IndraLab

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COPS6 inhibits CDKN2A. 18 / 18
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"Furthermore, CSN6 decreased the stability of tumor suppressor p16 in an ubiquitin-independent proteasomal degradation pathway and thereby promoted tumorigenicity (Figure 7)."
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"To explore whether the 20S proteasome activator REGγ was involved in CSN6 induced p16 degradation, we performed co-IP to examine the interaction of the proteins."
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"Taken together, the above data demonstrated that CSN6 downregulated p16 stability through regulating the 20S proteasome ubiquitin-independent degradation pathway."
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"CSN6 promoted p16 degradation in gastric cancer via ubiquitination 15."
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"Our mechanistic studies indicated that CSN6 interacted with p16, and that CSN6-mediated p16 downregulation was suppressed by a proteasome inhibitor."
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"In the current study, we examined the mechanism underlying the CSN6-mediated p16 degradation."
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"It is our goal to confirm whether CSN6 promotes the degradation of p16 via an ubiquitination pathway."
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"CSN6 downregulates p16 via proteasomal degradation ."
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"The mechanism underlying CSN6-mediated p16 degradation in GC remains to be explored."
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"Thus, we may reach a conclusion that CSN6 promotes p16 degradation through an ubiquitin-independent pathway."
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"CSN6 downregulates p16 in a dose-dependent manner."
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"In gastric cancer, CSN6 degrades p16 and promotes tumour progression through ubiquitination 15."
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"Together, these results suggested that CSN6 was able to negatively regulate p16 in a dose-dependent manner."
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"Du et al (42) demonstrated that CSN6 promoted the occurrence of gastric cancer via the ubiquitin-independent proteasomal degradation of p16INK4a."
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"These observations demonstrated that CSN6 might promote the 20S proteasomal ubiquitin-independent degradation of p16."
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"Thus, CSN6 may downregulate p16 by proteasomal degradation."
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"We then validated whether ubiquitination is involved in CSN6-mediated p16 degradation."
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"Ubiquitination assay was performed to validate whether ubiquitination is involved in CSN6-mediated p16 degradation."
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