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

## TL;DR

This paper reviews how acylation modifications of lysine and cysteine affect tumor progression and explores their therapeutic potential.

## Contribution

The paper provides a comprehensive summary and categorization of acylation modifications on lysine and cysteine in tumors.

## Key findings

- Acylation modifications influence protein stability and tumor progression.
- Key enzymes and inhibitors related to acylation modifications are identified.
- Acylation modifications are being explored in Phase I clinical trials for therapeutic use.

## 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.

The online version contains supplementary material available at 10.1186/s12964-026-02707-4.