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首页> 外文期刊>Journal of cellular physiology. >Lipopolysaccharide reduces USP13 stability through c-Jun N-terminal kinase activation in Kupffer cells
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Lipopolysaccharide reduces USP13 stability through c-Jun N-terminal kinase activation in Kupffer cells

机译：通过脂多糖减少USP13稳定在枯氏c-Jun n端激酶激活细胞

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摘要

Protein ubiquitination regulates protein stability, cellular localization, and enzyme activity. Deubiquitinases catalyze the removal of ubiquitin from target proteins and reverse ubiquitination. USP13, a deubiquitinase, has been shown to regulate a variety of cellular responses including inflammation; however, the molecular regulation of USP13 has not been demonstrated. In this study, we revealed that USP13 is degraded in response to lipopolysaccharide (LPS) in Kupffer cells. USP13 levels are significantly decreased in inflamed organs, including liver tissues from septic mice. LPS reduces USP13 protein stability, not transcription, in Kupffer cells. Furthermore, LPS increases USP13 polyubiquitination. Inhibition of proteasome, but not lysosome or immunoproteasome, attenuates LPS-induced USP13 degradation, suggesting USP13 degradation is mediated by the ubiquitin-proteasome system. A catalytically inactive form of USP13 exhibits similar degree of degradation compared with USP13 wild-type, suggesting that USP13 degradation is not dependent on its activity. Furthermore, USP13 degradation is dependent on new protein synthesis. Inhibition of c-Jun N-terminal kinase (JNK) attenuates USP13 degradation, indicating that JNK-dependent new protein synthesis is necessary for USP13 degradation. This study reveals a molecular mechanism of regulation of USP13 degradation in Kupffer cells in response to bacterial endotoxin.
机译：蛋白质泛素化调节稳定性、细胞定位和酶活动。从目标蛋白质,泛素逆转泛素化。调节多种细胞反应包括炎症;监管USP13尚未被证实。这项研究中,我们发现USP13退化对脂多糖(LPS)在枯氏细胞。在发炎的器官,包括肝脏组织败血症的老鼠。不是转录,在枯氏细胞。有限合伙人增加USP13 polyubiquitination。抑制蛋白酶体,但不溶酶体或immunoproteasome,变弱LPS-induced USP13退化,暗示USP13退化由ubiquitin-proteasome系统。催化地USP13展览的活动形式相似程度的退化与USP13相比野生型,表明USP13退化不依赖于其活动。退化是依赖于新的蛋白质合成。(物)变弱USP13退化,指示JNK-dependent新的蛋白质合成必要USP13退化。揭示了调控的分子机制USP13退化枯氏细胞反应细菌内毒素。

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