The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral-inhibitor of apoptosis proteins
The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral-inhibitor of apoptosis proteins
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DOI：
10.1016/0092-8674(95)90149-3
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发表时间：
1995-12-29
期刊：
影响因子：
64.5
通讯作者：
Goeddel, DV
中科院分区：
文献类型：
--
作者：
Rothe, M;Pan, MG;Goeddel, DV
75 kDa 肿瘤坏死因子受体 (TNFR2) 通过受体相关的细胞质蛋白转导细胞外信号。其中两个信号传感器 TRAF1 和 TRAF2 先前已被分离和表征。我们在此报告了两种新型 TNFR2 相关蛋白（命名为 c-IAP1 和 c-IAP2）的生化纯化和随后的分子克隆，它们是最初在杆状病毒中鉴定的凋亡蛋白抑制剂 (IAP) 家族密切相关的哺乳动物成员。病毒和细胞 IAP 包含 N 端杆状病毒 IAP 重复 (BIR) 基序和 C 端环指。 c-IAP 不直接接触 TNFR2，而是通过其 N 端包含 BIR 基序的结构域与 TRAF1 和 TRAF2 关联。将 c-IAP1 或 c-IAP2 募集至 TNFR2 信号传导复合物需要 TRAF2-TRAF1 异质复合物。
The 75 kDa tumor necrosis factor receptor (TNFR2) transduces extracellular signals via receptor-associated cytoplasmic proteins. Two of these signal transducers, TRAF1 and TRAF2, were isolated and characterized previously. We report here the biochemical purification and subsequent molecular cloning of two novel TNFR2-associated proteins, designated c-IAP1 and c-IAP2, that are closely related mammalian members of the inhibitor of apoptosis protein (IAP) family originally identified in baculoviruses. The viral and cellular IAPs contain N-terminal baculovirus IAP repeat (BIR) motifs and a C-terminal RING finger. The c-IAPs do not directly contact TNFR2, but rather associate with TRAF1 and TRAF2 through their N-terminal BIR motif-comprising domain. The recruitment of c-IAP1 or c-IAP2 to the TNFR2 signaling complex requires a TRAF2-TRAF1 heterocomplex.