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

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

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

Open access

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

Open this paper in CoChat — free account

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1038/nature07290

Cites

34 of 34 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

ONCOMINE: A Cancer Microarray Database and Integrated Data-Mining Platform
Rhodes, D. R., Yu, J., Sundaram, S. K., Deshpande, N., Varambally, R., Ghosh, D., Barrette, T. R., Pander, A., & Chinnaiyan, A. M. (2004) · Neoplasia · doi:10.1016/s1476-5586(04)80047-2 · Cited by 3,719
The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
Maehama, T., & Dixon, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13375 · Cited by 3,104
Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
Stambolic, V., Suzuki, A., de la Pompa, J. L., Brothers, G. M., Mirtsos, C., Sasaki, T., Ruland, J., Penninger, J. M., Siderovski, D. P., & Mak, T. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81780-8 · Cited by 2,551
Tenets of PTEN Tumor Suppression
Salmena, L., Carracedo, A., & Pandolfi, P. P. (2008) · Cell · doi:10.1016/j.cell.2008.04.013 · Cited by 1,050
Self-citation
Essential role for nuclear PTEN in maintaining chromosomal integrity
Shen, W. H., Balajee, A. S., Wang, J., Wu, H., Eng, C., Pandolfi, P. P., & Yin, Y. (2007) · Cell · doi:10.1016/j.cell.2006.11.042 · Cited by 979
Self-citation
Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
Bernardi, R., & Pandolfi, P. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2277 · Cited by 876
Self-citation
RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
Tatham, M. H., Geoffroy, M., Shen, L., Plechanovová, A., Hattersley, N., Jaffray, E., Palvimo, J. J., & Hay, R. T. (2008) · Nature Cell Biology · doi:10.1038/ncb1716 · Cited by 837
Mono- Versus Polyubiquitination: Differential Control of p53 Fate by Mdm2
Li, M., Brooks, C. L., Wu-Baer, F., Chen, D., Baer, R., & Gu, W. (2003) · Science · doi:10.1126/science.1091362 · Cited by 804
PTEN: One Gene, Many Syndromes
Eng, C. (2003) · Human Mutation · doi:10.1002/humu.10257 · Cited by 787
Ubiquitination regulates PTEN nuclear import and tumor suppression
Trotman, L. C., Wang, X., Alimonti, A., Chen, Z., Teruya-Feldstein, J., Yang, H., Pavletich, N. P., Carver, B. S., Cordon-Cardo, C., Erdjument-Bromage, H., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.040 · Cited by 748
Self-citation

