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USP29 binds CGAS. 8 / 8
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"In addition, USP29 selectively interacted with cGAS but not with other molecules including MITA, RIG-I, MAVS, TBK1 or IRF3 (Supplementary information, Fig.S2d)."
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"Interestingly, we found that TRIM38 constitutively interacts with cGAS but not with USP29, whereas USP29 constitutively interacts with cGAS but not with TRIM38 (Supplementary information, Fig.S2h), indicating that TRIM38 and USP29 independently interacts with and regulates cGAS."
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"Because USP29 interacts with cGAS and its enzyme activity is required for regulating antiviral signaling, we investigated whether USP29 eliminated polyubiquitin chains from cGAS."
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"Together, these data suggest that USP29 interacts with cGAS directly and constitutively in resting cells and after HSV-1 infection."
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"To test this hypothesis, we conducted an unbiased screening of cGAS interacting DUBs by cotransfection and immunoprecipitation assays as previous established, XREF_BIBR - XREF_BIBR and found that USP25 and USP29 interacted with cGAS in such a system."
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"Results from endogenous immunoprecipitation assays suggested that USP29 constitutively interacted with cGAS in bone marrow derived macrophages (BMDMs), bone marrow derived dendritic cells (BMDCs), mouse embryonic fibroblasts (MEFs), mouse lung fibroblasts (MLFs) or human monocytic THP-1 cells and their association was potentiated after HSV-1 infection."
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"In addition, we found that TRIM38 and USP29 interacts with cGAS independently, suggesting that TRIM38 mediated sumoylation and USP29 mediated deubiquitination of cGAS cooperatively regulate the stability of cGAS."
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"Because USP29 interacted with cGAS and was upregulated by HSV-1 infection, we investigated its role in regulating HSV-1- or cytoplasmic DNA triggered innate immune signaling."
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