IndraLab

Statements


USP7 deubiquitinates MDM4. 10 / 10
1 1 | 1 7

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"USP7 preferentially deubiquitylates the E3 ligase HDM2 and its binding partner HDMX, resulting in the destabilisation of p53 and the repression of p53 transactivation activity (Refs 43, 44, 45)."

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"More recent data suggest that Hausp also deubiquitinates Mdm4, another inhibitor of p53 activity."

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"Additionally, Mdm2, MdmX and p53 can be deubiquitinated by the HAUSP (herpesvirus associated ubiquitin specific protease) protein."

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"Importantly, HAUSP can deubiquitinate MDM2, MDMX, and p53."

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"MdmX phosphorylation (A38) inhibits (A40) the deubiquitination (A39) of MdmX by Hausp, which in turn increases ubiquitinated MdmX showing coherent regulation by DNA damage induced kinases."

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"HAUSP can also deubiquitinate and stabilize MdmX and has a role in DNA damaged induced degradation of MdmX [XREF_BIBR]."

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"Subsequently, HAUSP was shown to deubiquitinate Mdm2 and Mdmx, thereby stabilizing these proteins."

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"Additionally, Wip1 inhibits p53 through MdmX and enhances the interaction of MdmX with ubiquitin specific peptidase 7 (USP7), which deubiquitinates and stabilizes MdmX."

"Subsequently, hausp was shown to deubiquitinate mdm2 and mdmx, thereby stabilizing these proteins."