IndraLab

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OTUD3 activates MAVS. 5 / 5
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"Mechanistically, acetylation of the core OTU domain in OTUD3 markedly enhances deubiquitinase activity on MAVS (mitochondrial antiviral-signaling protein), thereby inhibiting the innate antiviral immune response."
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"Upon viral infection, sirtuin 1 (SIRT1) is recruited to deacetylate OTUD3, leading to the inactivation of OTUD3, which relieves MAVS suppression."
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"All these results indicate that OTUD3 represses MAVS aggregation and thus inhibits MAVS-mediated antiviral signaling.The findings reported above raised the question of how hosts respond rapidly to vir[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Remarkably, acetylation of OTUD3 on lysine 129 (K129) triggers deubiquitination of K63-polyubiquitination chains on MAVS thereby blocking the antiviral response (162) (Fig. 6B)."
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"Upon virus infection, SIRT1 was recruited to associate and co-localize with cytoplasmic OTUD3, which deacetylated OTUD3 and led to the loss of its ability to cleave MAVS Lys63-linked Ub."
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