Lysine Crotonylation: An Emerging Player in DNA Damage Response

Yuqin Zhao; Shuailin Hao; Wenchi Wu; Youhang Li; Kaiping Hou; Yu Liu; Wei Cui; Xingzhi Xu; Hailong Wang

doi:10.3390/biom12101428

Lysine Crotonylation: An Emerging Player in DNA Damage Response

Biomolecules. 2022 Oct 5;12(10):1428. doi: 10.3390/biom12101428.

Authors

Yuqin Zhao¹, Shuailin Hao¹, Wenchi Wu¹, Youhang Li¹, Kaiping Hou¹, Yu Liu¹, Wei Cui¹, Xingzhi Xu², Hailong Wang¹

Affiliations

¹ Beijing Key Laboratory of DNA Damage Response, College of Life Sciences, Capital Normal University, Beijing 100048, China.
² Guangdong Key Laboratory for Genome Stability & Disease Prevention and Carson International Cancer Center, Marshall Laboratory of Biomedical Engineering, China Shenzhen University School of Medicine, Shenzhen 518060, China.

Abstract

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.

Keywords: DNA damage response (DDR); DNA double-strand break (DSB); DNA replication stress response; lysine crotonylation.

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

DNA Damage
DNA Repair
Histones* / metabolism
Lysine* / chemistry
Protein Processing, Post-Translational

Substances

Lysine
Histones

Grants and funding

This work was supported by the National Natural Science Foundation of China (grant numbers 31971221 and 31370841) and the Beijing Natural Science Foundation (grant number 5182003) awarded to H.W.