Abstract
Lysine crotonylation (Kcr) refers to a type of modification in which crotonyl groups are transferred to lysine residues by histone crotonyltransferase (HCT) using crotonyl-coenzyme A (CoA) as a substrate. Kcr is distributed in core histones and in some nonhistone proteins. Histone crotonylation is a newly discovered epigenetic modification with a significant ability to regulate gene expression. Crotonylation occurs on the ε-amino group of lysine residues and results in a modification of the histone charge. Similar to acetylation, the substrate for crotonylation is a donor molecule, crotonyl-CoA, which is linked to the sulfhydryl group of CoA by a thioester bond. Crotonylation is involved in regulating a wide range of biological processes and diseases. With advances in detection technologies, the impact of histone crotonylation on tumors has been revealed. The present review examines the recent discoveries of histone crotonylation, its function in tumors and its regulatory mechanism, which will aid in elucidating the mechanisms of malignant tumor development and provide a theoretical foundation for the development of new targeted cancer therapies.