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FASN binds USP22. 14 / 18
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"These results suggest that H 2 O 2 induces cells apoptosis by repressing the USP22-FASN axis in p53 +/+ colorectal cancer cells."
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"Depletion of the USP22-FASN axis inhibits cell growth and colorectal tumorigenesis."
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"Our study demonstrates that overproduced ROS in colorectal cancer controls lipid synthesis by critically regulating the USP22-FASN axis through a p53-dependent manner."
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"To determine the potential clinical relevance of the USP22-FASN axis, we next assessed the expression of USP22 and FASN proteins in serial sections of 108 human CRC specimens, and found that FASN expression levels were significantly correlated with USP22 levels (Fig. xref , r  = 0.6626, P  < 0.0001)."
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"Our findings establish that the USP22-FASN axis plays an important role in regulating lipid accumulation and colorectal tumorigenesis, and targeting this axis may represent a promising therapeutic strategy for colorectal cancer."
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"Because p53 mutation usually loss the transcriptional activity and responses to upstream signals differently [ xref , xref ], p53-mediated repression of the USP22-FASN axis will be abolished in p53-mutated cancers, resulting in FASN stabilization, lipid accumulation, and tumor growth."
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"Thus, the USP22-FASN axis revealed in this study may be a critical mechanism for the maintenance of CSC properties and therapy resistance of human cancer, which deserves further investigation."
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"Due to a high-frequency of p53 mutation and dysfunction in human cancer, activation of the USP22-FASN axis may represent a prevailing mechanism that drives tumorigenesis, indicating a promising strategy for the treatment of colorectal cancer."
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"Our study demonstrates that ROS critically regulates lipid synthesis and tumorigenesis through the USP22-FASN axis in a p53-dependent manner, and targeting the USP22-FASN axis may represent a potential strategy for the treatment of colorectal cancer."
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"We have demonstrated that the USP22-FASN axis is highly activated in CRC and is critical for lipid accumulation and tumorigenesis."
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"USP22 interacts with FASN and inhibits FASN ubiqutination."
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"Reciprocal immunoprecipitation (IP) assays demonstrated that USP22 and FASN interact with each other in both RKO E6 and HT29 cells (Fig. xref ), which was further confirmed in 293T cells by co-transfection of HA-USP22 and Flag-FASN plasmids (Fig. S xref C)."
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"Together, these results support that USP22 interacts with FASN and inhibits FASN ubiquitination in CRC cells."
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"Because both USP22 and FASN are involved in the regulation of cell apoptosis [ xref , xref ], we next determined the role of the USP22-FASN axis in H 2 O 2 -induced cell apoptosis in p53 +/+ CRC cells."
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