Flagged first, then by citations

Show all 34 references

Sorted by citations

Items 201–300 of 546

A novel signaling network as a critical rheostat for the biology and maintenance of the normal stem cell and the cancer-initiating cell
Ito, K., Bernardi, R., & Pandolfi, P. P. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2009.01.004 · Cited by 53
Self-citation
USP7 as an emerging therapeutic target: A key regulator of protein homeostasis
Guo, N.-J., Wang, B., Zhang, Y., Kang, H., Nie, H., Feng, M.-K., Zhang, X.-Y., Zhao, L., Wang, N., Liu, H., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.130309 · Cited by 52
Nucleophosmin/B26 regulates PTEN through interaction with HAUSP in acute myeloid leukemia
Noguera, N. I., Song, M. S., Divona, M., Catalano, G., Calvo, K. L., García, F., Ottone, T., Florenzano, F., Faraoni, I., Battistini, L., et al. (2012) · Leukemia · doi:10.1038/leu.2012.314 · Cited by 50
Self-citation
The nuclear bodies inside out: PML conquers the cytoplasm
Carracedo, A., Ito, K., & Pandolfi, P. P. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.03.011 · Cited by 50
Self-citation
BAP1 suppresses prostate cancer progression by deubiquitinating and stabilizing PTEN
Deng, R., Guo, Y., Li, L., He, J., Qiang, Z., Zhang, H., Chen, R., Wang, Y., Zhao, X., & Yu, J. (2020) · Molecular Oncology · doi:10.1002/1878-0261.12844 · Cited by 50
The roles of ubiquitin modifying enzymes in neoplastic disease
Kumari, N., Jaynes, P. W., Saei, A., Iyengar, P. V., Richard, J. L. C., & Eichhorn, P. J. A. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.09.002 · Cited by 51
The role of deubiquitinating enzymes in cancer drug resistance
Tanguturi, P., Kim, K.-S., & Ramakrishna, S. (2020) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-020-04046-8 · Cited by 49
PTEN in kidney cancer: A review and meta-analysis
Que, W., Qiu, H., Cheng, Y., Liu, M., & Wu, C. (2018) · Clinica Chimica Acta · doi:10.1016/j.cca.2018.01.031 · Cited by 49
Recent advances in the development of ubiquitin-specific-processing protease 7 (USP7) inhibitors
Li, P., & Liu, H.-M. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112107 · Cited by 50
Ubiquitin-specific Protease 7 Is a Regulator of Ubiquitin-conjugating Enzyme UbE2E1
Sarkari, F., Wheaton, K., Delfa, A. L., Mohamed, M., Shaikh, F., Khatun, R., Arrowsmith, C. H., Frappier, L., Saridakis, V., & Sheng, Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.469262 · Cited by 48
CCDC6: the identity of a protein known to be partner in fusion
Cerrato, A., Merolla, F., Morra, F., & Celetti, A. (2017) · International Journal of Cancer · doi:10.1002/ijc.31106 · Cited by 47
Interplay between nuclear transport and ubiquitin/SUMO modifications in the regulation of cancer-related proteins
Rodríguez, J. A. (2014) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2014.03.005 · Cited by 48
The deubiquitinating enzyme USP17 is associated with nonsmall cell lung cancer (NSCLC) recurrence and metastasis
McFarlane, C., McFarlane, S., Paul, I., Arthur, K., Scheaff, M., Kerr, K. M., Stevenson, M., Fennell, D. A., & Johnston, J. A. (2013) · Oncotarget · doi:10.18632/oncotarget.1282 · Cited by 46
SCP Phosphatases Suppress Renal Cell Carcinoma by Stabilizing PML and Inhibiting mTOR/HIF Signaling
Lin, Y., Lu, L.-T., Chen, H., Duan, X., Lin, X., Feng, X., Tang, M., & Chen, R. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-1330 · Cited by 46
Small molecule activators of the p53 response
Ladds, M. J. G. W., & Laín, S. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz006 · Cited by 46
CRISPR/Cas9-Induced DNA Damage Enriches for Mutations in a p53-Linked Interactome: Implications for CRISPR-Based Therapies
Jiang, L., Ingelshed, K., Shen, Y., Boddul, S. V., Iyer, V. S., Kasza, Z., Sedimbi, S. K., Lane, D. P., & Wermeling, F. (2021) · Cancer Research · doi:10.1158/0008-5472.can-21-1692 · Cited by 47
PTEN Phosphorylation and Nuclear Export Mediate Free Fatty Acid-Induced Oxidative Stress
Wu, Y., Zhou, H., Wu, K., Lee, S., Li, R., & Liu, X. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5498 · Cited by 46
