads to apoptosis. Another DD-containing adaptor/signaling molecule, CRADD, was identified and was shown to induce apoptosis. CRADD has a dual-domain structure similar to that of FADD. It has an NH2-terminal caspase homology domain that interacts with caspase-2 and a COOH-terminal DD that interacts with RIP. CRADD is constitutively expressed in many tissues and thus could play a role in regulating apoptosis in mammalian cells.
