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USP22 Deubiquitinates CD274 to Suppress Anticancer Immunity.

Cancer Immunol Res. 2019; 
Huang Xing,Zhang Qi,Lou Yu,Wang Junli,Zhao Xinyu,Wang Lin,Zhang Xiaozhen,Li Shanshan,Zhao Yulan,Chen Qi,Liang Tingbo,Bai X
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Proteins, Expression, Isolation and Analysis Protein samples of immunoprecipitation or cell lysates were further resolved by SDS-PAGE with 4-20% 15-well SurePAGETM Gel (M00657, GenScript), and then transferred onto nitrocellulose membrane (66485, PALL) following standardprocedures. Get A Quote

摘要

PD-1 (CD279)-PD-L1 (CD274) inhibitory signaling is critical for cancer immune evasion, and thus has become one of the major targets in anticancer immunotherapy. There are several studies that demonstrate the potent effects of posttranslational modifications of CD274 on immune inactivation and suppression, such as ubiquitination, phosphorylation, glycosylation, and palmitoylation. However, the regulatory mechanisms for CD274 deubiquitination are still largely unclear. Here, we identified ubiquitin-specific protease 22 (USP22) as a novel deubiquitinase of CD274. USP22 directly interacted with the C terminus of CD274, inducing its deubiquitination and stabilization. Across multiple cancer types, ... More

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