IndraLab

Statements

USP51 binds PD‐L1. 5 / 5
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"At the molecular level, USP51 directly bound and deubiquitinated PD‐L1 at lysine residues K280 and K281."
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"These findings also supported our observation that disruption of USP51/PD‐L1‐deployed juxtacrine interaction with a USP51 inhibitor DHM showed a higher chemotherapeutic efficacy in NSCLC in vitro and in vivo, suggesting that chemo‐immunotherapy or a combined treatment of anti‐PD‐1/PD‐L1 with their specific inhibitors could potentially serve a therapeutic role in future anticancer therapies."
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"We further validated the physical interactions of PD‐L1 with USP51 (Figure  xref ), UCHL1 (Supplementary Figure xref ), RNF31 (Supplementary Figure xref ), and TRIM21 (Supplementary Figure xref ) in PD‐L1‐overexpressing A549 cells."
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"The results revealed that USP51 directly associated with PD‐L1 in A549 cells, which was further increased in A549 R cells (Figure  xref )."
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"In addition, three deletion constructs of PD‐L1‐C were generated to demonstrate that the deletion variant PD‐L1‐C3, but not PD‐L1‐C1 and PD‐L1‐C2, was able to interact with USP51 (Figure  xref ), highlighting that the PD‐L1C‐terminal region (280‐290aa) is critical for the USP51‐PD‐L1 association."
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