The PTEN protein: cellular localization and post-translational regulation
Leslie, N. R., Kriplani, N., Hermida, M. A., Garcia, V. A., & Wise, H. M. (2016) · Biochemical Society Transactions · doi:10.1042/bst20150224 · Cited by 45
Chemical Approaches to Intervening in Ubiquitin Specific Protease 7 (USP7) Function for Oncology and Immune Oncology Therapies
Wu, J., Kumar, S., Wang, F., Wang, H., Chen, L., Arsenault, P., Mattern, M. R., & Weinstock, J. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00498 · Cited by 47
Inhibition of guanosine monophosphate synthetase ( GMPS ) blocks glutamine metabolism and prostate cancer growth
Wang, Q., Guan, Y. F., Hancock, S. E., Wahi, K., van Geldermalsen, M., Zhang, B. K., Pang, A., Nagarajah, R., Mak, B., Freidman, N., et al. (2021) · The Journal of Pathology · doi:10.1002/path.5665 · Cited by 45
The intricate interplay between HIFs, ROS, and the ubiquitin system in the tumor hypoxic microenvironment
Wang, Y., Liu, X., Huang, W., Liang, J., & Chen, Y. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108303 · Cited by 44
SENP1 regulates PTEN stability to dictate prostate cancer development
Bawa‐Khalfe, T., Yang, F., Ritho, J., Lin, H., Cheng, J., & Yeh, E. T. H. (2016) · Oncotarget · doi:10.18632/oncotarget.13283 · Cited by 43
TRIP13 modulates protein deubiquitination and accelerates tumor development and progression of B-cell malignancies.
Li, C., Xia, J.-L., Machin, R. F., Chen, F.-P., He, Y.-J., Ashby, T., Teng, F., Xu, H.-W., Liu, D.-X., Gai, D.-Z., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci146893 · Cited by 39
The equilibrium of tumor suppression: DUBs as active regulators of PTEN
Christine, A., Park, M. K., Song, S. J., & Song, M. S. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00887-w · Cited by 41
Self-citation
Ubiquitin-specific protease 7 (USP7): an emerging drug target for cancer treatment
Carreira, L. D., Oliveira, R. I., Moreira, V. M., & Salvador, J. A. R. (2023) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2023.2266571 · Cited by 42
Clinical Significance of Ubiquitin Specific Protease 7 (USP7) in Predicting Prognosis of Hepatocellular Carcinoma and its Functional Mechanisms
Wang, X., Zhang, Q., Wang, Y. K., Zhuang, H., & Chen, B. (2018) · Medical Science Monitor · doi:10.12659/msm.909368 · Cited by 41
USP49 participates in the DNA damage response by forming a positive feedback loop with p53
Tu, R., Kang, W., Yang, X.-F., Zhang, Q., Xie, X., Liu, W., Zhang, J., Zhang, X.-D., Wang, H., & Du, R. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0475-3 · Cited by 41
Inhibition of ubiquitin-specific protease 7 sensitizes acute myeloid leukemia to chemotherapy
Cartel, M., Mouchel, P., Gotanègre, M., David, L., Bertoli, S., Mas, V. M., Besson, A., Sarry, J., Manenti, S., & Didier, C. (2020) · Leukemia · doi:10.1038/s41375-020-0878-x · Cited by 43
USP7 targets XIAP for cancer progression: Establishment of a p53-independent therapeutic avenue for glioma
Saha, G., Sarkar, S., Mohanta, P. S., Kumar, K., Chakrabarti, S., Basu, M., & Ghosh, M. K. (2022) · Oncogene · doi:10.1038/s41388-022-02486-5 · Cited by 41
The role of deubiquitinases in breast cancer
Xiao, Z., Zhang, P., & Ma, L. (2016) · Cancer and Metastasis Reviews · doi:10.1007/s10555-016-9640-2 · Cited by 41
A global survey of CRM1-dependent nuclear export sequences in the human deubiquitinase family
García‐Santisteban, I., Bañuelos, S., & Rodríguez, J. A. (2011) · Biochemical Journal · doi:10.1042/bj20111300 · Cited by 40
TRIM32-dependent transcription in adult neural progenitor cells regulates neuronal differentiation
Hillje, A., Pavlou, M. A. S., Beckmann, E., Worlitzer, M. M. A., Bahnassawy, L., Lewejohann, L., Palm, T., & Schwamborn, J. C. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.487 · Cited by 40
PTEN Modulates miR-21 Processing via RNA-Regulatory Protein RNH1
Kim, Y.-J., Park, S., Choi, E. Y., Kim, S., Kwak, H. J., Yoo, B. C., Yoo, H., Lee, S., Kim, D., Park, J. B., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028308 · Cited by 41
