ArticleCell communication and signaling : CCS2023
Analysis of a macrophage carbamylated proteome reveals a function in post-translational modification crosstalk.
Article in Cell communication and signaling : CCS, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 5 citations in OpenAlex.
- SOD1 lactylation impair its enzymatic activity by conformational change to aggravate intervertebral disc degeneration.Nature communications · 2026Article
- Epigenetic modifications of immune cells in rheumatoid arthritis.Annals of medicine · 2025Review
- Integrative Multi-PTM Proteomics Reveals Dynamic Global, Redox, Phosphorylation, and Acetylation Regulation in Cytokine-Treated Pancreatic Beta Cells.Molecular & cellular proteomics : MCP · 2024Article
- Protein carbamylation and proteomics: from artifacts to elucidation of biological functions.Frontiers in analytical science · 2024Article
- Automated Immunoprecipitation Workflow for Comprehensive Acetylome Analysis.Methods in molecular biology (Clifton, N.J.) · 2024Article
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10 authors at 3 institutions in 1 country.
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Abstract
backgroundLysine carbamylation is a biomarker of rheumatoid arthritis and kidney diseases. However, its cellular function is understudied due to the lack of tools for systematic analysis of this post-translational modification (PTM).
methodsWe adapted a method to analyze carbamylated peptides by co-affinity purification with acetylated peptides based on the cross-reactivity of anti-acetyllysine antibodies. We also performed immobilized-metal affinity chromatography to enrich for phosphopeptides, which allowed us to obtain multi-PTM information from the same samples.
resultsBy testing the pipeline with RAW 264.7 macrophages treated with bacterial lipopolysaccharide, 7,299, 8,923 and 47,637 acetylated, carbamylated, and phosphorylated peptides were identified, respectively. Our analysis showed that carbamylation occurs on proteins from a variety of functions on sites with similar as well as distinct motifs compared to acetylation. To investigate possible PTM crosstalk, we integrated the carbamylation data with acetylation and phosphorylation data, leading to the identification 1,183 proteins that were modified by all 3 PTMs. Among these proteins, 54 had all 3 PTMs regulated by lipopolysaccharide and were enriched in immune signaling pathways, and in particular, the ubiquitin-proteasome pathway. We found that carbamylation of linear diubiquitin blocks the activity of the anti-inflammatory deubiquitinase OTULIN.
conclusionsOverall, our data show that anti-acetyllysine antibodies can be used for effective enrichment of carbamylated peptides. Moreover, carbamylation may play a role in PTM crosstalk with acetylation and phosphorylation, and that it is involved in regulating ubiquitination in vitro. Video Abstract.
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