Governing glutaminolysis by regulation of glutaminase succinylation

• 作者: Qingxia Ma Hongfei Jiang Leina Ma Ying Meng Dong Guo Yingying Tong Zhimin Lu
• 来源期刊: 蛋白质与细胞
• 年，卷（期）: 2022,（3）
• 所属期刊栏目: COMMENTARY
• 页码范围: 163-166
• 页数: 4页
• 语种: 英文

摘要

Of the 20 ribosomally coded amino acid residues,lysine(K)can be frequently and uniquely modified by many types of posttranslational acylation,including acetylation,suc-cinylation,crotonylation,propionylation,butyrylation,glu-tarylation,malonylation,β-hydroxybutyrylation,and 2-hydroxyisobutyrylation in histones and other proteins(Li et al.,2018a;Xu et al.,2021).Among these acylations,succinylation is a commonly occurred modification,and histone H3K79 succinylation is identified in the transcription start sites of more than 7,000 genes,implying its critical role in the expression regulation of a large number of genes(Wang et al.,2017).