ArticleEBioMedicine2019
The deubiquitinase USP13 stabilizes the anti-inflammatory receptor IL-1R8/Sigirr to suppress lung inflammation.
Article in EBioMedicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 45 citations in OpenAlex.
- Increasing hydrophobicity in poly(amino acid) adjuvants elicits potent and durable anti-tumor immunityBioactive materials · 2027Article
- Molecular scissors for inflamed lungs: targeting ubiquitin-specific peptidases in acute lung injury.Thorax · 2026Article
- Targeting USP14 enhances immunotherapy response by reprogramming tumor-associated macrophages in colon cancer.iScience · 2026Article
- Article
- Characteristics of T-Cells Expressing IL-37 and Its Receptors in Inflammatory Bowel Disease.International journal of molecular sciences · 2026Article
- USP13 stabilizes NLRP3 to facilitate inflammasome activation by preventing TRIM31-mediated NLRP3 ubiquitination and degradation.Science advances · 2025Article
- Beyond Negative Regulation: IL-1R8 and IL-1R2 as Novel Immune Checkpoints.European journal of immunology · 2025Review
- YY1 induced USP13 transcriptional activation drives the malignant progression of hepatocellular carcinoma by deubiquitinating WWP1.Cellular & molecular biology letters · 2025Article
- RNA aptamer-mediated RNA nanotechnology for potential treatment of cardiopulmonary diseases.Pharmacological research · 2025Review
- Advancements in omics technologies: Molecular mechanisms of acute lung injury and acute respiratory distress syndrome (Review).International journal of molecular medicine · 2025Review
- YOD1 regulates microglial homeostasis by deubiquitinating MYH9 to promote the pathogenesis of Alzheimer's disease.Acta pharmaceutica Sinica. B · 2025Article
- Lung contusion complicated by pneumonia worsens lung injury via the inflammatory effect of alveolar small extracellular vesicles on macrophages and epithelial cells.The journal of trauma and acute care surgery · 2025Article
- USP13 ameliorates nonalcoholic fatty liver disease through inhibiting the activation of TAK1.Journal of translational medicine · 2024Article
- Molecular Regulation of Transforming Growth Factor-β1-induced Thioredoxin-interacting Protein Ubiquitination and Proteasomal Degradation in Lung Fibroblasts: Implication in Pulmonary Fibrosis.Journal of respiratory biology and translational medicine · 2024Article
- USP13 regulates cell senescence through mediating MDM2 stability.Life sciences · 2023Article
- SIGIRR-caspase-8 signaling mediates endothelial apoptosis in Kawasaki disease.Italian journal of pediatrics · 2023Article
- Elucidating the role of ubiquitination and deubiquitination in osteoarthritis progression.Frontiers in immunology · 2023Review
- Deubiquitinase USP13 regulates glycolytic reprogramming and progression in osteosarcoma by stabilizing METTL3/mInternational journal of biological sciences · 2023Article
- Disease-related blood-based differential methylation in cystic fibrosis and its representation in lung cancer revealed a regulatory locus inEpigenetics · 2022Article
- Role of USP13 in physiology and diseases.Frontiers in molecular biosciences · 2022Review
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
backgroundThe Single immunoglobin interleukin-1 (IL-1)-related receptor (Sigirr), also known as IL-1R8, has been shown to exhibit broad anti-inflammatory effects against inflammatory diseases including acute lung injury, while molecular regulation of IL-1R8/Sigirr protein stability has not been reported. This study is designed to determine whether stabilization of IL-1R8/Sigirr by a deubiquitinating enzyme (DUB) is sufficient to suppress inflammatory responses and lessen lung inflammation.
methodsA molecular signature of ubiquitination and degradation of IL-1R8/Sigirr was determined using a receptor ligation chase model. The anti-inflammatory effects on USP13 were investigated. USP13 knockout mice were evaluated for stabilization of IL-1R8/Sigirr and disease phenotype in an acute lung injury model.
findingsIL-1R8/Sigirr degradation is mediated by the ubiquitin-proteasome system, through site-specific ubiquitination. This effect was antagonized by the DUB USP13. USP13 levels correlate directly with IL-1R8/Sigirr, and both proteins were reduced in cells and tissue from mice subjected to inflammatory injury by the TLR4 agonist lipopolysaccharide (LPS). Knockdown of USP13 in cells increased IL-1R8/Sigirr poly-ubiquitination and reduced its stability, which enhanced LPS-induced TLR4 signaling and cytokine release. Likewise, USP13-deficient mice were highly susceptible to LPS or Pseudomonas aeruginosa models of inflammatory lung injury. IL-1R8/Sigirr overexpression in cells or by pulmonary viral transduction attenuated the inflammatory phenotype conferred by the USP13
interpretationStabilization of IL-1R8/Sigirr by USP13 describes a novel anti-inflammatory pathway in diseases that could provide a new strategy to modulate immune activation. FUND: This study was supported by the US National Institutes of Health (R01HL131665, HL136294 to Y.Z., R01 GM115389 to J.Z.).
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