IndraLab

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USP7 deubiquitinates PTEN. 28 / 30
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"Deubiquitination of PTEN by USP7 inactivates PTEN by nuclear exclusion, leading to impairment of tumor growth (Song et al., 2008)."

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"PML bodies were shown to contain DAXX protein that opposes deubiquitination of PTEN by HAUSP, and the treatment with drugs that trigger PML-RARα degradation, such as all-trans retinoic acid or arsenic[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"However, PTEN is deubiquitinated by USP7/HAUSP and released to the cytoplasm on the PML-RARα signaling network [24]."
| PMC

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"Furthermore, Usp7 can deubiquitinate PTEN to exclude it from the nucleus 28, facilitating PI3K-mTOR signaling in leukemia cells 112."

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"On the other hand, reversal of PTEN monoubiquitination by USP7 (also known as HAUSP) alters PTEN subcellular localization without affecting its protein level [XREF_BIBR]."

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"We have demonstrated that PTEN monoubiquitination at lysines 13 and 289 is essential for its nuclear localization and tumor suppressive function and, conversely, deubiquitination of PTEN by HAUSP renders PTEN predominantly cytoplasmic."

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"USP7 in turn deubiquitinates PTEN and promotes its exclusion from the nucleus (24)."

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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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"Previous reports have demonstrated that USP7 induces PTEN deubiquitination, causing exclusion of PTEN from the nucleus and subsequently increasing in the PI3K and AKT signaling pathway."

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"USP7 also deubiquitylates other cancer targets (PTEN, FOXO4 or claspin), and plays a role in DNA replication, apoptosis, and endosomal organization."

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"XREF_BIBR, XREF_BIBR, XREF_BIBR The DUB USP7 can reverse PTEN monoubiquitylation, affecting its cellular localization; 28 however, to date no DUBs have been described that reverse PTEN polyubiquitylation or otherwise influence PTEN expression levels."

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"More recently, the ability of USP7 to deubiquitinate PTEN was found to be under the control of BCR-ABL."

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"In addition to stability control, USP7 (also called HAUSP, herpesvirus-associated ubiquitin-specific protease) deubiquitinates PTEN to promote PTEN nuclear export, and this process can be antagonized by binding and sequesting USP7 from PTEN by PTEN phosphorylation at Ser380 by S6K ."

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"HAUSP deubiquitinates PTEN to cause its nuclear exclusion, leading to tumour aggressiveness XREF_BIBR."

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"245 HAUSP (herpesvirus associated ubiquitin specific protease) deubiquitinates PTEN in the nucleus."

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"For example, deubiquitination of monoubiquitinated transcription factors PTEN and FOX (O) 4 by USP7 serves to negatively regulate transcription activity of these proteins."

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"HAUSP deubiquitinates monoubiquitinated nuclear PTEN, facilitating nuclear exclusion of PTEN and promoting cancer progression in prostate cancer."

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"Once in the nucleus, PTEN is de-ubiquitinated by USP7 and subsequently remains nuclear localized."

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"A PTEN deubiquitinating enzyme, HAUSP (herpesvirus associated ubiquitin specific protease) may serve in the deubiquitination of PTEN and its shuttling out of the nucleus."

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"In contrast, the promyelocytic leukemia gene can inhibit the de-ubiquitination of phosphatase and tensin homolog by USP7."

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"Patients with acute promyelocytic leukaemia (PML) harbour a PML-RARα translocation in which USP7 deubiquitinates PTEN primarily in the cytoplasm, promoting nuclear rejection (59).4.3 USP10."

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"Furthermore, several DUBs, including HAUSP/USP7, USP10, USP11, USP13, OTUD3, and Ataxin-3 have been shown to reverse the ubiquitination of PTEN, a key antagonist in the PI3K growth-promoting pathway, implicating its function in cancer-specific contexts [15]."

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"These four Ub-PTEN peptide conjugates and Ub-t-PTEN protein were subjected to USP7 deubiquitinase, which was previously reported to deubiquitinate PTEN."

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"The tumor suppressor PTEN is also deubiquitinated by USP7, resulting in its nuclear export and inactivation."

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"PTEN is a tumor suppressor associated with tumor aggressiveness, wherein deubiquitination of PTEN by USP7 plays a pivotal role in PTEN localization and function."

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"[98] USP7, which is overexpressed in prostate cancer, deubiquitinates PTEN leading to reduced nuclear localization."

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"Recent results showed that HAUSP deubiquitinates PTEN to cause its nuclear exclusion and leads to tumour progression, supporting the oncogenic role of HAUSP XREF_BIBR."

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"In this study, we show that BCR-ABL enhances HAUSP-induced de-ubiquitination of PTEN in turn favoring its nuclear exclusion."