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首页> 外文期刊>Journal of Molecular Biology >Id-1 induces proteasome-dependent degradation of the HBX protein.
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Id-1 induces proteasome-dependent degradation of the HBX protein.

机译：Id-1诱导蛋白酶体依赖的HBX蛋白降解。

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Id-1 is a member of the HLH protein family that regulates a wide range of cellular processes such as cell proliferation, apoptosis, senescence and overexpression of Id-1 was recently suggested to play roles in the development and progression of different cancers. Previously, Id-1 was shown to physically interact with the viral protein E1A. Meanwhile, Id-1 expression was found to be regulated by several of the virus-encoded proteins, suggesting that Id-1 may be a common cellular target of the viral proteins. Here, we report that Id-1 interacts with the Hepatitis-B virus (HBV)-encoded protein HBX and regulates its stability in hepatocellular carcinoma (HCC) cells. We found that in HCC cells, ectopic Id-1 expression significantly decreased the half-life of the HBX protein, indicating that HBX is destabilized by Id-1. Meanwhile, the Id-1-induced HBX degradation was found to be inhibited by treatment with proteasome inhibitor, suggesting that this process is mediated through the proteasome pathway. Interestingly, while Id-1 did not induce HBX-ubiquitination, we found that removal of all the lysine residues of the HBX protein protects it from the effect of Id-1, indicating that ubiquitination is still required for the Id-1-mediated HBX degradation. Meanwhile, we found that Id-1 binds to the proteasome subunit C8 and facilitates its interaction with the HBX protein and disruption of this interaction completely abolishes the negative effect of Id-1 on HBX protein stability. Taken together, our results demonstrated a novel function of Id-1 in regulating HBX protein stability through interaction with the proteasome.
机译：Id-1是HLH蛋白家族的成员，该家族调节广泛的细胞过程，例如细胞增殖，凋亡，衰老和Id-1的过表达，最近被认为在不同癌症的发生和发展中起作用。以前，Id-1被证明与病毒蛋白E1A发生物理相互作用。同时，发现Id-1的表达受几种病毒编码蛋白的调节，这表明Id-1可能是病毒蛋白的常见细胞靶标。在这里，我们报告Id-1与乙型肝炎病毒（HBV）编码的蛋白质HBX相互作用，并调节其在肝细胞癌（HCC）细胞中的稳定性。我们发现在HCC细胞中，异位Id-1表达明显降低了HBX蛋白的半衰期，表明HBX被Id-1破坏了。同时，发现Id-1诱导的HBX降解受到蛋白酶体抑制剂治疗的抑制，表明该过程是通过蛋白酶体途径介导的。有趣的是，尽管Id-1不会诱导HBX泛素化，但我们发现去除HBX蛋白的所有赖氨酸残基可以保护它免受Id-1的影响，这表明Id-1介导的HBX仍需要泛素化降解。同时，我们发现Id-1与蛋白酶体亚基C8结合并促进其与HBX蛋白的相互作用，而这种相互作用的破坏完全消除了Id-1对HBX蛋白稳定性的负面影响。综上所述，我们的结果证明了Id-1通过与蛋白酶体相互作用来调节HBX蛋白稳定性的新功能。

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