IndraLab

Statements

USP18 inhibits GSDMD. 11 / 11
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"USP18 enhances the autophagic degradation of GSDMD."
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"USP18 down-regulates the protein abundance of GSDMD, thereby inhibiting the activation of GSDMD and pyroptosis (Fig. 7)."
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"Accordingly, overexpression of USP18 decreases the GSDMD protein levels and LPS-triggered inflammation in vivo."
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"These findings indicate that the degradation of GSDMD induced by USP18 predominantly occurs through the autolysosome pathway rather than the proteasome pathway."
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"Moreover, USP18 was found to enhance the degradation of GSDMD induced by EBSS (Fig. S2K and L)."
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"Additionally, we found that the degradation of GSDMD triggered by USP18 was almost completely abolished in BECN1- or ATG5-KO cells (Fig. 2M and N)."
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"Additionally, single knockdown of SQSTM1/p62, OPTN, or CALCOCO2/NDP52 could not completely block USP18-mediated GSDMD degradation, while USP18 failed to increase the degradation of GSDMD in triple knockdown cells (Fig. 2Q and Fig. S2U)."
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"Collectively, these findings suggest that USP18 promotes GSDMD degradation through ubiquitination of GSDMD at K168, thereby impairing its subsequent pyroptosis."
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"To examine the potential role of MIB2 in regulating USP18-mediated GSDMD ubiquitination and degradation, we performed siRNA-mediated knockdown of MIB2 in HEK293T cells, and observed that MIB2 knockdown resulted in the abrogation of USP18-mediated ubiquitination of GSDMD (Fig. 5A and B) as well as USP18-mediated GSDMD degradation (Fig. 5C and D)."
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"USP18 depletion induces both GSDMD and GSDME-dependent pyroptosis upon IFN treatment."
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"Depletion of USP18 induced GSDMD and GSDME cleavage, both markers of pyroptosis, upon IFN treatment."
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