TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase
TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase
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DOI：
10.1016/j.bbrc.2009.04.010
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发表时间：
2009-05-29
影响因子：
3.1
通讯作者：
Inoue, Satoshi
中科院分区：
文献类型：
--
作者：
Urano, Tomohiko;Usui, Takahiko;Inoue, Satoshi
Terf/TRIM 17是TRIM蛋白家族的成员，其特征在于RING指、B-box和卷曲螺旋结构域。在本研究中，我们发现terf与TRIM 44相互作用。Terf在E2酶UbcH 6存在下进行体外泛素化;这表明terf具有E3泛素连接酶活性。在哺乳动物细胞中，terf与多聚泛素链结合并被蛋白酶体抑制剂稳定：这表明terf通过多聚泛素化使其自身易于被蛋白酶体降解。我们还发现TRIM 44抑制terf的泛素化，从而稳定了蛋白质。TRIM 44的N-末端区域含有在泛素水解酶（ZF UBP）和泛素特异性蛋白酶（USP）中发现的锌指结构域。因此，我们提出TRIM 44可能作为一类新的“USP样TRIM”发挥作用，其调节相关TRIM蛋白的活性。(C)2009 Elsevier Inc. All rights reserved.
Terf/TRIM17 is a member of the TRIM family of proteins, which is characterized by the RING finger, B-box, and coiled-coil domains. In the present Study, we found that terf interacts with TRIM44. Terf underwent ubiquitination in vitro in the presence of the E2 enzyme UbcH6; this Suggests that terf exhibits E3 ubiquitin ligase activity. It was also found that terf was conjugated with polyubiquitin chains and stabilized by the proteasome inhibitor in mammalian cells: this Suggested that terf tendered itself susceptible to proteasomal degradation through polyubiquitination. We also found that TRIM44 inhibited ubiquitination of terf, and thus stabilized the protein. The N-terminal region of TRIM44 contains a zinc-finger domain found in ubiquitin hydrolases (ZF UBP) and ubiquitin specific proteases (USPs). Thus, we proposed that TRIM44 may function as a new class of the "USP-like-TRIM" which regulates the activity of associated TRIM proteins. (C) 2009 Elsevier Inc. All rights reserved.