IndraLab

Statements


USP25 inhibits RIGI. 11 / 13
| 11

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"Similarly, USP21 has been reported to negatively regulate RIG-I by removing K63 linked ubiquitination [XREF_BIBR]."

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"USP3, USP21, and CYLD suppress RIG-I activation by removing the K63 polyubiquitin chain on the N-terminal CARD of RIG-I [ 19–21 ]."

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"In addition, USP21 depletion contributed to the significant production of IFNs by activating the RIG-I or STING pathway, raising the possibility that USP21 inhibitors may enhance immune responses against virus infection (Fan et al., 2014; Chen et al., 2017a)."

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"Collectively, these findings suggest that USP25 inhibits RIG-I and MDA5-dependent type I IFN signaling."

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"The deubiquitinases USP3 and USP21 inhibit RIG-I activity by removing K63-linked ubiquitin chains."
| PMC

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"Interestingly, USP21 inhibits both TRIM25- and RNF135 mediated antiviral response and RIG-I activation (XREF_FIG and not depicted)."

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"In particular, USP3, USP21, USP25 and USP15 have all been shown to directly inhibit RIG-I."

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"Both USP3 and USP21 negatively regulate RIG-I activation via the cleavage of Lys63-linked Ubs conjugated on the 2CARD [ 51,52 ]."

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"RIG-I is negatively regulated by a deubiquitinase, USP21 (Fan et al. 2014)."
| PMC

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"Conversely, the removal of Lys63-linked ubiquitylation by the cellular deubiquitylating enzymes (DUBs) ubiquitin C-terminal hydrolase 3 (USP3), USP21 and CYLD, represses RIG-I signalling (reviewed in Ref."

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"USP21 and USP15 remove K63 linked polyubiquitin chains from RIG-I and block the ability of RIG-I to induce IFN-beta XREF_BIBR XREF_BIBR."