Role of novel protein acylation modifications in immunity and its related diseases

Abstract

The cross‐regulation of immunity and metabolism is currently a research hotspot in life sciences and immunology. Metabolic immunology plays an important role in cutting‐edge fields such as metabolic regulatory mechanisms in immune cell development and function, and metabolic targets and immune‐related disease pathways. Protein post‐translational modification (PTM) is a key epigenetic mechanism that regulates various biological processes and highlights metabolite functions. Currently, more than 400 PTM types have been identified to affect the functions of several proteins. Among these, metabolic PTMs, particularly various newly identified histone or non‐histone acylation modifications, can effectively regulate various functions, processes and diseases of the immune system, as well as immune‐related diseases. Thus, drugs aimed at targeted acylation modification can have substantial therapeutic potential in regulating immunity, indicating a new direction for further clinical translational research. This review summarises the characteristics and functions of seven novel lysine acylation modifications, including succinylation, S‐palmitoylation, lactylation, crotonylation, 2‐hydroxyisobutyrylation, β‐hydroxybutyrylation and malonylation, and their association with immunity, thereby providing valuable references for the diagnosis and treatment of immune disorders associated with new acylation modifications.