IndraLab

Statements

COPS6 binds CARD16. 22 / 22
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"Recently, CSN6's interaction with COP1 is characterized in mammalian cells, and CSN6-COP1 axis is involved in 14-3-3σ degradation [ xref ]."
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"These observations led us to investigate the functional relevance of the interaction of CSN6 and COP1. xref shows that CSN6 associates with COP1 endogenously as assayed by co-ip and an In vitro binding assay confirms that CSN6 directly binds to COP1."
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"To address the significance of the CSN6 and COP1 interaction, we examined the impact of CSN6 on COP1 levels and noted that the steady-state level of COP1 increased when CSN6 was overexpressed ( xref )."
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"Co-IP shows that CSN6 associates with COP1 endogenously and in vivo binding assay confirms that CSN6 directly binds to COP1 [ xref ]."
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"The results illustrate a pathway regulation of FOXO4‐mediated serine/glycine metabolism through the function of CSN6‐COP1 axis."
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"Given that CSN6 associates with COP1 and that COP1 co-elutes with 14-3-3σ in gel filtration assays ( xref ), we reasoned that COP1 could be involved in CSN6-mediated 14-3-3σ ubiquitination."
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"For example, the stability of the p53-regulated protein 14-3-3σ, a cell cycle regulator, appears to be regulated through interactions with CSN6 and COP1 [ xref ]."
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"One study demonstrated that the CSN6–COP1 axis plays a critical role in controlling the stability of p27 [ xref ]."
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"Recently, CSN6 's interaction with COP1 is characterized in mammalian cells, and CSN6-COP1 axis is involved in 14-3-3sigma degradation [XREF_BIBR]."
26186957
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"These observations led us to investigate the functional relevance of the interaction of CSN6 and COP1."
21625211
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"To further confirm the CSN6‐COP1 axis is involved in regulating FOXO4 ubiquitination, we investigate the ubiquitination level of FOXO4 (428VP→AA) mutant in the presence of CSN6."
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"XREF_FIG shows that CSN6 associates with COP1 endogenously as assayed by co-ip and an In vitro binding assay confirms that CSN6 directly binds to COP1."
21625211
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"To address the significance of the CSN6 and COP1 interaction, we examined the impact of CSN6 on COP1 levels and noted that the steady-state level of COP1 increased when CSN6 was overexpressed (XREF_FIG)."
21625211
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"We show for the first time that COP9 signalosome subunit 6 (CSN6) associates with COP1 and is involved in 14-3-3σ ubiquitin-mediated degradation."
21625211
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"In this study, we found that CSN6, COP1 and 14-3-3σ interact and we demonstrated the role of the CSN6-COP1 axis in regulating 14-3-3σ stability."
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"A previous study has reported that CSN6 associates with COP1 and positively regulates its stability through inhibition of ubiquitin-mediated COP1 proteasomal degradation [ xref ]."
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"CSN6 can bind COP1, but the significance of this interaction is largely unknown."
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"Importantly, CSN6 not only associates with COP1 but also prevents COP1’s self-ubiquitination, adding yet another layer of regulation."
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"Moreover, CSN6 stabilizes COP1 through reducing COP1 self-ubiquitination and the CSN6-COP1 axis function as an E3 ubiquitin ligase involved in 14-3-3σ degradation to regulate cell growth and tumorigenicity xref , xref ."
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"To demonstrate the impact of CSN6‐COP1 axis in regulating FOXO4 and subsequent gene expression of SGOC genes in vivo, we performed mouse xenograft cancer studies and demonstrated that CSN6 knockdown suppressed tumor growth (Figure S17C, Supporting Information)."
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"Together, these data indicated that CSN6‐COP1 axis is involved in promoting FOXO4 ubiquitination."
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"CSN6 can bind COP1, but the significance of this interaction is largely unknown.In this study, we characterize the upstream regulators of the FOXO4 in tumorigenesis including EGF, PKB/Akt, CSN6 and COP1."
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