ArticleAutophagy2024
LTN1 promotes RLR degradation to inhibit immune response to RNA virus through the ESCRT pathway.
Article in Autophagy, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Deubiquitinase OTULIN dampens RIG-I-dependent antiviral signaling by removing linear ubiquitination from TRAF6.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Methadone maintenance therapy alters the expression of PLK1 and IFIH1 in patients with heroin addiction: a case-control study.Psychopharmacology · 2026Article
- Zinc finger protein ZNF33B facilitates Japanese encephalitis virus replication by regulating mCell & bioscience · 2026Article
- TRIB1 silencing attenuates epilepsy by restoring mitochondrial homeostasis and suppressing microglia-driven neuroinflammation via MAPK pathway inhibition.Journal of molecular histology · 2025Article
- Astrocyte Autophagy in Neurodegenerative Diseases: Current Progress in Mechanisms and Therapeutics.Neurochemical research · 2025Review
- Mechanism of action and new developments in the study of curcumin in the treatment of osteoarthritis: a narrative review.Inflammopharmacology · 2025Review
- Platinum nanoparticles in cancer therapy: chemotherapeutic enhancement and ROS generation.Medical oncology (Northwood, London, England) · 2025Review
- Histone deacetylase 8 promotes innate antiviral immunity through deacetylation of RIG-I.Frontiers in cellular and infection microbiology · 2024Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The excessive activation of immune responses will trigger autoimmune diseases or inflammatory injury. The endosomal sorting complexes required for transport (ESCRT) system can capture and mediate ubiquitinated protein degradation, which timely terminates signaling pathway hyperactivation. However, whether the ESCRT system participates in regulating RIGI-like receptor (RLR)-mediated antiviral responses remains unknown. In this study, we show that LTN1/listerin, a major component of RQC, can recruit E3 ubiquitin ligase TRIM27 to trigger K63-linked polyubiquitination of RIGI and IFIH1/MDA5. This K63-linked polyubiquitination facilitates the sorting and degradation of RIGI and IFIH1 proteins through the ESCRT-dependent pathway. Concordantly, LTN1 deficiency enhances the innate antiviral response to infection with RNA viruses. Thus, our work uncovers a new mechanism for RIGI and IFIH1 degradation and identifies the role of LTN1 in negatively regulating RLR-mediated antiviral innate immunity, which may provide new targets for the intervention of viral infection.
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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.