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USP8 decreases the amount of CD274. 9 / 9
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"Therefore, we determined that USP8 could decrease PD-L1 degradation by reducing the ubiquitination level of PD-L1."
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"Xiong et al.’s research indicates that deubiquitinase USP8 downregulates PD-L1 protein levels by targeting K63-linked deubiquitination instead of K48-linked deubiquitination."
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"USP8 inhibition by DUB-IN-2 not only upregulated MHC I via NF-κB signaling but also increased PD-L1 levels by maintaining K63-linked polyubiquitination to improve the sensitivity of cells to ICB in vivo [22] (Table 1)."
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"In this study, we demonstrated that in pancreatic tumor cell lines, USP8 deficiency induced a time and dose-dependent decrease in the PD-L1 protein level and increased the amount and function of tumor-infiltrated activated T-cells."
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"USP8 Inhibition enhances protein expression of PD-L1 by increasing the TRAF6-mediated Lys63-linked polyubiquitin chains of PD-L1 to antagonize Lys48-linked ubiquitination and degradation of PD-L1."
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"Accordingly, silencing USP8 increased ubiquitination level and decreased protein level of PD-L1, without significantly affecting PD-L1 mRNA level."
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"For instance, deficiency of USP8 can enhance PD-L1 expression on tumor cell surfaces, increase infiltration of effector T-cells within the tumor microenvironment, and promote antitumor immunity [ 20 ][MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP8 downregulation led to an increase in ubiquitination level of PD-L1 (P < 0.01, Fig. 6D), no significant change in PD-L1 mRNA level (Fig. 6E), and decreased protein level of PD-L1 (P < 0.01, Fig. 6F)."
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"The findings showed that USP8 overexpression resulted in no change in PD-L1 mRNA level, decreased ubiquitination level of PD-L1, and increased protein level of PD-L1 (P < 0.05, Fig. 7B–D)."
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