[PDF][PDF] The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA

T Tsuchida, J Zou, T Saitoh, H Kumar, T Abe… - Immunity, 2010 - cell.com
T Tsuchida, J Zou, T Saitoh, H Kumar, T Abe, Y Matsuura, T Kawai, S Akira
Immunity, 2010cell.com
The innate immune system detects pathogen-and host-derived double-stranded DNA
exposed to the cytosol and induces type I interferon (IFN) and other cytokines. Here, we
identified interferon-inducible tripartite-motif (TRIM) 56 as a regulator of double-stranded
DNA-mediated type I interferon induction. TRIM56 overexpression enhanced IFN-β promoter
activation after double-stranded DNA stimulation whereas TRIM56 knockdown abrogated it.
TRIM56 interacted with STING and targeted it for lysine 63-linked ubiquitination. This …
Summary
The innate immune system detects pathogen- and host-derived double-stranded DNA exposed to the cytosol and induces type I interferon (IFN) and other cytokines. Here, we identified interferon-inducible tripartite-motif (TRIM) 56 as a regulator of double-stranded DNA-mediated type I interferon induction. TRIM56 overexpression enhanced IFN-β promoter activation after double-stranded DNA stimulation whereas TRIM56 knockdown abrogated it. TRIM56 interacted with STING and targeted it for lysine 63-linked ubiquitination. This modification induced STING dimerization, which was a prerequisite for recruitment of the antiviral kinase TBK1 and subsequent induction of IFN-β. Taken together, these results indicate that TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses.
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