IndraLab

Statements

USP22 activates CD274. 10 / 13
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"Stability, USP22 can promote PD-L1 to remove the ubiquitin chain and prevent it from being degraded by the proteasome [13–16] ."
37769523
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"Either CSN5 or USP22 enhanced the binding of PD-L1 with the other one."
37215134
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"Additionally, ubiquitin-specific peptidase 22 (USP22) in HCC [141], ubiquitin-specific peptidase 9, X-linked (USP9X) in OSCC [142], and ubiquitin C-terminal hydrolase L1 (UCHL1) in NSCLC [143] deubiquitinate and upregulate the PD-L1 expression.As a ubiquitously expressed protein, CMTM6 binds PD-L1 either at the plasma membrane or in recycling endosomes, repressing lysosome-mediated degradation of PD-L1 and upregulating protein half-time of PD-L1 without affecting the transcription level of PD-L1 [144, 145]."
34088360
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"On the one hand, USP22 could directly regulate PD-L1 stability through deubiquitination."
32665011
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"Knockdown of USP22 or OTUB1 only significantly reduces PD-L1 abundance in NCI-H358 cells but not in SK-MES-1 cells."
38167274
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"By modulating the stability of the CD274 protein by its deubiquitinase activity, USP22 prevents the proteasomal degradation of CD274 [74]."
39979972
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"On the one hand, USP22 can directly regulate the stability of PD-L1 through deubiquitination, leading to tumor immune resistance."
35935969
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"On the one hand, USP22 can directly regulate PD-L1 stability through deubiquitination [ 81 ]."
33989708
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"Our hypothesis is that the poor clinical efficacy of the treatments targeting PD-L1 may be due to the stabilization of PD-L1 mediated by USP22, abolishing the effect of anti-PD-L1 drugs."
32850399
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"USP22 knockdown reduces T cell-dependent tumor metastasis, increases the immunogenicity of tumors, increases the lymphatic invasion of tumors and natural killer cell activity [ 82 ], and enhances anti[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
33989708