IndraLab

Statements

USP7 activates localization. 6 / 6
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"Unlike previous USPs, USP7 modulates the localization and conformational structure editing of the well-known tumor suppressors p53 and PTEN."
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"Amongst its substrates, MDM2 and PTEN have been shown to be deubiquitinated by HAUSP to cause the stabilization or change of cellular localization, respectively, leading to tumorigenesis [XREF_BIBR, XREF_BIBR]."
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"Furthermore, knockout of one USP7 allele in HCT116 cells (USP7 +/-) resulted in impaired CI-M6PR recycling (XREF_FIG), decreased Arp2/3 localization to VPS35 positive endosomes (XREF_FIG and XREF_SUPPLEMENTARY), and decreased F-actin accumulation on VPS35 positive endosomes (XREF_FIG and XREF_SUPPLEMENTARY)."
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"For example, the deubiquitylase MATH-33 recently has been reported to stabilize and activate DAF-16 by antagonizing polyubiquitylation, while its mammalian counterpart USP7 and HAUSP inhibits FOXO1 and FOXO4 by decreasing their nuclear localization and transcriptional activity, respectively, by removing monoubiquitin moieties [XREF_BIBR - XREF_BIBR]."
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"In addition, the subcellular localization of PTEN can be modulated by a mutation or masking of the NLS or nuclear export signals (NES) [55] in the PTEN protein or by deubiquitinylation of PTEN by HAUSP as seen in PML [56]."
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"XREF_BIBR Moreover, USP7 may contribute to cancer by modulating the nuclear localization of PTEN."
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