ArticleVirology journal2011
Enterovirus 71 induces degradation of TRIM38, a potential E3 ubiquitin ligase.
Article in Virology journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- TRIM38 Suppresses Breast Cancer Progression via Modulating SQSTM1 Ubiquitination and Autophagic Flux.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Article
- TRIM38 suppresses migration, invasion, metastasis, and proliferation in non-small cell lung cancer (NSCLC) via regulating the AMPK/NF-κB/NLRP3 pathway.Molecular and cellular biochemistry · 2024Article
- Role of protein Post-translational modifications in enterovirus infection.Frontiers in microbiology · 2024Review
- Tripartite motif 38 alleviates the pathological process of NAFLD-NASH by promoting TAB2 degradation.Journal of lipid research · 2023Article
- Tripartite motif 38 attenuates cardiac fibrosis after myocardial infarction by suppressing TAK1 activation via TAB2/3 degradation.iScience · 2022Article
- Emerging Roles of MHC Class I Region-Encoded E3 Ubiquitin Ligases in Innate Immunity.Frontiers in immunology · 2021Review
- An update on enterovirus 71 infection and interferon type I response.Reviews in medical virology · 2019Review
- Conserved structural and functional aspects of the tripartite motif gene family point towards therapeutic applications in multiple diseases.Pharmacology & therapeutics · 2018Review
- Multifaceted roles of TRIM38 in innate immune and inflammatory responses.Cellular & molecular immunology · 2017Review
- Toll-like receptor 3 in viral pathogenesis: friend or foe?Immunology · 2013Review
- TRIM38 negatively regulates TLR3-mediated IFN-β signaling by targeting TRIF for degradation.PloS one · 2012Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe tripartite motif (TRIM) proteins are a family of more than 70 members in human. However, only a few of them have been well studied. The TRIM proteins contain the conserved RING, B-box, coiled-coil, and SPRY domains, most of which are involved in protein ubiquitination. TRIM38 is a member of the TRIM protein family, which we studied in more detail here as its functions are largely unknown.
resultsOur study shows that, similar to other TRIM family members, TRIM38 is localized in the cytoplasm. TRIM38 increases ubiquitination of other cellular proteins and catalyzes self-ubiquitination. TRIM38 also promotes K63- and K48-linked ubiquitination of cellular proteins. An intact RING domain is important for the functions of TRIM38. In addition, enterovirus 71 infection induces TRIM38 degradation.
conclusionsOur observations demonstrate that TRIM38 has E3 ubiquitin ligase activity and can be degraded during virus infection. These findings may provide insight into innate immune signaling pathways.
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