Crotonylation

Crotonylation is a post-translational modification where a crotonyl group is added to a protein. This modification primarily occurs on lysine residues, forming a crotonyl-lysine adduct. It is a relatively newly discovered modification, with research into its biological functions and mechanisms still ongoing.

The crotonyl group is derived from crotonyl-CoA, a metabolite produced during the breakdown of fatty acids and also found in the metabolisms of certain bacteria. This metabolic connection suggests that crotonylation may play a role in regulating cellular responses to metabolic states or environmental cues.

Evidence suggests that crotonylation can influence protein activity, stability, and interactions. It has been observed in various cellular compartments, including the nucleus and mitochondria, and implicated in processes such as DNA repair, gene regulation, and energy metabolism. The enzymes responsible for catalyzing crotonylation are called crotonyltransferases, and conversely, enzymes that remove the crotonyl group are known as decrotonylases.

Research into crotonylation is expanding our understanding of the complex regulatory landscape of proteins beyond canonical modifications like phosphorylation and acetylation. Its potential involvement in diseases, including cancer and metabolic disorders, is an active area of investigation. Further studies are needed to fully elucidate the precise roles and downstream consequences of this evolving post-translational modification.