IndraLab

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USP7 deubiquitinates CD274. 4 / 4
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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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"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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"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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"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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