ArticleEMBO reports2024
Recognition of phylogenetically diverse pathogens through enzymatically amplified recruitment of RNF213.
Article in EMBO reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Article
- The role of E3 ubiquitin ligases in selective types of macroautophagy.EMBO reports · 2026Review
- RNF213-dependent lytic destruction ofProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Listeria promotes systemic infection by targeting the host deubiquitinase CYLD.Nature communications · 2026Article
- Cell-autonomous immunity as an integrated immune network against bacterial and viral pathogens.Nature microbiology · 2026Review
- Manipulation of nonclassical ubiquitin signaling by pathogenic bacteria.Current opinion in microbiology · 2026Review
- Degrons and degradation signals beyond short linear motifs.Nature chemical biology · 2026Review
- HoweLife · 2025Article
- Shigella flexneri evades LPS ubiquitylation through IpaH1.4-mediated degradation of RNF213.Nature structural & molecular biology · 2025Article
- ATP functions as a pathogen-associated molecular pattern to activate the E3 ubiquitin ligase RNF213.Nature communications · 2025Article
- Insights into non-proteinaceous ubiquitination.Biochemical Society transactions · 2025Review
- Shigella effector IpaH1.4 subverts host E3 ligase RNF213 to evade antibacterial immunity.Nature communications · 2025Article
- Bacterial effector screening reveals RNF214 as a virus restriction factor in mammals.PLoS pathogens · 2025Article
- Autophagy and Bacterial infections.Autophagy reports · 2025Review
- Bacterial Effector Screening Reveals RNF214 as a Virus Restriction Factor in Mammals.bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
14 authors.
Funding
Abstract
Innate immunity senses microbial ligands known as pathogen-associated molecular patterns (PAMPs). Except for nucleic acids, PAMPs are exceedingly taxa-specific, thus enabling pattern recognition receptors to detect cognate pathogens while ignoring others. How the E3 ubiquitin ligase RNF213 can respond to phylogenetically distant pathogens, including Gram-negative Salmonella, Gram-positive Listeria, and eukaryotic Toxoplasma, remains unknown. Here we report that the evolutionary history of RNF213 is indicative of repeated adaptation to diverse pathogen target structures, especially in and around its newly identified CBM20 carbohydrate-binding domain, which we have resolved by cryo-EM. We find that RNF213 forms coats on phylogenetically distant pathogens. ATP hydrolysis by RNF213's dynein-like domain is essential for coat formation on all three pathogens studied as is RZ finger-mediated E3 ligase activity for bacteria. Coat formation is not diffusion-limited but instead relies on rate-limiting initiation events and subsequent cooperative incorporation of further RNF213 molecules. We conclude that RNF213 responds to evolutionarily distant pathogens through enzymatically amplified cooperative recruitment.
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