Lysine Crotonylation: An Emerging Player in DNA Damage Response

The DNA damage response (DDR) system plays an important role in maintaining genome stability and preventing related diseases. The DDR network comprises many proteins and posttranslational modifications (PTMs) to proteins, which work in a coordinated manner to counteract various genotoxic stresses. L...

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Bibliographic Details
Published in:Biomolecules (Basel, Switzerland) Switzerland), 2022-10, Vol.12 (10), p.1428
Main Authors: Zhao, Yuqin, Hao, Shuailin, Wu, Wenchi, Li, Youhang, Hou, Kaiping, Liu, Yu, Cui, Wei, Xu, Xingzhi, Wang, Hailong
Format: Article
Language:English
Subjects:
Acylation
Cell cycle
Crystal structure
Deoxyribonucleic acid
DNA
DNA biosynthesis
DNA damage
DNA damage response (DDR)
DNA double-strand break (DSB)
DNA repair
DNA replication stress response
Double-strand break repair
Enzymes
Epigenetics
Fatty acids
Gene regulation
Gene silencing
Genetic aspects
Genomes
Genotoxicity
Health aspects
Histones
Lysine
lysine crotonylation
Mammals
Medical research
Medicine, Experimental
Metabolism
Metabolites
Oxidation
Phosphorylation
Post-translational modification
Proteins
Review
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Summary:The DNA damage response (DDR) system plays an important role in maintaining genome stability and preventing related diseases. The DDR network comprises many proteins and posttranslational modifications (PTMs) to proteins, which work in a coordinated manner to counteract various genotoxic stresses. Lysine crotonylation (Kcr) is a newly identified PTM occurring in both core histone and non-histone proteins in various organisms. This novel PTM is classified as a reversible acylation modification, which is regulated by a variety of acylases and deacylases and the intracellular crotonyl-CoA substrate concentration. Recent studies suggest that Kcr links cellular metabolism with gene regulation and is involved in numerous cellular processes. In this review, we summarize the regulatory mechanisms of Kcr and its functions in DDR, including its involvement in double-strand break (DSB)-induced transcriptional repression, DSB repair, and the DNA replication stress response.
ISSN:2218-273X
2218-273X
DOI:10.3390/biom12101428