IndraLab

Statements


MDM2 activates USP7. 7 / 7
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"In vitro and in cancer cell lines, p300 mediated acetylation of MDM2 on Lys 182 and Lys 185 enabled HAUSP to bind, presumably deubiquitinate, and stabilize MDM2."

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"HAUSP plays pivotal roles in the stability of p53 and MDM2, raising HAUSP as a potential therapeutic target for tuning p53 mediated anti-tumor activity."

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"Both USP2 and USP7 and HAUSP target MDM2 and lead to its degradation XREF_BIBR."

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"P22077 downregulated USP7 targets MDM2, claspin, and Chk1 [XREF_BIBR] and inhibited neuroblastoma growth [XREF_BIBR], and P50429 inhibited HCT116 proliferation [XREF_BIBR, XREF_BIBR]."

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"Since MDM2 is the preferred target of USP7 under unstressed conditions [XREF_BIBR, XREF_BIBR], then logically, suppression of USP7 should destabilize MDM2."

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"These findings suggest that p300 mediated MDM2 acetylation within the NLS domain enables HAUSP to be recruited to the acidic domain, leading to deubiquitination of MDM2 (XREF_FIG)."

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"It has been shown that Mdm2 is the primary target of USP7 mediated stabilization."