典型文献
Alteration of mitochondrial protein succinylation against cellular oxidative stress in cancer
文献摘要:
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. It is therefore not surprising that mitochondrial proteins have a higher potential to be succinylated, although succinylation has been reported to be accumulated at transcriptional starting sites, modulating histones to regulate gene expression. Being a key component of the TCA cycle, the α-ketoglutarate dehydrogenase (α-KGDH) complex as the key source of succinyl-CoA has been found to interact with KAT2A in the nucleus for mediating histone succinylation on H3K79. Notably, only 1.0%–1.6% of the α-KGDH complex is located in the nucleus, which consequently contributes to histone succinylation[2].
文献关键词:
中图分类号:
作者姓名:
Jing Zhang;Zi?Qin Han;Yang Wang;Qing?Yu He
作者机构:
Department of Radiology,the First Affiliated Hospital of Jinan University,Guangzhou 510627,China;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;MOE Key Laboratory of Tumor Molecular Biology,the First Affiliated Hospital of Jinan University,Guangzhou 510627,China
文献出处:
引用格式:
[1]Jing Zhang;Zi?Qin Han;Yang Wang;Qing?Yu He-.Alteration of mitochondrial protein succinylation against cellular oxidative stress in cancer)[J].军事医学研究(英文),2022(05):637-638
A类:
Lysine,Succinylation,KAT2A,succinyl,succinylated
B类:
Alteration,mitochondrial,succinylation,against,cellular,oxidative,stress,cancer,Dear,Editor,residue,novel,post,translational,modification,that,recently,attracted,extensive,attention,achieved,by,enzymatic,processes,series,enzymes,like,p300,lysine,acetyltransferase,groups,from,coenzyme,CoA,specific,modulating,function,various,physiological,energy,metabolite,mainly,produced,within,matrix,peroxisomes,Its,generation,tricarboxylic,acid,TCA,cycle,its,impermeability,across,inner,membrane,negative,charge,property,enhance,accumulation,therefore,not,surprising,proteins,have,higher,potential,although,has,been,reported,accumulated,transcriptional,starting,sites,histones,regulate,expression,Being,key,component,ketoglutarate,dehydrogenase,KGDH,complex,source,found,interact,nucleus,mediating,H3K79,Notably,only,located,which,consequently,contributes
AB值:
0.551734
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