IndraLab

Statements

CD274 binds USP22. 25 / 37
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"USP22 directly interacts with the C-terminus of PD-L1, thereby inducing its deubiquitination and stabilization."
38474186
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"USP22 physically interacted with PD-L1."
32665011
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"Now that USP22 could regulate PD-L1 protein level, we asked whether USP22 interacted with PD-L1."
32665011
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"We performed co-immunoprecipitation assays in HEK293FT and H157 cells respectively, and we found that USP22 interacted with PD-L1 (Fig.  xref a, Additional file xref : Fig. S2A)."
32665011
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"Thus, we validated the interaction between USP22 and PD-L1."
32665011
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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. xref 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. xref According to a recent research, the tumor-promoting long noncoding RNA (lncRNA) KCNQ1OT1 controls the ubiquitination of PD-L1 and decreases the response of CD8 + T cells via the miR-30a-5p/USP22 pathway."
37396527
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"USP22 may be a particularly attractive target for cancer immunotherapy, because USP22 can limit the effect of anti-tumor immune response in Treg cells, and there is currently evidence that USP22 can i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
37769523
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"The deubiquitinase USP22 can bind with PD-L1 and enhance its stability, leading to reduced T cell cytotoxicity in tumor cells (76)."
36733484
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"In addition, USP22 could facilitated the interaction between CSN5 and PD-L1, and CSN5 promoted the interaction between USP22 and PD-L1."
32665011
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"Another study also showed that USP22 interacted with PD-L1, enhancing its stability by removing ubiquitin and preventing its breakdown by the proteasome."
38638430
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"Another study revealed that USP22 interacts with the C terminus of PD-L1 and deubiquitinates it."
37415977
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"Our results showed that CSN5 enhanced the interaction between USP22 and PD-L1 (Fig.  xref a)."
32665011
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"XREF_BIBR, XREF_BIBR While USP22 interacts with PD-L1 and inhibits PD-L1 ubiquitination, this DUB binds and stabilizes CSN5, suggesting that its PD-L1-regulatory function may involve coordination with CSN5."
33436547
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"Furthermore, we confirmed the interaction between USP22 and PD-L1 both in HEK293FT and NSCLC cells."
32665011
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"The deubiquitinase USP22 can bind with PD-L1 and enhance its stability, leading to reduced T cell cytotoxicity in tumor cells ( xref )."
36733484
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"That is, USP22 enhanced CSN5 stability and in turn facilitated the interaction of USP22 and PD-L1, indicating that USP22 and CSN5 worked cooperatively to regulate PD-L1."
32665011
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"Our data showed that USP22 interacted with PD-L1 and promoted its stability."
32665011
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"USP22 interacted with PD-L1 and maintained PD-L1 stability via deubiquitination in A549, H1299 and H1792 NSCLC cells ( xref )."
37215134
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"USP7, USP22, USP8, USP18, USP9X and USP5 have been demonstrated directly bind with PD-L1 to induce its deubiquitination and stabilization [60, 100–102, 143, 164, 186]."
37658402
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"USP22 enhances the stability of CSN5, which, in turn, promotes the interaction between USP22 and PD-L1, suggesting that USP22 and CSN5 synergistically regulate PD-L1."
35935969
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"USP22 enhances the stability of CSN5, which, in turn, promotes the interaction between USP22 and PD-L1, suggesting that USP22 and CSN5 synergistically regulate PD-L1.It should be noted that USP22 plays a positive regulatory role in certain T-cell subsets."
35935969
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"USP22 directly interacted with the C terminus of CD274, inducing its deubiquitination and stabilization and targeting USP22 is a promising strategy to potentiate anticancer immunity for CD274-amplifie[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
36328194
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"Our data showed that USP22 interacted with PD-L1 and promoted its stability."
32665011
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"Hepatocellular carcinoma is the tumor that better fits in the exploration of tumor inhibition mediated by USP22–PD-L1, because the expression of USP22 in this tumor is higher than its expression in other cancer types ( xref )."
32850399
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"USP22 directly interacted with the C terminus of CD274, inducing its deubiquitination and stabilization."
31399419