Structural Characterization of Interaction between Human Ubiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex Virus-1
Pozhidaeva, A., Mohni, K. N., Dhe‐Paganon, S., Arrowsmith, C. H., Weller, S. K., Korzhnev, D. M., & Bezsonova, I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664805 · Cited by 42
miR-382-5p modulates the ATRA-induced differentiation of acute promyelocytic leukemia by targeting tumor suppressor PTEN
Liu, D., Zhong, L., Yuan, Z., Yao, J., Zhong, P., Liu, J., Yao, S., Zhao, Y., Liu, L., Chen, M., et al. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.11.012 · Cited by 40
Novel function of PiT1/SLC20A1 in LPS-related inflammation and wound healing
Koumakis, E., Botti, J., Benna, J. E., Leroy, C., Boitez, V., Codogno, P., Friedlander, G., & Forand, A. (2019) · Scientific Reports · doi:10.1038/s41598-018-37551-1 · Cited by 41
Multifaceted Regulation of PTEN Subcellular Distributions and Biological Functions
Liu, T., Wang, Y., Wang, Y., & Chan, A. M.-L. (2019) · Cancers · doi:10.3390/cancers11091247 · Cited by 41
Ubiquitination/de-ubiquitination: A promising therapeutic target for PTEN reactivation in cancer
Wang, K., Liu, J., Li, Y., Li, J., & Zhang, R. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188723 · Cited by 40
Posttranslational Regulation and Conformational Plasticity of PTENPreprint
Kotelevets, L., Trifault, B., Chastre, E., & Scott, M. G. H. (2020) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a036095 · Cited by 40
USP7 Regulates Cytokinesis through FBXO38 and KIF20B
Georges, A. A., Coyaud, É., Marcon, E., Greenblatt, J. F., Raught, B., & Frappier, L. (2019) · Scientific Reports · doi:10.1038/s41598-019-39368-y · Cited by 42
Deubiquitylase USP7 regulates human terminal erythroid differentiation by stabilizing GATA1
Liang, L., Peng, Y., Zhang, J., Zhang, Y., Roy, M., Han, X., Xiao, X., Sun, S., Liu, H., Nie, L., et al. (2019) · Haematologica · doi:10.3324/haematol.2018.206227 · Cited by 37
A 2.2 Å resolution structure of the USP7 catalytic domain in a new space group elaborates upon structural rearrangements resulting from ubiquitin binding
Molland, K. L., Zhou, Q., & Mesecar, A. D. (2014) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x14002519 · Cited by 38
The Role of PTEN in Myeloid Malignancies
Morotti, A., Panuzzo, C., Crivellaro, S., Carrà, G., Torti, D., Guerrasio, A., & Saglio, G. N. (2015) · Hematology Reports · doi:10.4081/hr.2015.6027 · Cited by 38
Targeting ubiquitin specific protease 7 in cancer: A deubiquitinase with great prospects
Khusbu, F. Y., Chen, F., & Chen, H. (2018) · Cell Biochemistry and Function · doi:10.1002/cbf.3336 · Cited by 36
Targeting the Ubiquitin System in Glioblastoma
Scholz, N., Kurian, K. M., Siebzehnrübl, F. A., & Licchesi, J. D. F. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.574011 · Cited by 37
The Ubiquitin System: a Regulatory Hub for Intellectual Disability and Autism Spectrum Disorder
Kasherman, M. A., Premarathne, S., Burne, T. H. J., Wood, S. A., & Piper, M. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01881-x · Cited by 41
Suppression of USP7 induces BCR-ABL degradation and chronic myelogenous leukemia cell apoptosis
Jiang, S., Wang, X., He, Y., Huang, H., Cao, B., Zhang, Z., Liu, J., Wang, Q., Huang, Z., & Mao, X. (2021) · Cell Death & Disease · doi:10.1038/s41419-021-03732-6 · Cited by 35
Current and future directions of USP7 interactome in cancer study
Park, H., & Baek, K. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188992 · Cited by 35
Role of the promyelocytic leukaemia protein in cell death regulation
Salomoni, P., Dvorkina, M., & Michod, D. (2012) · Cell Death and Disease · doi:10.1038/cddis.2011.122 · Cited by 35
Overexpression and Biological Function of Ubiquitin-Specific Protease 42 in Gastric Cancer
Hou, K., Zhu, Z., Wang, Y., Zhang, C., Yu, S., Zhu, Q., & Yan, B. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152997 · Cited by 35
Deubiquitinases in hematological malignancies
