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COPS5 deubiquitinates CD274. 46 / 48
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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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"CSN5 deubiquitinates PD-L1 thereby preventing its proteasomal degradation."

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"Next we asked whether CSN5 deubiquitinates PD-L1 to increase protein stabilization."

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"Jab1 also suppresses the ubiquitination and degradation of programmed cell death-ligand 1 (PD-L1)."

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"Furthermore, CSN5 was reported to inhibit the ubiquitination of PD-L1 and β-catenin [16,38], which was confirmed in the present study."

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"CSN5, which is the fifth component of the COP9 signalosome complex, is responsible for de-ubiquitination and stabilization of PD-L1 and thereby, inhibition of T-cell mediated adaptive immune activity."

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"CSN5 then binds to and deubiquitinates PD-L1, thus enhancing expression of PD-L1."
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"In addition, Lim et al. found that TNF-α upregulates the expression of ubiquitin enzyme CSN5, which reduces the ubiquitination of PD-L1 and stabilizes its expression (41)."

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"TNF-alpha within the tumor microenvironment stabilizes PD-L1 expression by means of COP9 signalosome 5 (CSN5) that directly deubiquitinates PD-L1 and impedes degradation of PD-L1."

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"JAB1 could also de-ubiquitinate and stabilize PD-L1 which, in turn, leaded to T cell suppression (Lim et al. 2016)."

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"COP9 signalosome complex subunit 5 (CSN5), a JAMM family DUB, deubiquitinates and stabilizes PD-L1, thereby escaping T cell mediated immune surveillance."

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"The activation of the miR-676-3p/COPS5 axis induced by GATA3-AS1 promotes the deubiquitination of PD-L1 by upregulating CSN5, thereby causing immune escape.248The mechanism of tumor immune escape is extremely complex."

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"Deubiquitination and Stabilization of PD-L1 by CSN5."

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"Mechanistically, the downregulation of DAPK1 facilitates IKKβ-mediated COP9 signalosome 5 (CSN5) phosphorylation and further deubiquitinates PD-L1, which compromises NK cell-mediated killing effects [33]."

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"Its transcript COPS5 inhibits PD-L1 ubiquitination; thus, more PD-L1 can be synthesized."

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"Additionally, research indicates that COPS5 inhibits the ubiquitination and degradation of PD-L1."

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"Deubiquitination and Stabilization of PD-L1 by CSN5."

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"As mentioned above, PD-L1 can be deubiquitinated by CSN5 to enhance its stability."

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"Macrophages secrete the pro-inflammatory cytokine TNF-α to activate NF-κB and induce tumor cells to express CSN5 (85), which subsequently inhibits ubiquitination and degradation of PD-L1, thereby enhancing PD-L1/PD-1 interactions and evading immune surveillance by T cells."

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"Another inhibitor, curcumin (XREF_FIG E), inhibits a JAMM DUB CSN5 that deubiquitinates and stabilizes PD-L1, thereby destabilizing PD-L1 in various cancers [XREF_BIBR, XREF_BIBR]."

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"CSN5 binds PD-L1 and deubiquitinates PD-L1, enhancing PD-L1 stability, and evading T cell immune surveillance [97]."

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"For instance, lncRNA GATA3-AS1 can sequester miR-676-3p to promote the CSN5 level, which deubiquitinates PD-L1 and facilitates immunosuppression in TNBC [108]."

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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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"Moreover, GATA binding protein 3 antisense RNA 1 (GATA3-AS1) promotes PD-L1 deubiquitination by miR-676-3p/COPS5 (CSN5) in human TNBC cell lines."

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"After translation, NfKB regulates and maintains PD-L1 expression by inducing the transcription of the COPS5 gene, which deubiquitinates PD-L1 protein to stabilize PD-L1 on the cell membrane [11], [20] ( Fig. 3)."

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"Then, the results demonstrated that PD-L1 ubiquitination and downregulation of PD-L1 induced by GOLM1-KD was abolished by CSN5 overexpression (Fig. 3g, h)."

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"Although PD-L1 had notable basal ubiquitination, CSN5 abolished ubiquitination of PD-L1 (XREF_FIG)."

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"CSN5 can also directly deubiquitinate PD-L1 and maintains its stability in human non-small cell lung cancer and liver cancers (123,124)."

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"CSN5 directly deubiquitinates and stabilizes PD-L1 in cancer cells to escape from immune surveillance XREF_BIBR."

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"However, our results suggested that CSN5 directly deubiquitinates and stabilizes PD-L1 in cancer cells to escape from immune surveillance."

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"Aside from inhibiting ubiquitination, CSN5 further deubiquitinates PD-L1 directly."

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"In contrast, decreased PD-L1 on 4T1-EVs was observed when ubiquitinated PD-L1 was reduced by COP9 signalosome 5 (CSN5), which has been reported to mediate PD-L1 deubiquitination (Figures 2S and S2S)."

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"Moreover, CSN5 modulated the deubiquitination and stability of PD-L1."

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"CSN5, induced by NF-κB in response to inflammatory cytokine TNF-α, was reported to inhibit ubiquitination and degradation of PD-L1 protein [ 143 ]."

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"Mediated by tumor necrosis factor-alpha (TNF-α), CSN5 can deubiquitinate PD-L1 in cancer cells, maintain its stability, and escape immune surveillance (Lim et al., 2016)."

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"CSN5 in turn, prevents the ubiquitination of PD-L1, hinders its degradation and as a result enhances tumor escape from immunosurveillance."

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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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"On the other hand, as a deubiquitinase, CSN5 deubiquitinates PD-L1, promoting tumor progression and immune escape (12)."

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"The strongest citation burst occurred in 2018 for the article titled “Deubiquitination and Stabilization of PD-L1 by CSN5” (burst strength = 7.37)."

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"As discussed above in the section 3.2 , CSN5 suppresses the ubiquitination and degradation of PD-L1, which resulted in enhancement of PD-L1/PD-1 interaction to avoid immune surveillance."

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"In particular, CSN5 inhibited the ubiquitination of PD-L1 and enhanced its stability on the surface of tumor cells."

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"However, this approach lacks international collaboration, limiting the global impact of these research outcomes.The most frequently co-cited article (Deubiquitination and Stabilization of PD-L1 by CSN5, published in Cancer Cell) elucidates the critical role of DUBs in promoting tumor immune evasion through PD-L1 stabilization."

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"Jab1/CSN5 directly deubiquitinates and stabilizes PD-L1 through TNF-α in cancer cells to escape from immune surveillance."

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"Jab1 and COPS5 reduces PD-L1 ubiquitination and stabilizes it."

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"Collectively, the above results demonstrate that PDIA6 contributes to PC progression, which may be associated with CSN5-regulated deubiquitination of beta-catenin and PD-L1."

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"Western blot analysis manifested that the basic ubiquitination of PD-L1 was eliminated by CSN5 ( Fig. 4 H)."