IndraLab

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USP9X deubiquitinates CD274. 8 / 9
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"Mechanistically, they found that USP9X deubiquitinated PD-L1 and stabilized its protein expression, thereby promoting immune escape of tumor cells in OSCC using immunohistochemistry, immunoprecipitation, western blotting, liquid chromatography-mass spectrometry and a T-cell-mediated tumor cell killing assay.3."

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"Moreover, USP9X directly binds PD-L1, and USP9X reduces PD-L1 ubiquitination and increases its protein abundance."

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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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"In oral squamous cell carcinoma (OSCC), USP9X deubiquitinates PD-L1 as well as maintain its protein stable expression [164]."

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"Indeed, USP9X induces PD-L1 deubiquitination and regulates its stabilization by ubiquitin specific protease activity."

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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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"Moreover, USP9X, USP8, and CSN5 can deubiquitinate PD-L1, and OTUB1 increase PD-L1 levels by preventing new synthetic PD-L1 from entering the ERAD."

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"Our data indicate that USP9X deubiquitinates and stabilizes PD-L1."