Lei, H., Wang, J., Hu, J., Zhu, Q., & Wu, Y. (2021) · Biomarker Research · doi:10.1186/s40364-021-00320-w · Cited by 40
Emerging role of ubiquitination/deubiquitination modification of PD-1/PD-L1 in cancer immunotherapy
Ding, P., Ma, Z., Fan, Y., Feng, Y., Shao, C., Pan, M., Zhang, Y., Huang, D., Han, J. Y., Hu, Y., et al. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2022.01.002 · Cited by 37
USP7 protects genomic stability by regulating Bub3.
Giovinazzi, S., Sirleto, P., Aksenova, V., Morozov, V. M., Zori, R., Reinhold, W. C., & Ishov, A. M. (2014) · Oncotarget · doi:10.18632/oncotarget.1989 · Cited by 34
USP35 activated by miR let-7a inhibits cell proliferation and NF-κB activation through stabilization of ABIN-2
Liu, C., Wang, L., Chen, W., Zhao, S., Yin, C., Lin, Y., Jiang, A., & Zhang, P. (2015) · Oncotarget · doi:10.18632/oncotarget.4451 · Cited by 34
Expression of PPARγ and PTEN in human colorectal cancer: An immunohistochemical study using tissue microarray methodology
Lin, M. S., Huang, J. X., Chen, W., Zhang, B. F., Fang, J., Zhou, Q., Hu, Y., & Heng Jun, G. A. O. (2011) · Oncology Letters · doi:10.3892/ol.2011.414 · Cited by 34
Herpesvirus-associated Ubiquitin-specific Protease (HAUSP) Modulates Peroxisome Proliferator-activated Receptor γ (PPARγ) Stability through Its Deubiquitinating Activity
Lee, K. W., Cho, J. G., Kim, C. M., Kang, A. Y., Kim, M., Ahn, B. Y., Chung, S. S., Lim, K., Baek, K., Sung, J.-H., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.496331 · Cited by 36
USP7 manipulation by viral proteins
Bojagora, A., & Saridakis, V. (2020) · Virus Research · doi:10.1016/j.virusres.2020.198076 · Cited by 37
The deubiquitinase USP7 promotes HNSCC progression via deubiquitinating and stabilizing TAZ
Li, J., Dai, Y., Ge, H., Guo, S., Zhang, W., Wang, Y., Liu, L., Cheng, J., & Jiang, H. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05113-z · Cited by 34
PARP-inhibitor-induced synthetic lethality for acute myeloid leukemia treatment
Zhao, L., & So, C. W. E. (2016) · Experimental Hematology · doi:10.1016/j.exphem.2016.07.007 · Cited by 32
Targeting Deubiquitinating Enzymes in Glioblastoma Multiforme: Expectations and Challenges
Jin, W., Mao, X., & Qiu, G. (2016) · Medicinal Research Reviews · doi:10.1002/med.21421 · Cited by 32
The HECT family of E3 ubiquitin ligases and PTEN
Song, M. S., & Pandolfi, P. P. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.06.012 · Cited by 32
Self-citation
Regulation of the nucleocytoplasmic trafficking of viral and cellular proteins by ubiquitin and small ubiquitin‐related modifiers
Wang, Y. E., Pernet, O., & Lee, B. (2011) · Biology of the Cell · doi:10.1111/boc.201100105 · Cited by 32
Selective protein N-terminal labeling with N-hydroxysuccinimide esters
Jiang, H., D’Agostino, G. D., Cole, P. A., & Dempsey, D. R. (2020) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2020.04.018 · Cited by 31
Usp7 promotes medulloblastoma cell survival and metastasis by activating Shh pathway
Zhan, M., Sun, X., Liu, J., Li, Y., Li, Y., He, X., Zhou, Z., & Lu, L. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.01.144 · Cited by 31
Human Herpesvirus 8 Interferon Regulatory Factors 1 and 3 Mediate Replication and Latency Activities via Interactions with USP7 Deubiquitinase
Xiang, Q., Ju, H., Li, Q., Mei, S.-C., Chen, D., Choi, Y. B., & Nicholas, J. (2018) · Journal of Virology · doi:10.1128/jvi.02003-17 · Cited by 32
Nuclear PTEN deficiency causes microcephaly with decreased neuronal soma size and increased seizure susceptibility
Igarashi, A., Itoh, K., Yamada, T., Adachi, Y., Kato, T., Murata, D., Sesaki, H., & Iijima, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002356 · Cited by 31
Targeting PTEN in Colorectal Cancers
Kotelevets, L., Scott, M. G. H., & Chastre, E. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-02771-1_5 · Cited by 31
The role of ubiquitination and deubiquitination in PI3K/AKT/mTOR pathway: A potential target for cancer therapy
Jin, J., He, J., Li, X., Li, X., & Jin, X. (2023) · Gene · doi:10.1016/j.gene.2023.147807 · Cited by 31
