Alteration of mitochondrial protein succinylation against cellular oxidative stress in cancer  

作　　者：Jing Zhang Zi-Qin Han Yang Wang Qing-Yu He 

机构地区：[1]Department of Radiology,the First Affiliated Hospital of Jinan University,Guangzhou 510627,China [2]MOE Key Laboratory of Tumor Molecular Biology and Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes,Institute of Life and Health Engineering,College of Life Science and Technology,Jinan University,Guangzhou 510632,China [3]MOE Key Laboratory of Tumor Molecular Biology,the First Affiliated Hospital of Jinan University,Guangzhou 510627,China

出　　处：《Military Medical Research》2022年第5期637-638,共2页军事医学研究（英文版）

基　　金：the Guangdong Natural Science Research Grant(2019A1515010196).

摘　　要：Dear Editor,Lysine residue succinylation is a novel post-translational modification that recently attracted extensive attention.Succinylation is achieved by non-enzymatic processes or by a series of enzymes[like p300,lysine acetyltransferase 2A(KAT2A)]that transfer the succinyl groups from succinyl-coenzyme A(CoA)to the specific lysine,modulating protein function in various physiological processes[1].As a high-energy metabolite,succinyl-CoA is mainly produced within the mitochondrial matrix and peroxisomes.Its high-rate generation in the tricarboxylic acid(TCA)cycle and its impermeability across the mitochondrial inner membrane(due to its negative charge property)enhance succinyl-CoA accumulation within mitochondria.

关 键 词：MITOCHONDRIA SUCCINYLATION PHOSPHORYLATION GLUTAMINASE 

分 类 号：R730.2[医药卫生—肿瘤]