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• W2024562564 abstract "The intracellular sensor DDX41 is important for generating innate responses to DNA viruses. Liu et al. demonstrate that the ubiquitin ligase TRIM21 degrades and thereby regulates DDX41-dependent responses. DDX41 is a sensor of intracellular double-stranded DNA (dsDNA) in myeloid dendritic cells (mDCs) that triggers a type I interferon response via the signaling adaptor STING. We identified the E3 ligase TRIM21 as a DDX41-interacting protein and found that knockdown of or deficiency in TRIM21 resulted in enhanced type I interferon responses to intracellular dsDNA and DNA viruses. Overexpression of TRIM21 resulted in more degradation of DDX41 and less production of interferon-β (IFN-β) in response to intracellular dsDNA. The SPRY-PRY domain of TRIM21 interacted with the DEADc domain of DDX41. Lys9 and Lys115 of DDX41 were the targets of TRIM21-mediated ubiquitination. TRIM21 is therefore an interferon-inducible E3 ligase that induces the Lys48 (K48)-linked ubiquitination and degradation of DDX41 and negatively regulates the innate immune response to intracellular dsDNA." @default.
• W2024562564 created "2016-06-24" @default.
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• W2024562564 date "2012-12-09" @default.
• W2024562564 modified "2023-10-17" @default.
• W2024562564 title "The E3 ubiquitin ligase TRIM21 negatively regulates the innate immune response to intracellular double-stranded DNA" @default.
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• W2024562564 doi "https://doi.org/10.1038/ni.2492" @default.
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