IndraLab

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USP7 deubiquitinates E3_Ub_ligase. 10 / 10
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"USP7 deubiquitinates several tumour suppressors (p53, PTEN, FOXO and claspin) and E3 ligases (MDM2, Mule and viral proteins ICP0) and therefore regulates important signalling pathways that are involved in tumorigenesis XREF_BIBR XREF_BIBR."
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"In this case, Usp7 antagonizes the ubiquitination of the E3 Hdm2."
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"USP7 preferentially deubiquitylates and stabilizes E3 ligase MDM2 (human ortholog HDM2), which negatively regulates the celebrated tumor suppressor p53 [6,7] ."
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"XREF_BIBR - XREF_BIBR USP7 deubiquitinates and stabilizes not only p53, but also Mdm2, the primary E3 ubiquitin ligase of p53 XREF_BIBR, XREF_BIBR Given that both p53 and Mdm2 are known regulators of the steady-level of Poleta, we speculated that changes in cellular USP7 levels may also modulate Poleta level."
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"USP7 preferentially causes the deubiquitination of MDM2 (an oncogenic E3 ligase), which subsequently causes ubiquitination of p53 (a tumor suppressor protein) and decreases its cellular level."
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"53 Genetic and biochemical validation in cancer cells 54 , 55 have indicated that USP7 deubiquitinates and stabilizes the E3 ligase, MDM2."
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"Interestingly, USP7 can deubiquitinate both p53 and its negative regulator HDM2, an E3 ubiquitin ligase responsible for polyubiquitination and subsequent degradation of p53."
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", Study has shown that USP7 deubiquitinates and stabilizes E3 ubiquitin ligase mouse double minute 2 (MDM2), leading to ubiquitinated degradation of p53 and thereby promoting cell growth in ovarian cancer cells."
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"USP7 deubiquitinates MDM2, an E3 ligase of p53, and in turn destabilizes p53 (Colland et al., 2009)."
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"However, it remains uncertain whether up-regulation of MDM2 by USP7 facilitates FoxO4-ubiquitinated degradation and subsequently promotes PDGF-induced PASMCs proliferation.Previous studies have reported that USP7 deubiquitinates and stabilizes E3 ubiquitin ligase MDM2, thereby promoting cell growth in ovarian cancer cells."
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