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"The overexpression of the exogenous Mdm2 gene further downregulated the level of cellular p53 protein, causing a low level of cellular p21 protein, while the cellular level of the CCDC106 protein was maintained at a low level independent of the expression of exogenous and endogenous Mdm2 (Fig. 4c)."
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"Of note, the knockdown of MDM2 increased the expression of p21/CDKN1A in parallel with p53 and inhibited the growth of IOMM-Lee and A172 cells (Figure 2A,B), suggesting that both of these cell lines expressed functional MDM2 and p53 and also that the endogenous expression of MDM2 contributed to the inactivation of p53 in these cell lines."
"MDM2 facilitates p21 degradation independent of ubiquitination and the E3 ligase function of MDM2. Instead, MDM2 promotes p21 degradation by facilitating binding of p21 with the proteasomal C8 subunit. The physical interaction between p21 and MDM2 was demonstrated both in vitro and in vivo with the binding region in amino acids 180-298 of the MDM2 protein."