HAUSP regulates c-MYC expression via de-ubiquitination of TRRAP
Bhattacharya, S., & Ghosh, M. K. (2015) · Cellular Oncology · doi:10.1007/s13402-015-0228-6 · Cited by 32
PML-mediated signaling and its role in cancer stem cells
Zhou, W., & Bao, S. (2013) · Oncogene · doi:10.1038/onc.2013.111 · Cited by 31
Tumor suppressor protein Pdcd4 interacts with Daxx and modulates the stability of Daxx and the Hipk2-dependent phosphorylation of p53 at serine 46
Kumar, N., Wethkamp, N., Waters, L. C., Carr, M. D., & Klempnauer, K.-H. (2013) · Oncogenesis · doi:10.1038/oncsis.2012.37 · Cited by 30
Plasma protein profiling in a stage defined pancreatic cancer cohort – Implications for early diagnosis
Gerdtsson, A. S., Wingren, C., Persson, H., Delfani, P., Nordström, M., Ren, H., Wen, X., Ringdahl, U., Borrebaeck, C. A. K., & Hao, J. (2016) · Molecular Oncology · doi:10.1016/j.molonc.2016.07.001 · Cited by 30
Design, synthesis, biological evaluation and structure-activity relationship study of quinazolin-4(3H)-one derivatives as novel USP7 inhibitors
Li, P., Liu, Y., Yang, H., & Liu, H.-M. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113291 · Cited by 30
Ubiquitin-specific peptidase 48 regulates Mdm2 protein levels independent of its deubiquitinase activity
Cetkovská, K., Šustová, H., & Uldrijan, S. (2017) · Scientific Reports · doi:10.1038/srep43180 · Cited by 30
WDR79 promotes the proliferation of non-small cell lung cancer cells via USP7-mediated regulation of the Mdm2-p53 pathway
Sun, Y., Cao, L., Sheng, X., Chen, J., Zhou, Y., Yang, C., Deng, T., Ma, H., Feng, P., Liu, J., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.162 · Cited by 31
Polyphosphoinositides in the nucleus: Roadmap of their effectors and mechanisms of interaction
Jacobsen, R. G., Gavgani, F. M., Edson, A. J., Goris, M., Altankhuyag, A., & Lewis, A. E. (2019) · Advances in Biological Regulation · doi:10.1016/j.jbior.2019.04.001 · Cited by 30
Nuclear phosphoinositides and their roles in cell biology and disease
Martelli, A. M., Ognibene, A., Buontempo, F., Fini, M., Bressanin, D., Goto, K., McCubrey, J. A., Cocco, L., & Evangelisti, C. (2011) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2011.609530 · Cited by 29
Increase in the nuclear localization of PTEN by the Toxoplasma GRA16 protein and subsequent induction of p53‐dependent apoptosis and anticancer effect
Kim, S., Seo, S., Shin, J., Yang, J., Lee, S. H., & Shin, E. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14207 · Cited by 29
Emerging role of ubiquitin-specific protease 14 in oncogenesis and development of tumor: Therapeutic implication
Liu, B., Chen, J., & Zhang, S. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.116875 · Cited by 29
Proteome Analysis of USP7 Substrates Revealed Its Role in Melanoma Through PI3K/Akt/FOXO and AMPK Pathways
Gao, L., Zhu, D., Wang, Q., Bao, Z., Yin, S., Qiang, H., Wieland, H., Zhang, J., Teichmann, A. T., & Jia, J. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.650165 · Cited by 29
Targeting the Ubiquitin Proteasome System: Beyond Proteasome Inhibition
Xolalpa, W., Pérez‐Galán, P., Rodríguez, M. S., & Roué, G. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319220014 · Cited by 30
Infected cell protein 0 functional domains and their coordination in herpes simplex virus replication
Gu, H. (2016) · World Journal of Virology · doi:10.5501/wjv.v5.i1.1 · Cited by 29
Recent advances in PTEN signalling axes in cancer
Chow, J. T.-S., & Salmena, L. (2020) · Faculty Reviews · doi:10.12703/r/9-31 · Cited by 29
Self-citation
Discovery of Ubiquitin-Specific Protease 7 (USP7) Inhibitors with Novel Scaffold Structures by Virtual Screening, Molecular Dynamics Simulation, and Biological Evaluation
Liu, S., Zhou, X., Li, M., Zhao, W., Zhou, S., Cheng, K., Xu, Q., Chen, C., Wen, X., Sun, H., et al. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00154 · Cited by 28
Combination of Inhibitors of USP7 and PLK1 has a Strong Synergism against Paclitaxel Resistance
