IndraLab

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USP7 increases the amount of TP53. 32 / 32
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"UNBS5162 actives USP7 and increases the p53 protein level."
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"However depletion of HAUSP in cells does not decrease p53 levels as predicted, but rather increases p53 levels, apparently due to HAUSP 's ability to bind and deubiquitinate Mdm2."
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"When USP7 was coexpressed with p53 in these cells, USP7 increased the expression levels of p53 as expected (Figure  4A)."
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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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"Inhibition of USP7 may inhibit the proliferation of gastric cancer cells by halting the cell cycle during the G2-M phase, maintaining p53 expression, and downregulating PD-L1 expression."
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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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"USP7 Depletion Decreases Neuroblastoma Cell Growth, Increases Protein Expression of p53, and Decreases Protein Expression of EZH2."
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"Among the four sgRNAs _USP7, sg3_ USP7 most significantly increased the expression of p53 both in p53-mutated and p53-wild type LSCC cell lines in the results of qRT-PCR and western blot (Fig. 4A, B)."
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"USP7 enhances Tip60 acetyltransferase activity towards p53 at K120 and promotes p53-mediated pro-apoptotic gene expression [102]."
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"Almac4 treatment and USP7 depletion led to decreased USP7, MDM2, N-myc, and EZH2 expression levels and to increased p53 expression, with reduced p53 ubiquitination and increased EZH2 ubiquitination (Figure 9)."
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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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"By regulating p53 levels through their deubiquitinating activities, USP7 and USP2a may contribute to cancer pathogenesis and therapeutic strategies that target these p53 specific DUBs may become important as cancer treatments [XREF_BIBR]."
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"By simulating TSPY1 function in Tspy1 deficient spermatogonia derived from mouse testes, we found that TSPY1 could promote spermatogonial proliferation by decreasing the Usp7 modulated p53 level."
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"To balance this action, HAUSP and USP7, an ubiquitin hydrolase, in turn regulates MDM2 activity and therefore P53, while the deubiquitinating enzyme USP7 works to augment P53 levels through inhibition of its degradation [XREF_BIBR]."
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"In addition, we figure out that usp7 knockdown attenuates Shh pathway, while does not alter P53 protein level and P53 target gene expression."
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"Subsequently, it was shown that while partial knockdown of USP7 decreased p53 levels, complete ablation of USP7 led to an increase in p53 levels."
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"Besides, protein expression of p53 and p21 was dramatically downregulated by either GMPS or USP7 knockdown in MCF-7 and DU4475 cells (Fig. 4f, g)."
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"Overexpression of catalytically inactive USP7 in cells promotes P53 binding to its target sequences and P21 expression, without increasing the levels of P53 protein."
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"While USP7 can directly regulate p53 levels, these levels can also be regulated by the DUB USP2a."
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"Both, the DUB HAUSP (herpesvirus associated ubiquitin specific protease) and USP10 (ubiquitin specific protease 10), targeting poly-ubiquitinated p53, have been shown to restore p53 levels even when Hdm2 is overexpressed."
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"Quite a few studies have shown that USP7 promotes tumor cell development, progression, and metastasis by deubiquitinating the p53 negative regulatory protein MDM2, which decreases intracellular levels of p53 (44-47)."
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"Taken together, USP7 overexpression rescued the decline expression of p53 through an Mdm2 independent manner."
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"Silencing of USP7 decreased the p53 level and increased ubiquitinated-p53."
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"Downregulation of USP7 can increase the level of P53 via promoting MDM2 degradation (96)."
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"However, knockout of USP7 in cells does not decrease p53 levels as predicted, but rather stabilizes p53 [XREF_BIBR]."
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"Overexpression of USP7 markedly promoted the expressions of USP7 and p53, whereas knockdown of USP7 decreased the expressions of USP7 and p53 ( Figure 3C)."
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"When the proteasome inhibitor, MG132, was applied in HUVECs, knockdown of USP7 failed to decrease the expression of p53, indicating the involvement of ubiquitination underlying the reduction of p53 ( Figure 3E)."
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"These results indicated that USP7 could promote the expression of p53 by inducing its deubiquitination."
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"Additionally, the expressions of p53 and p21 could be promoted by the overexpression of USP7, which was reversed by the downregulation of p53 ( Figure 4G,H)."
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"Moreover, USP7 could increase the expression of p53 through promoting its deubiquitination."
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"According to a recent study, inhibition or knockdown of ubiquitin-specific peptidase 7 diminished H/R damage (reducing LDH release and necrosis), improved ubiquitination of p53, decreased p53 and TFR1 levels, and attenuated ferroptosis [68]."
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"For instance, USP7 can promote cancer development by downregulating p53 levels through deubiquitination of mouse double minute 2 (MDM2); lysine 63 deubiquitinase (CYLD), which is frequently mutated in nasopharyngeal carcinoma, inhibits cell invasion and metastasis by interfering with the NF-κB signaling pathway; USP28 is an oncogenic factor that deubiquitinates F-box and WD repeat domain containing 7 (FBXW7), thereby enhancing the stability of RAF family members and inhibiting activation of the MEEK pathway."
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