IndraLab

Statements

USP49 binds STING1. 11 / 11
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"In this study, we demonstrated that USP49 interacted with MITA and deconjugated K63-linked polyubiquitin chains from MITA after HSV-1 infection, thereby downregulating MITA activation and turning down immune responses ( xref )."
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"In this context, we observed that USP49-MITA association was induced by HSV-1 infection and the basal expression of type I IFNs or proinflammatory cytokines was comparable between the wild-type and Usp49 -/- cells."
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"These data together suggest that USP49 interacts with MITA and inhibits MITA-mediated signaling."
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"Here, we report that USP49 interacts with and deubiquitinates MITA after HSV-1 infection, thereby turning down cellular antiviral responses."
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"To test our hypothesis, we conducted an unbiased screening of MITA-interacting DUBs by cotransfection and immunoprecipitation assays and found that USP49 interacted with MITA [ xref ]."
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"In an unbiased screening of MITA-interacting DUBs, we have found that USP49 interacts with MITA [ xref ]."
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"Whether and how the USP49-MITA axis regulates inflammatory diseases such as colitis and tumorigenesis such as colon cancer is of great interest and requires future investigations."
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reach
"USP49, a ubiquitin-specific protease, interacts with and deubiquitinates STING after HSV-1 infection."
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"USP49 interacts with MITA and inhibits MITA-mediated signaling."
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"Furthermore, USP49 binds to and deubiquitinates MITA, thus reducing antiviral responses after HSV-1 infection [ xref ]."
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No evidence text available
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