《生命科学》 2023, 35(3): 307-314

衣康酸修饰的化学蛋白质组学分析

秦　为^1,* , 王　初^2,*

¹清华大学药学院，清华-北大生命科学联合中心，北京 100084 ²北京大学化学与分子工程学院，北大-清华生命科学联合中心，北京 100871

摘　要：

衣康酸是近年来被发现的参与到病原体- 宿主相互作用中的炎症调控代谢物。衣康酸由于其亲电性可以共价修饰蛋白质中的半胱氨酸，从而调控底物蛋白的功能并介导其在巨噬细胞中的抗炎活性。目前，科学家们利用化学蛋白质组学技术大规模地鉴定了巨噬细胞与病原菌中的衣康酸修饰蛋白及位点，揭示了衣康酸修饰在糖酵解、细胞死亡和炎性小体活化等过程中的重要调控作用。现就衣康酸修饰生物学功能及其化学蛋白质组学分析方法的研究进展进行综述，并对该领域的研究难点进行探讨和展望。

通讯作者：秦　为 , Email:weiqin@mail.tsinghua.edu.cn 王　初 , Email:；chuwang@pku.edu.cn

Chemoproteomic profiling of cysteine itaconation

QIN Wei^1,* , WANG Chu^2,*

¹School of Pharmaceutical Sciences, Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing 100084, China ²College of Chemistry and Molecular Engineering, Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China

Abstract:

Itaconate has been recently recognized as an immune-modulatory metabolite involved in the hostpathogen interface. Itaconate, as an α,β-unsaturated dicarboxylic acid, could covalently modify cysteine and modulate protein function, contributing to its anti-inflammatory effect in macrophages. Chemoproteomics enables the large-scale identification of itaconated proteins and sites in macrophages and pathogens, revealing the important regulatory roles of itaconate in biological processes including glycolysis, cell death and inflammasome activation. This review summarizes the recent progresses on itaconation in terms of its biological functions and chemoproteomic profiling methods, and highlights the research challenges in this field.

Communication Author：QIN Wei , Email:weiqin@mail.tsinghua.edu.cn WANG Chu , Email:；chuwang@pku.edu.cn