Cited by 548Ubiquitin and proteasome pathwaysCancer-related Molecular PathwaysPI3K/AKT/mTOR signaling in cancer

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The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network

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Song, Min Sup, Salmena, Leonardo, Carracedo, Arkaitz, Egia, Ainara, Lo-Coco, Francesco, Teruya-Feldstein, Julie, Pandolfi, Pier Paolo·2008·Nature

DOI 10.1038/nature07290PMC PMC3398484

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Abstract

Nuclear exclusion of the PTEN (phosphatase and tensin homologue deleted in chromosome 10) tumour suppressor has been associated with cancer progression. However, the mechanisms leading to this aberrant PTEN localization in human cancers are currently unknown. We have previously reported that ubiquitinylation of PTEN at specific lysine residues regulates its nuclear-cytoplasmic partitioning. Here we show that functional promyelocytic leukaemia protein (PML) nuclear bodies co-ordinate PTEN localization by opposing the action of a previously unknown PTEN-deubiquitinylating enzyme, herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7), and that the integrity of this molecular framework is required for PTEN to be able to enter the nucleus. We find that PTEN is aberrantly localized in acute promyelocytic leukaemia, in which PML function is disrupted by the PML-RARalpha fusion oncoprotein. Remarkably, treatment with drugs that trigger PML-RARalpha degradation, such as all-trans retinoic acid or arsenic trioxide, restore nuclear PTEN. We demonstrate that PML opposes the activity of HAUSP towards PTEN through a mechanism involving the adaptor protein DAXX (death domain-associated protein). In support of this paradigm, we show that HAUSP is overexpressed in human prostate cancer and is associated with PTEN nuclear exclusion. Thus, our results delineate a previously unknown PML-DAXX-HAUSP molecular network controlling PTEN deubiquitinylation and trafficking, which is perturbed by oncogenic cues in human cancer, in turn defining a new deubiquitinylation-dependent model for PTEN subcellular compartmentalization.

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Authors: Song, M. S., Salmena, L., Carracedo, A., Egia, A., Lo-Coco, F., Teruya-Feldstein, J., & Pandolfi, P. P.
Affiliations: Beth Israel Deaconess Medical Center (US)
Corresponding author: Pandolfi, Pier Paolo
ORCID: Salmena, Leonardo
Carracedo, Arkaitz
Pandolfi, Pier Paolo
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2008-08-20
Volume: 455
Issue: 7214
Pages: 813-817
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature07290
PMC: PMC3398484
OpenAlex: W2162648910
Cited by: 548
References: 34
Citations by year: 2026: 15 · 2025: 27 · 2024: 22 · 2023: 35 · 2022: 25 · 2021: 37 · 2020: 43 · 2019: 40 · 2018: 33 · 2017: 39 · 2016: 34 · 2015: 36 · 2014: 32 · 2013: 27 · 2012: 31
FWCI: 9.86
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Cineca Institutional Research Information System (Tor Vergata University) (submittedVersion)
Institutional Research Information System University of Turin (University of Turin) (submittedVersion)
Funders: European Molecular Biology Organization
National Institutes of Health
National Cancer Institute (R01CA082328, P50CA092629)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Keywords: PTEN, USP7, PML, nuclear localization, PML nuclear bodies, DAXX, PML-RARA fusion, acute promyelocytic leukemia, all-trans retinoic acid, arsenic trioxide, prostate cancer, tumor suppressor regulation, ubiquitination, nuclear-cytoplasmic trafficking
MeSH terms: Promyelocytic Leukemia Protein, Ubiquitin-Specific Peptidase 7, Animals, Cell Nucleus, Fibroblasts, Humans, Male, Nuclear Proteins, Prostatic Neoplasms, Transcription Factors, Tretinoin, Ubiquitins, Leukemia, Promyelocytic, Acute, Apoptosis, Molecular Chaperones, Active Transport, Cell Nucleus, Tumor Suppressor Proteins, Ubiquitin Thiolesterase, Cell Line, Tumor, Adaptor Proteins, Signal Transducing, PTEN Phosphohydrolase, Mice, Ubiquitination, Co-Repressor Proteins

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The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network

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