VDAC1型
电压依赖性阴离子通道
线粒体
氧化应激
细胞生物学
百草枯
氧化磷酸化
化学
生物化学
生物
线粒体ROS
粒体自噬
自噬
细胞凋亡
细菌外膜
大肠杆菌
基因
作者
Simona Reina,Stefano Conti Nibali,Marianna Flora Tomasello,Andrea Magrì,Angela Messina,Vito De Pinto
出处
期刊:Redox biology
[Elsevier]
日期:2022-05-01
卷期号:51: 102264-102264
被引量:27
标识
DOI:10.1016/j.redox.2022.102264
摘要
Unraveling the role of VDAC3 within living cells is challenging and still requires a definitive answer. Unlike VDAC1 and VDAC2, the outer mitochondrial membrane porin 3 exhibits unique biophysical features that suggest unknown cellular functions. Electrophysiological studies on VDAC3 carrying selective cysteine mutations and mass spectrometry data about the redox state of such sulfur containing amino acids are consistent with a putative involvement of isoform 3 in mitochondrial ROS homeostasis. Here, we thoroughly examined this issue and provided for the first time direct evidence of the role of VDAC3 in cellular response to oxidative stress. Depletion of isoform 3 but not isoform 1 significantly exacerbated the cytotoxicity of redox cyclers such as menadione and paraquat, and respiratory complex I inhibitors like rotenone, promoting uncontrolled accumulation of mitochondrial free radicals. High-resolution respirometry of transiently transfected HAP1-ΔVDAC3 cells expressing the wild type or the cysteine-null mutant VDAC3 protein, unequivocally confirmed that VDAC3 cysteines are indispensable for protein ability to counteract ROS-induced oxidative stress.
科研通智能强力驱动
Strongly Powered by AbleSci AI