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Updated: Jul 13, 2026
Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
Published on: April 4, 2018
Site-specific profiling of lysine itaconylation via a thiol-based probe
Xia-Ping Fu1, Ziming Tang1, Chu Wang2
1College of Chemistry and Molecular Engineering, Synthetic and Functional Biomolecules Center, Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Peking University, Beijing 100871, China.
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Lysine itaconylation is a novel post-translational modification (PTM) that was recently discovered in macrophage proteomes mediated by the immunoregulatory metabolite, itaconate. However, comprehensive and high-accuracy analytical methods are currently lacking for the global identification of itaconylation sites in proteomes, which limits the study of their biological functions. Here, we developed a thiol-based bioorthogonal probe, BMAyne, to site-specifically profile itaconylation in macrophage proteomes by a chemoproteomic strategy. Notably, 31 endogenous itaconylation sites on 29 proteins were identified in lipopolysaccharide (LPS)-stimulated macrophages using BMAyne, which complemented the results obtained previously by the promiscuous antibody enrichment. Our effort provides a unique chemical tool to enrich endogenous lysine itaconylation and establishes a rich database for guiding subsequent functional studies of this unique lysine PTM.
