IndraLab

Statements


USP7 deubiquitinates PTEN. 20 / 20
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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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"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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"HAUSP deubiquitinates PTEN to cause its nuclear exclusion, leading to tumour aggressiveness XREF_BIBR."

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

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

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

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

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

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