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Proteasomal activator 28 gamma stabilizes hepatitis B virus X protein by competitively inhibiting the Siah-1-mediated proteasomal degradation
Biochemical and Biophysical Research Communications ( IF 2.5 ) Pub Date : 2021-09-16 , DOI: 10.1016/j.bbrc.2021.09.028
Jiwoo Han 1 , Haeji Kim 1 , Hyerin Jeong 1 , Hyunyoung Yoon 1 , Kyung Lib Jang 2
Affiliation  

Proteasomal activator 28 gamma (PA28γ) upregulates the levels of HBx, a regulatory protein of hepatitis B virus (HBV) to stimulate HBV replication; however, the detailed mechanism remains unknown. Here, we found that PA28γ impaired the ability of seven in absentia homolog 1 (Siah-1) as an E3 ubiquitin ligase of HBx. PA28γ competitively inhibited the binding of Siah-1 to HBx in human hepatoma cells. Accordingly, PA28γ increased the stability of HBx and decreased HBx ubiquitination, abolishing the potential of Siah-1 to downregulate HBx levels. PA28γ also executed its role as an antagonist of Siah-1 during HBV replication, as demonstrated by an in vitro HBV replication system. The present study may provide insights into the mechanisms underlying the regulation of HBV replication.



中文翻译:

蛋白酶体激活剂 28 γ 通过竞争性抑制 Siah-1 介导的蛋白酶体降解来稳定乙型肝炎病毒 X 蛋白

蛋白酶体激活剂 28 γ (PA28γ) 上调 HBx 的水平,HBx 是乙型肝炎病毒 (HBV) 的一种调节蛋白,可刺激 HBV 复制;然而,详细的机制仍然未知。在这里,我们发现 PA28γ 损害了 7 个缺失同源物 1 (Siah-1) 作为 HBx 的 E3 泛素连接酶的能力。PA28γ 竞争性抑制人肝癌细胞中 Siah-1 与 HBx 的结合。因此,PA28γ 增加了 HBx 的稳定性并降低了 HBx 泛素化,消除了 Siah-1 下调 HBx 水平的潜力。PA28γ 在 HBV 复制过程中也发挥了其作为 Siah-1 拮抗剂的作用,如体外HBV 复制系统所证明的。本研究可能提供对 HBV 复制调控机制的深入了解。

更新日期:2021-09-20
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