IndraLab

Statements

USP22 inhibits CD274. 9 / 9
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"USP22 also deubiquitinated and stabilized CDC274 (PD-L1) to decrease the efficacy of CD274 targeted immunotherapy in mice."
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"In addition, USP22 deubiquitinated CD274 leading to the stabilization of its expression, knockdown of USP22 enhanced the anticancer immunity of CD274 in liver cancer [ 31 ]."
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"The loss of USP22 causes PD-L1 to be degraded at the post-translational level, which has been shown to reduce carcinogenesis and increase T cell-mediated cell death.101 PD-L1 targeted immunotherapy and CDDP-based chemotherapy were both shown to benefit from USP22 reduction in another research, highlighting the complex and important functions of the USP22-PD-L1 axis in cancer treatment."
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"By modulating the stability of the CD274 protein by its deubiquitinase activity, USP22 prevents the proteasomal degradation of CD274 [74]."
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"Replacing lysine with arginine in the intercellular domain of PD-L1 prevents USP22 depletion-induced downregulation of PD-L1, suggesting that USP22 stabilizes PD-L1 through deubiquitination of lysine (23)."
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"On the one hand, USP22 can directly regulate PD-L1 degradation through deubiquitination."
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"EZH2 inhibition transcriptionally upregulates USP22 expression, and upregulated USP22 further stabilizes PD-L1."
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"In a liver cancer mouse model, USP22 knockdown significantly enhanced the efficacy of combined PD-L1 targeted immunotherapy and cisplatin by boosting tumor immunogenicity [210]."
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"In LIHC and NSCLC, USP22 acts as a deubiquitinating enzyme for PD-L1, inhibiting the ubiquitin-proteasome degradation pathway of PD-L1 and thus leading to tumor immune escape (Huang et al., 2019; Wang et al., 2020)."
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