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USP50 deubiquitinates STS. 9 / 9
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"In conclusion, we here demonstrate a novel regulatory mechanism regarding the ASC protein which is deubiquitinated by USP50 and provide experimental evidence emphasizing the importance of a regulatory mechanism mediated by ubiquitination and deubiquitination in inflammasome activation."
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"Wild-type USP50 and the Flag-USP50 (H322A) mutant significantly deubiquitinated the ASC protein."
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"Mechanistically, USP50 accelerates bile acid-induced NLRP3 inflammasome activation and pyroptosis via interacting with and deubiquitinating ASC in macrophages."
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"Expression of exogenous USP50 greatly decreased ASC ubiquitylation ( Figure 4E )."
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"However, the Flag-USP50 (C53S) mutant, did not affect polyubiquitination of the ASC protein, indicating that the Cys residue at position 53 is critical for the catalytic activity of USP50 deubiquitination of the ASC protein."
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"Taken together, these data suggested that USP50 physically interacted with and deubiquitinated ASC to induce ASC speck formation and oligomerization.3.5 USP50 stimulates HMGB1 release in DGR-induced gastric inflammation."
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"USP50 deubiquitinates the ASC protein."
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"To further confirm our finding that USP50 deubiquitinates the ASC protein, we performed in vitro deubiquitination assays."
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"Ubiquitination of Flag-ASC proteins was significantly decreased in the presence of Flag-USP50 protein, indicating that USP50 directly deubiquitinates the polyubiquitination of the ASC protein."
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