IndraLab

Statements

USP14 binds MDM2. 6 / 6
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"In the current study, we studied the cell proliferation status after IU1 treatment and the USP14-MDM2 protein interaction in cervical cancer cells."
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"Moreover, co-immunoprecipitation assays showed that USP14 formed a complex with MDM2 (Figure xref B), which was consistent with the hypothesis that USP14 could bind to MDM2 and stabilize it."
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"Whereas MDM2 could interact with USP14, which removed the conjugated polyubiquitin chains from MDM2 and increased the stabilization of MDM2 protein."
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"In conclusion, this work has provided a novel insight into the interaction between proteasome-associated DUB USP14 and MDM2 in cervical cancer cells."
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"Whereas MDM2 could interact with USP14, which removed the conjugated polyubiquitin chains from MDM2 and increased the stabilization of MDM2 protein."
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"Moreover, co-immunoprecipitation assays showed that USP14 formed a complex with MDM2, which was consistent with the hypothesis that USP14 could bind to MDM2 and stabilize it."
33061808