ArticleNature communications2021
Ring finger protein 213 assembles into a sensor for ISGylated proteins with antimicrobial activity.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
95 citing papers in PubMed, 127 citations in OpenAlex.
- Article
- Understanding protein ISGylation, a multifaceted posttranslational modification.Cell chemical biology · 2026Review
- Article
- 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
- RNF213 in Panvascular Disease: A Molecular Hub Linking Genetic Susceptibility to Systemic Vasculopathy.Biomedicines · 2026Review
- Mutations in Exon 29 of Ring Finger Protein 213 Are Associated with Early-Onset Colorectal Cancer.Digestive diseases and sciences · 2026Article
- Cell-autonomous immunity as an integrated immune network against bacterial and viral pathogens.Nature microbiology · 2026Review
- Mechanisms influencing transient cytoplasmic protein targeting to intracellular lipid droplets.Biochemical Society transactions · 2026Review
- Mechanisms and strategies of host xenophagy manipulation by intracellular bacteria.Cellular and molecular life sciences : CMLS · 2026Review
- Review
- Manipulation of nonclassical ubiquitin signaling by pathogenic bacteria.Current opinion in microbiology · 2026Review
- RNF213 Is an Interferon-Stimulated Gene That Targets Influenza A Virus NP and Activates MDA5 to Restrict Infection.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Proximity proteomics reveals a role for IFI16 during human coronavirus infection.bioRxiv : the preprint server for biology · 2026Article
- Coral color morphs exhibit distinct microbial and proteomic profiles linked to stress and immune mechanisms in a changing ocean.Microbiome · 2026Article
- Ring finger protein 213 regulates B-cell receptor signaling, metabolism, and development in B lymphocytes.Signal transduction and targeted therapy · 2026Article
- Proximity labeling of thebioRxiv : the preprint server for biology · 2026Article
- Molecular and multimodal biomarkers in Moyamoya disease: from pathogenic mechanisms to clinical translation.European journal of medical research · 2026Review
- Reframing moyamoya vasculopathy within steno-occlusive disease of the circle of Willis.Frontiers in stroke · 2026Review
- Decreased <italic>Lactococcus lactis</italic> and Propionic Acid in Feces of Patients with Moyamoya Disease: Possible Implications of Immune Dysregulation.Cerebrovascular diseases (Basel, Switzerland) · 2026Article
35 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
26 authors at 7 institutions in 5 countries.
Funding
Abstract
ISG15 is an interferon-stimulated, ubiquitin-like protein that can conjugate to substrate proteins (ISGylation) to counteract microbial infection, but the underlying mechanisms remain elusive. Here, we use a virus-like particle trapping technology to identify ISG15-binding proteins and discover Ring Finger Protein 213 (RNF213) as an ISG15 interactor and cellular sensor of ISGylated proteins. RNF213 is a poorly characterized, interferon-induced megaprotein that is frequently mutated in Moyamoya disease, a rare cerebrovascular disorder. We report that interferon induces ISGylation and oligomerization of RNF213 on lipid droplets, where it acts as a sensor for ISGylated proteins. We show that RNF213 has broad antimicrobial activity in vitro and in vivo, counteracting infection with Listeria monocytogenes, herpes simplex virus 1, human respiratory syncytial virus and coxsackievirus B3, and we observe a striking co-localization of RNF213 with intracellular bacteria. Together, our findings provide molecular insights into the ISGylation pathway and reveal RNF213 as a key antimicrobial effector.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.