# Role of novel protein acylation modifications in sepsis

## TL;DR

This paper reviews new protein acylation modifications and their roles in sepsis, offering insights for diagnosis and treatment.

## Contribution

The first comprehensive analysis of seven lysine acylation modifications in sepsis pathogenesis.

## Key findings

- Novel PTMs like succinylation and lactylation are linked to sepsis progression.
- These modifications affect protein stability, activity, and localization in sepsis.
- Understanding these PTMs could lead to new diagnostic and therapeutic strategies.

## Abstract

Sepsis is a life-threatening organ dysfunction caused by a dysregulated host response to infection, exhibiting high global morbidity and mortality. Accumulating evidence indicates that post-translational modifications (PTMs), as pivotal epigenetic mechanisms, play a crucial role in regulating diverse biological processes. The significance of PTMs in sepsis is increasingly recognized, as they may influence disease progression by modulating protein stability, activity, and localization. In recent years, advances in mass spectrometry have elucidated a series of novel PTMs, including succinylation (Ksucc), S-palmitoylation, lactylation (Kla), crotonylation (Kcr), 2-hydroxyisobutyrylation (Khib), β-hydroxybutyrylation (Kbhb), and malonylation (Kmal). This review presents the first comprehensive analysis of the characteristics, functions, and implications of these seven lysine acylation modifications in the pathogenesis and progression of sepsis, aiming to provide valuable insights for diagnosis and therapeutic intervention.