Reversible phosphorylation of the 26S proteasome.
Reversible phosphorylation of the 26S proteasome.
复制标题
26S 蛋白酶体的可逆磷酸化
DOI：
10.1007/s13238-017-0382-x
复制
发表时间：
2017-04
期刊：
影响因子：
21.1
通讯作者：
Chen MJ
中科院分区：
文献类型：
--
作者：
Guo X;Huang X;Chen MJ
位于泛素-蛋白酶体系统(UPS)中心的26S蛋白酶体在真核生物的几乎所有细胞过程中都是必不可少的。关于蛋白酶体的一个常见误解是，一旦制造出来，它仍然是一个静态的、统一的复合体，具有自发的和结构性的蛋白质降解活性。最近的发现提供了令人信服的证据支持完全相反的情况，如26S蛋白酶体在各种生理病理条件下经历动态和可逆的磷酸化。本文综述了蛋白酶体磷酸化的历史和研究现状，并提出以蛋白酶体蛋白激酶/磷酸酶为靶点，作为临床干预多种人类疾病的一种新策略。
The 26S proteasome at the center of the ubiquitin-proteasome system (UPS) is essential for virtually all cellular processes of eukaryotes. A common misconception about the proteasome is that, once made, it remains as a static and uniform complex with spontaneous and constitutive activity for protein degradation. Recent discoveries have provided compelling evidence to support the exact opposite insomuch as the 26S proteasome undergoes dynamic and reversible phosphorylation under a variety of physiopathological conditions. In this review, we summarize the history and current understanding of proteasome phosphorylation, and advocate the idea of targeting proteasome kinases/phosphatases as a new strategy for clinical interventions of several human diseases.