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CRADD,一种新的半胱天冬酶-2的人类凋亡衔接分子,以及FasL/肿瘤坏死因子受体相互作用蛋白RIP。

CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP.

作者信息

Ahmad M, Srinivasula S M, Wang L, Talanian R V, Litwack G, Fernandes-Alnemri T, Alnemri E S

机构信息

Kimmel Cancer Institute, Jefferson Medical College, Philadelphia, Pennsylvania 19107, USA.

出版信息

Cancer Res. 1997 Feb 15;57(4):615-9.

PMID:9044836
Abstract

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.

摘要

FADD/MORT1是一种含有死亡结构域(DD)的衔接子/信号分子,它与FAS/APO-I(CD95)和肿瘤坏死因子受体1的细胞内DD以及半胱天冬酶-8(Mch5/MACH/FLICE)的前结构域相互作用。FADD与半胱天冬酶-8的结合大概会激活这种半胱天冬酶并导致细胞凋亡。另一种含有DD的衔接子/信号分子CRADD被鉴定出来,并被证明可诱导细胞凋亡。CRADD具有与FADD相似的双结构域结构。它有一个与半胱天冬酶-2相互作用的NH2末端半胱天冬酶同源结构域和一个与RIP相互作用的COOH末端DD。CRADD在许多组织中组成性表达,因此可能在调节哺乳动物细胞的细胞凋亡中发挥作用。

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