IndraLab
Statements
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"Thus, USP7 induces PML degradation by another pathway that does not implicate phosphorylation of PML by CK2 or polyubiquitination by RNF4."
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"USP7 silencing restored the number of PML NBs and the level of the PML protein (XREF_FIG), indicating that EBNA1 does not disrupt PML NBs in the absence of USP7."
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"CK2 and RNF4 regulators of PML catabolism are dispensable for USP7 mediated PML NB disruption and PML degradation."
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"On that note, we have recently shown that USP7 promotes the degradation of PML proteins (whose gene is activated by p53) by a mechanism that is independent of its catalytic activity XREF_BIBR."
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"In keeping with these observations, USP7 was subsequently shown to negatively regulate PML proteins (even in the absence of EBV or EBNA1), by a mechanism that is independent of its ubiquitin cleavage activity [XREF_BIBR]."
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"Overall our results point to a novel model of PML regulation in which USP7 triggers degradation of PML by a mechanism that does not require phosphorylation of PML by CK2 or polyubiquitylation by RNF4."
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"USP7 could then promote PML degradation either through its catalytic activity or through recruitment of additional cellular proteins."
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"47 These reports raise the possibility that HAUSP decreases PML protein accumulation indirectly by upregulating UHRF1 protein abundance."