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USP7 deubiquitinates CD274. 10 / 10
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"Then, to further verify that USP7 can deubiquitinate PD-L1, Flag-PD-L1 was co-transfected with HA-His-Ub in the presence of HA-USP7 or not in HEK293cells."
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"Results in XREF_FIG E suggest that PD-L1 was strongly ubiquitinated (lane 2, XREF_FIG E) in the presence of MG132 but without HA-USP7, while HA-USP7 abolished PD-L1 ubiquitination (lane3, XREF_FIG E)."
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"USP7 can directly interact with and de-ubiquitinate PD-L1, and then enhance the immune escape level in tumor immunity and promote the progression of GC (34)."
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"Among them, USP9X, CSN5, USP22 and USP7 are responsible for the deubiquitination and stabilization of PD-L1 in tumor cells [98–101]."
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"USP7 mediates the deubiquitination of PD-L1, leading to increased PD-L1 expression."
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"Contrary, it is reported that PD-L1 can be deubiquitinated by CSN5, USP22, USP7, USP9X, and OTUB1 (Feng et al.)."
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"Similarly, treatment of MFC cells with mUSP7-sgRNA-lentivirus or Almac4 also led to similar results which further confirm the results derived from XREF_FIG G and H. All these results indicate that USP7 interacts with PD-L1 and deubiquitinates PD-L1 to promote the stability of PD-L1."
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"In the current study, we show that USP7 deubiquitinates PD-L1 to cause cancer immune resistance to promote cancer growth."
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"Hence, this might be attributed to USP7’s ability to deubiquitinate and stabilize PD-L1, consequently playing a role in tumor immune evasion (Gao et al., 2023)."
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"Co-IP showed that CPP-A11 obviously antagonized USP7-downregulated endogenous PD-L1 ubiquitination in the three types of human cancer cells (figure 2G) and also antagonized exogenous USP7-downregulated exogenous PD-L1 ubiquitination in HEK293 cells (figure 2H)."
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