Histone lactylation: epigenetic mark of glycolytic switch

Xiaofeng Dai; Xinyu Lv; Erik W Thompson; Kostya Ken Ostrikov

doi:10.1016/j.tig.2021.09.009

Histone lactylation: epigenetic mark of glycolytic switch

Trends Genet. 2022 Feb;38(2):124-127. doi: 10.1016/j.tig.2021.09.009. Epub 2021 Oct 7.

Authors

Xiaofeng Dai¹, Xinyu Lv², Erik W Thompson³, Kostya Ken Ostrikov⁴

Affiliations

¹ Wuxi School of Medicine, Jiangnan University, Wuxi 214122, China. Electronic address: xiaofeng.dai@jiangnan.edu.cn.
² Wuxi School of Medicine, Jiangnan University, Wuxi 214122, China.
³ Queensland University of Technology, School of Biomedical Sciences, Faculty of Health, Brisbane 4059, Australia; Translational Research Institute, Woolloongabba, QLD 4102, Australia.
⁴ Queensland University of Technology, School of Chemistry and Physics, Faculty of Science, Brisbane, QLD 4059, Australia.

PMID: 34627643
DOI: 10.1016/j.tig.2021.09.009

Abstract

Histone lactylation and acetylation compete for epigenetic modification of lysines and mark the levels of lactates and acetyl-CoA. Whether pyruvate is committed to lactate or acetyl-CoA generation as the outlet of glycolysis determines cell fate towards malignancy or not. Taking control over the glycolytic switch as marked by lactylation suggests novel therapeutic opportunities against cancers.

Keywords: acetylation; epigenetic mark; glycolysis switch; lactylation.

Publication types

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

MeSH terms

Acetyl Coenzyme A / genetics
Acetyl Coenzyme A / metabolism
Acetylation
Epigenesis, Genetic
Glycolysis* / genetics
Histones* / genetics
Histones* / metabolism

Substances

Histones
Acetyl Coenzyme A