《生命科学》 2023, 35(8): 1071-1079
泛素特异性蛋白酶30在线粒体动力学和自噬中的作用研究进展
摘 要:
线粒体作为细胞的能量中心,在细胞内呈现高度的动态变化,其数量、质量及功能的稳定对维持细胞的正常活动至关重要。线粒体动力学与线粒体自噬之间可互相调控,共同构成线粒体质量控制的重要环节。泛素特异性蛋白酶30 (USP30) 作为去泛素化酶,既可通过线粒体融合蛋白1/2 (Mfn1/2)、线粒体动力蛋白相关蛋白1 (Drp1) 等融合与分裂蛋白参与调控线粒体动力学过程,还能通过E3 泛素连接酶Parkin、泛素(Ub) 及电压依赖性阴离子通道1 (VDAC1) 等多种信号而调控PTEN 诱导激酶1 (PINK1)/Parkin 途径介导的线粒体自噬,但其详细机制尚未完全阐明。本文对USP30 在调控线粒体动力学和线粒体自噬中的作用与其机制进行了综述。
通讯作者:尚画雨 , Email:santanasan@163.com
Abstract:
Mitochondrion, as an important energy center, presents highly dynamic changes in cells, and the stability of its quantity, quality and function is essential to maintain the normal activities of cells. Mitochondrial dynamics and mitophagy can be mutually regulated, which together constitute important parts of mitochondrial quality control. Ubiquitin-specific protease 30 (USP30), as a deubiquitinating enzyme, not only participates in the regulation of mitochondrial dynamics through deubiquitinating fusion and fission proteins such as mitofusin 1/2 (Mfn1/2) and dynamin-related protein 1 (Drp1), but also deubiquitinates E3 ubiquitin ligase Parkin, ubiquitin (Ub) and voltage-dependent anion channel 1 (VDAC1) to regulate PTEN-induced kinase 1 (PINK1)/Parkin-mediated mitophagy. This article reviews the role and mechanism of USP30 in regulating mitochondrial dynamics and mitophagy.
Communication Author:SHANG Hua-Yu , Email:santanasan@163.com