S-glycosylation-based cysteine profiling reveals regulation of glycolysis by itaconate

• Published in: Nature chemical biology Vol. 15; no. 10; pp. 983 - 991
• Main Authors: Qin, Wei, Qin, Ke, Zhang, Yanling, Jia, Wentong, Chen, Ying, Cheng, Bo, Peng, Linghang, Chen, Nan, Liu, Yuan, Zhou, Wen, Wang, Yan-Ling, Chen, Xing, Wang, Chu
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.10.2019; Nature Publishing Group
• Subjects: 631/92/1643; 631/92/458; 631/92/475; 631/92/96; Aldolase; Biochemical Engineering; Biochemistry; Biology; Bioorganic Chemistry; Cell Biology; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Cysteine; Datasets; Enzymes; Fructose; Fructose-bisphosphate aldolase; Glutathione; Glycolysis; Glycosylation; Immune response; Inflammation; Inflammatory response; Labeling; Laboratories; Macrophages; Mass spectrometry; Metabolism; Metabolites; Pathogens; Peptides; Proteins; Proteomes; Scientific imaging; Substrates

Itaconate has been recently recognized as an anti-inflammatory metabolite involved in the pathogen–macrophage interface. Due to its weak electrophilicity, itaconate could modify cysteines of the protein KEAP1 and glutathione, which contribute to its anti-inflammatory effect. However, the substrates...