Functions and Mechanisms of Lysine Glutarylation in Eukaryotes

Longxiang Xie; Yafei Xiao; Fucheng Meng; Yongqiang Li; Zhenyu Shi; Keli Qian

doi:10.3389/fcell.2021.667684

Functions and Mechanisms of Lysine Glutarylation in Eukaryotes

Front Cell Dev Biol. 2021 Jun 24:9:667684. doi: 10.3389/fcell.2021.667684. eCollection 2021.

Authors

Longxiang Xie¹, Yafei Xiao¹, Fucheng Meng¹, Yongqiang Li¹, Zhenyu Shi¹, Keli Qian²

Affiliations

¹ Institute of Biomedical Informatics, Cell Signal Transduction Laboratory, Bioinformatics Center, Henan Provincial Engineering Center for Tumor Molecular Medicine, School of Basic Medical Sciences, Huaihe Hospital, Henan University, Kaifeng, China.
² Infection Control Department, The First Affiliated Hospital of Chongqing Medical University, Chongqing, China.

Abstract

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.

Keywords: PTM; SIRT5; glutaryl-CoA; glutarylation; proteomic.

Publication types

Review