IndraLab

Statements


COPS5 activates CD274. 10 / 10
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"Either CSN5 or USP22 enhanced the binding of PD-L1 with the other one."

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"Inhibitors of CSN5 and HDAC2, identified as the posttranslational modification regulators of PD-L1, can reduce PD-L1 stability and nuclear localization, respectively, providing an effective approach for combinational therapy with the help of immune checkpoint therapy (41, 44, 47)."

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"Lim et al. [161] showed that NF-kB p65 induces COP9 signalosome 5 (CSN5) which is required for TNF-alpha mediated PD-L1 stabilization in cancer cells."

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"Thus, CSN5 inhibits PD-L1 degradation by proteasome complex (Lim et al, 2016)."

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"The insights gained from this research highlight the potential of curcumin in cancer treatment, particularly as a complementary approach to existing immunotherapies, by targeting CSN5-mediated stabilization of PD-L1."

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"Jab1 is a key regulatory factor and promotes the stabilization of PD-L1."

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"Another pathway is that the upregulation of CSN5 increased the stability of PD-L1 through the deubiquitination of PD-L1, thereby promoted the immune evasion of PC cells."

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"A current study described if, PD-L1 through CSN5 was coordinated by GATA3-AS1 because an earlier study implied that CSN5 mediated the PD-L1 protein deubiquitinating level."

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"Studies has shown that Jab1 mediates PD-L1 stabilization via the ubiquitination and degradation of PD-L1 [24, 29, 30]."

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"The p65 subunit of NF-κB directly augments the expression of COP9 signalosome complex subunit 5 (CSN5), thereby preventing PD-L1 proteasomal degradation through deebiquitinating it [65] ."