Shin, S., Kim, C.-H., Jang, H.-R., & Yim, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228629 · Cited by 28
Enzymatic Characterisation of USP7 Deubiquitinating activity and Inhibition
Wrigley, J. D. J., Eckersley, K., Hardern, I. M., Millard, L., Walters, M., Peters, S. W., Mott, R., Nowak, T., Ward, R. A., Simpson, P. B., et al. (2011) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-011-9186-4 · Cited by 28
Noncatalytic PTEN missense mutation predisposes to organ-selective cancer development in vivoPreprint
Caserta, E., Egriboz, O., Wang, H., Martin, C. K., Koivisto, C. S., Pécot, T., Kladney, R. D., Shen, C., Shim, K.-S., Pham, T., et al. (2015) · Genes & Development · doi:10.1101/gad.262568.115 · Cited by 28
Pro-apoptotic and anti-apoptotic regulation mediated by deubiquitinating enzymes
Choi, H., & Baek, K. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04132-5 · Cited by 27
Characterizing (un)binding mechanism of USP7 inhibitors to unravel the cause of enhanced binding potencies at allosteric checkpoint
Srivastava, M., Mittal, L., Kumari, A., Agrahari, A. K., Singh, M., Mathur, R., & Asthana, S. (2022) · Protein Science · doi:10.1002/pro.4398 · Cited by 27
Deubiquitylating enzymes as cancer stem cell therapeutics
Haq, S., Suresh, B., & Ramakrishna, S. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.10.004 · Cited by 27
Role of Ubiquitination in PTEN Cellular Homeostasis and Its Implications in GB Drug Resistance
Qin, X., Ali, S., Liu, L., Li, Y., Liu, X., Zhang, L., & Dong, L. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01569 · Cited by 27
Opening the conformation is a master switch for the dual localization and phosphatase activity of PTEN
Nguyen, H.-N., Yang, J.-M., Miyamoto, T., Itoh, K., Rho, E., Zhang, Q., Inoue, T., Devreotes, P. N., Sesaki, H., & Iijima, M. (2015) · Scientific Reports · doi:10.1038/srep12600 · Cited by 29
Nuclear PTEN’s Functions in Suppressing Tumorigenesis: Implications for Rare Cancers
Langdon, C. G. (2023) · Biomolecules · doi:10.3390/biom13020259 · Cited by 27
The stability of epigenetic factor ASXL1 is regulated through ubiquitination and USP7-mediated deubiquitination
Inoue, D., Nishimura, K., Kozuka‐Hata, H., Oyama, M., & Kitamura, T. (2015) · Leukemia · doi:10.1038/leu.2015.90 · Cited by 26
Protein Interactions of Phosphatase and Tensin Homologue (PTEN) and Its Cancer-associated G20E Mutant Compared by Using Stable Isotope Labeling by Amino Acids in Cell Culture-based Parallel Affinity Purification
Gunaratne, J., Goh, M. X., Swa, H. L. F., Lee, F. Y., Sanford, E., Wong, L. M., Hogue, K. A., Blackstock, W. P., & Okumura, K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.221184 · Cited by 26
USP7 inhibition induces apoptosis in glioblastoma by enhancing ubiquitination of ARF4
Pan, T., Li, X., Li, Y., Tao, Z., Yao, H., Wu, Y., Chen, G., Zhang, K., Zhou, Y., & Huang, Y. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02208-z · Cited by 26
Targeting deubiquitinating enzymes in cancer stem cells
Lei, H., Shan, H., & Wu, Y. (2017) · Cancer Cell International · doi:10.1186/s12935-017-0472-0 · Cited by 26
PML/RARa inhibits PTEN expression in hematopoietic cells by competing with PU.1 transcriptional activity
Noguera, N. I., Piredda, M. L., Taulli, R., Catalano, G., Angelini, G., Gaur, G., Nervi, C., Voso, M. T., Lunardi, A., Pandolfi, P. P., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.11964 · Cited by 27
Self-citation
DUBs Activating the Hedgehog Signaling Pathway: A Promising Therapeutic Target in Cancer
Bufalieri, F., Severini, L. L., Caimano, M., Infante, P., & Marcotullio, L. D. (2020) · Cancers · doi:10.3390/cancers12061518 · Cited by 25
The Loss of Nuclear PTEN Increases Tumorigenesis in a Preclinical Mouse Model for Hepatocellular Carcinoma
Kato, T., Yamada, T., Nakamura, H., Igarashi, A., Anders, R. A., Sesaki, H., & Iijima, M. (2020) · iScience · doi:10.1016/j.isci.2020.101548 · Cited by 24

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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks