期刊
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
卷 9, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fcell.2021.667684
关键词
glutarylation; SIRT5; glutaryl-CoA; PTM; proteomic
资金
- National Natural Science Foundation of China [82002172]
- Program for Science and Technology Development in Henan Province [202102310205, 192102310350, 192102310379]
- Key Scientific Research Project Plan of Henan Province [20A180001]
- China Postdoctoral Science Foundation [2020M682279]
- Henan University Medical National Natural Science Foundation Cultivation Program
Lysine glutarylation is a newly discovered post-translational modification involved in metabolism regulation, oxidative damage, chromatin dynamics, and disease development. The process is reversible and evolving computational tools enable better prediction of modification sites.
Lysine glutarylation (Kglu) is a newly discovered post-translational modification (PTM), which is considered to be reversible, dynamic, and conserved in prokaryotes and eukaryotes. Recent developments in the identification of Kglu by mass spectrometry have shown that Kglu is mainly involved in the regulation of metabolism, oxidative damage, chromatin dynamics and is associated with various diseases. In this review, we firstly summarize the development history of glutarylation, the biochemical processes of glutarylation and deglutarylation. Then we focus on the pathophysiological functions such as glutaric acidemia 1, asthenospermia, etc. Finally, the current computational tools for predicting glutarylation sites are discussed. These emerging findings point to new functions for lysine glutarylation and related enzymes, and also highlight the mechanisms by which glutarylation regulates diverse cellular processes.
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