The E3 ubiquitin ligase HOIL-1 induces the polyubiquitination and degradation of SOCS6 associated proteins
The E3 ubiquitin ligase HOIL-1 induces the polyubiquitination and degradation of SOCS6 associated proteins
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DOI：
10.1016/j.febslet.2006.03.093
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发表时间：
2006-05-15
期刊：
影响因子：
3.5
通讯作者：
De Sepulveda, Paulo
中科院分区：
文献类型：
--
作者：
Bayle, Julie;Lopez, Sophie;De Sepulveda, Paulo
细胞因子信号传导抑制因子（SOCS）蛋白被认为通过在泛素/蛋白酶体降解途径中招募相互作用蛋白来发挥其功能。所有的SOCS蛋白通过共同的SOCS -box结合一个伸长BC E3泛素连接酶复合物。在这里，我们发现血液氧化的IRP2泛素连接酶-1 (HOIL-1)，另一个E3泛素连接酶，与SOCS6相互作用。HOIL-1的Ubl结构域和SOCS6的SH2和soc -box结构域需要相互作用。HOIL-1表达稳定SOCS6并诱导与SOCS6相关蛋白的泛素化和降解。这些数据表明，SOCS蛋白可能与不同的E3泛素连接酶相互作用，除了一个常见的伸长BC E3复合体。(c) 2006年欧洲生化学会联合会。Elsevier B.V.版权所有。
The suppressor of cytokine signaling (SOCS) proteins are thought to exert their function through the recruitment of interacting-proteins to the ubiquitin/proteasome degradation pathway. All SOCS proteins bind an Elongin BC E3 ubiquitin ligase complex through the common Socs-box. Here, we show that haem-oxidized IRP2 ubiquitin ligase-1 (HOIL-1), another E3 ubiquitin ligase, interacts with SOCS6. The Ubl domain of HOIL-1 and the SH2 and Socs-box domains of SOCS6 are required for the interaction. HOIL-1 expression stabilizes SOCS6 and induces the ubiquitination and degradation of proteins associated with SOCS6. These data suggest that SOCS proteins may interact with different E3 ubiquitin ligases in addition to a common Elongin BC E3 complex. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.