IndraLab

Statements

USP7 activates PTEN. 11 / 12
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"Additionally, knock-down of HAUSP by RNA interference (RNAi) increased PTEN monoubiquitinylation (XREF_FIG and XREF_SUPPLEMENTARY)."
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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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"For example, deprivation of PTEN as a tumor suppressor resulting from nuclear exclusion of PTEN mediated by USP7 is associated with acute promyelocytic leukaemia and prostate cancer [47] ."
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"[15] USP7 also mediates regulation of the Akt antagonist PTEN and affects its localization."
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"27 Changes in subcellular localization of PTEN mediated by HAUSP are crucial in certain leukemias."
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"To further investigate this possibility we tested the ability of PML to oppose HAUSP mediated PTEN deubiquitinylation."
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"XREF_BIBR, XREF_BIBR Daxx localization to PODs increases PTEN nuclear localization and PTEN tumor suppressor activity by inhibiting HAUSP mediated PTEN deubiquitinylation."
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"Unlike PML, PML-RARalpha overexpression was not able to prevent HAUSP mediated deubiquitinylation of PTEN (XREF_FIG)."
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"First, HAUSP (a DUB previously known to modify several important genes including p53 and FOXO4) overexpression leads to a predominantly nuclear excluded PTEN."
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"Furthermore, USP7 overexpression reduces phosphatase and tensin homolog (PTEN) monoubiquitination and leads to PTEN nuclear exclusion, which is associated with a more aggressive phenotype (Song et al., 2008)."
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"XREF_BIBR Moreover, USP7 may contribute to cancer by modulating the nuclear localization of PTEN."
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