Protein lysine crotonylation: past, present, perspective

Lysine crotonylation has been discovered in histone and non-histone proteins and found to be involved in diverse diseases and biological processes, such as neuropsychiatric disease, carcinogenesis, spermatogenesis, tissue injury, and inflammation. The unique carbon-carbon pi -bond structure indicates that lysine crotonylation may use distinct regulatory mechanisms from the widely studied other types of lysine acylation. In this review, we discussed the regulation of lysine crotonylation by enzymatic and non-enzymatic mechanisms, the recognition of substrate proteins, the physiological functions of lysine crotonylation and its cross-talk with other types of modification. The tools and methods for prediction and detection of lysine crotonylation were also described.

Automated summary

Lysine crotonylation, discovered in both histone and non-histone proteins, is involved in various diseases and biological processes. Unique in its carbon-carbon pi-bond structure, lysine crotonylation may utilize distinct regulatory mechanisms and has interactions with other types of modifications. Tools and methods for predicting and detecting lysine crotonylation have also been discussed.