ArticleProceedings of the National Academy of Sciences of the United States of America2026
Deubiquitinase OTULIN dampens RIG-I-dependent antiviral signaling by removing linear ubiquitination from TRAF6.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed.
- OTULIN: a master regulator of linear ubiquitin homeostasis in immune signaling, inflammation, and disease.Frontiers in immunology · 2026Review
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Authors and funding
10 authors.
Funding
Abstract
Linear ubiquitination and deubiquitination represent critical regulatory mechanisms in inflammation and cell death, yet their roles in RIG-I-like receptor (RLR)-dependent signaling remain unclear. Here, we identified OTU deubiquitinase with linear linkage specificity (OTULIN) as a negative regulator of RIG-I-dependent type I IFN (IFN-I) signaling. Overexpression of OTULIN markedly attenuated NF-κB and IFNβ reporter activation triggered by RNA viruses or synthetic analogs, suppressed downstream gene expression, impaired IFN-I production, and diminished phosphorylation of IκBα, TBK1, and IRF3, thereby facilitating viral replication. Conversely, knockout of
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