IndraLab

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USP7 increases the amount of MDM2. 18 / 18
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"As shown in XREF_FIG, knockdown of USP7 reduced the levels of Mdm2 and p53, a result consistent with that of a previous study."
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"In fact, we found that HAUSP silencing in SAMe-D cells induced a decrease in Mdm2 levels (XREF_FIG), the major substrate stabilized by HAUSP, and an increase in nuclear localization of p53 after UVC treatment (XREF_FIG left panel)."
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"Indeed, we also found that coexpression of HAUSP can prevent the Hdm2-mediated degradation of p53, whereas at the same time, Hdm2 levels are increased by ectopic HAUSP expression ( Figure 1 A )."
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"USP7 silencing by siRNA reduces chromatin accessibility and repair by modulating Mdm2 levels."
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"16 The discovery that USP7 modulates the levels of not only p53 but also Hdm2 and HdmX has greatly increased the complexity of its role within the p53–Hdm2 pathway."
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"Hdmx is efficiently degraded by Hdm2 ( Figure 1 B), but coexpression of HAUSP counteracts the Hdm2-mediated degradation of Hdmx in a dose-dependent manner, whereas the levels of Hdm2 are simultaneousl[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP7 (ubiquitin specific protease 7), which deubiquitinates HDM2, can lead to increased levels of HDM2 and decreased levels of p53."
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"While we have established that the two closely related proteins, Hdm2 and HdmX, have a conserved USP7 interaction site, the functional significance of this conserved interaction site is still unknown [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Moreover, while the levels of Mdm2 were enhanced by USP7 co-transfection, Mdm2 mediated Poleta degradation was indeed strongly rescued by USP7 overexpression (XREF_FIG)."
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"This deubiquitinating enzyme protects MDM2 from degradation by the ubiquitin–proteasome system [21], and it has been reported that pharmacological inhibition of USP7 reduces MDM2 expression, which activates p53 and leads to senescent cell apoptosis [24,25,26]."
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"Our immunoblotting results showed that while Usp7 knockdown decreased MDM2 level, it did not lead to increased p53 level (fig."
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"USP7 can increase the level of MDM2, the negative regulatory protein of the tumor suppressor gene p53, and then decrease the level of p53 [13]."
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"Thus, HAUSP-mediated de-ubiquitination can bring about increased levels of MDM2 that then accelerate p53 degradation to directly reduce the level of p53."
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"To determine whether USP7 mediates PDGF regulation of MDM2, FoxO4 and CyclinD1 expression in PASMCs, cells were first transfected with USP7 sequence-specific siRNA for 24 h and then treated with 10 ng/ml PDGF for 24 h; the protein level of MDM2, FoxO4 and CyclinD1 was measured using Western blotting."
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"These results suggest that USP7 mediates PDGF regulation of the protein expression of MDM2, FoxO4 and CyclinD1 in PASMCs."
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"Inhibition of USP7 decreases Mdm2 levels resulting in a corresponding increase in p53, inducing apoptosis."
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"In addition, USP7 depletion led to decreased expression of both MDM2 and EZH2 and an increase in p53 protein expression (Figure 6C,D), similar to that seen with pharmacologic inhibition of USP7 and further supporting a role for USP7 in NB tumor growth via to its effect on USP7 deubiquitinase activity, allowing for target protein degradation."
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"As shown by the Gu group, partial reduction of USP7 levels in several human cell lines promotes decreased levels of both MDM2 and p53, yet total abolition of USP7 stabilizes p53 levels by decreasing MDM2 [117, 118]."
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