Processes and therapeutic perspectives of acylation modifications of lysine and cysteine in tumors

Abstract Acylation modification plays a crucial role in tumor progression through altering protein homeostasis and localization. However, a comprehensive summary of these processes is lacking. Protein acylation modifications are comprehensively summarized and categorized based on the amino acids that are modified. This review focuses on modifications of the lysine (acetylation, succinylation, crotonylation, malonylation, and glutarylation) and cysteine (myristoylation and palmitoylation) groups. The key enzymes involved in the occurrence and erasure of different modifications, as well as their effects on protein stability, cell localization, and tumor progression, are highlighted. The targeted delivery systems related to acylation modification are summarized, and currently available commercial inhibitors are also reviewed. Finally, acylation modifications with therapeutic potential in Phase I clinical trials are reviewed.