E3泛素连接酶HOIL-1可诱导SOCS6相关蛋白的多聚泛素化及降解。
The E3 ubiquitin ligase HOIL-1 induces the polyubiquitination and degradation of SOCS6 associated proteins.
作者信息
Bayle Julie, Lopez Sophie, Iwaï Kazuhiro, Dubreuil Patrice, De Sepulveda Paulo
机构信息
INSERM UMR599, Laboratoire d'hématopoïèse moléculaire et fonctionnelle, Marseille, France.
出版信息
FEBS Lett. 2006 May 15;580(11):2609-14. doi: 10.1016/j.febslet.2006.03.093. Epub 2006 Apr 21.
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.
细胞因子信号转导抑制因子（SOCS）蛋白被认为是通过招募相互作用蛋白至泛素/蛋白酶体降解途径来发挥其功能的。所有SOCS蛋白都通过共同的Socs盒结合Elongin BC E3泛素连接酶复合物。在此，我们表明血红素氧化的IRP2泛素连接酶-1（HOIL-1），另一种E3泛素连接酶，与SOCS6相互作用。HOIL-1的Ubl结构域以及SOCS6的SH2和Socs盒结构域是这种相互作用所必需的。HOIL-1的表达使SOCS6稳定，并诱导与SOCS6相关的蛋白质的泛素化和降解。这些数据表明，除了常见的Elongin BC E3复合物外，SOCS蛋白可能还与不同的E3泛素连接酶相互作用。
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