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USP8 inhibition regulates autophagy flux and controls Salmonella infection
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Journal Article
USP8 inhibition regulates autophagy flux and controls Salmonella infection
2023
Overview
Ubiquitination is an important protein modification that regulates various essential cellular processes, including the functions of innate immune cells. Deubiquitinases are enzymes responsible for removing ubiquitin modification from substrates, and the regulation of deubiquitinases in macrophages during infection with
Typhimurium and
remains unknown.
To identify deubiquitinases regulated in human macrophages during bacterial infection, an activity-based proteomics screen was conducted. The effects of pharmacological inhibition of the identified deubiquitinase, USP8, were examined, including its impact on bacterial survival within macrophages and its role in autophagy regulation during
infection.
Several deubiquiitnases were differentially regulated in infected macrophages. One of the deubiquitinases identified was USP8, which was downregulated upon
infection. Inhibition of USP8 was associated with a decrease in bacterial survival within macrophages, and it was found to play a distinct role in regulating autophagy during
infection. The inhibition of USP8 led to the downregulation of the p62 autophagy adaptor.
The findings of this study suggest a novel role of USP8 in regulating autophagy flux, which restricts intracellular bacteria, particularly during
infection.
Publisher
Frontiers Media SA,Frontiers Media S.A
Subject
/ Bacteria
/ Cellular and Infection Microbiology
/ Deubiquitinating Enzymes - metabolism
/ Endosomal Sorting Complexes Required for Transport - genetics
/ Enzymes
/ Humans
/ Labeling
/ Proteins
/ Salmonella typhimurium - metabolism
/ Ubiquitin Thiolesterase - genetics
/ Ubiquitin Thiolesterase - metabolism
/ USP8
