ArticleFrontiers in immunology2024
Ring finger protein 5 mediates STING degradation through ubiquitinating K135 and K155 in a teleost fish.
Article in Frontiers in immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- A teleost-specific oxygen-immunity axis where FIH activates NF-κB via competitive IκBα binding.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- STING single amino acid polymorphisms modulate iridovirus immune evasion and pathogenicity spectrum.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Bacterial effector screening reveals RNF214 as a virus restriction factor in mammals.PLoS pathogens · 2025Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Stimulator of interferon genes (STING) is a key connector protein in interferon (IFN) signaling, crucial for IFN induction during the activation of antiviral innate immunity. In mammals, ring finger protein 5 (RNF5) functions as an E3 ubiquitin ligase, mediating STING regulation through K150 ubiquitylation to prevent excessive IFN production. However, the mechanisms underlying RNF5's regulation of STING in teleost fish remain unknown. This study investigated the regulatory role of the mandarin fish (
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