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PTEN function: the long and the short of it
Open accessAbstract
Phosphatase and tensin homolog deleted on chromosome ten (PTEN) is a phosphatase that is frequently altered in cancer. PTEN has phosphatase-dependent and -independent roles, and genetic alterations in PTEN lead to deregulation of protein synthesis, the cell cycle, migration, growth, DNA repair, and survival signaling. PTEN localization, stability, conformation, and phosphatase activity are controlled by an array of protein-protein interactions and post-translational modifications. Thus, PTEN-interacting and -modifying proteins have profound effects on the tumor suppressive functions of PTEN. Moreover, recent studies identified mechanisms by which PTEN can exit cells, via either exosomal export or secretion, and act on neighboring cells. This review focuses on modes of PTEN protein regulation and ways in which perturbations in this regulation may lead to disease.
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“A tumour suppressor gene, like phosphatase and tensin homologue (PTEN), is commonly mutated in wide ranges of GBM, which may be a great candidate for therapeutic intervention27,54.”
From Blood–brain-barrier-crossing lipid nanoparticles for mRNA delivery to the central nervous system (2025) · cites this paper as [54]
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Ubiquitination regulates PTEN nuclear import and tumor suppression
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MC1R Is a Potent Regulator of PTEN after UV Exposure in Melanocytes
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“The PI3K/Akt signaling cascade plays a pivotal role in cell survival, proliferation, and differentiation in a wide range of cellular processes [8], and dysregulation of this pathway is involved in various malignancies [9].”
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“Structurally, the PTEN protein comprises five domains: PDZ‐binding domains, C‐tail‐, C2‐, phosphatase, and PBD‐domains (Hopkins et al., 2014), which consists two major functional regions (a C2 domain and a phosphatase domain) and three structural regions (a C‐terminal tail containing proline–glutamic acid–serine–threo…”
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“PTEN regulates the PI3K signaling pathway (40).”
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“PTEN is encoded by a single Pten gene that can be translated into a canonical or long form of PTEN (PTEN-Long) protein through differential usage of start codons (Hopkins et al., 2013; Hopkins et al., 2014).”
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“While PTEN is primarily known as a tumor suppressor [151], it has also been associated with IR.”
Stochasticity and positive feedback enable enzyme kinetics at the membrane to sense reaction size
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“PTEN has phosphatase-dependent and -independent effects, and PTEN affects cell cycle, migration, and growth [16, 17].”
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MicroRNA-21 induces cisplatin resistance in head and neck squamous cell carcinoma
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“PTEN, as a tumor suppressor gene, regulate multiple signal transduction pathways that function in cell growth, cell migration and apoptosis [12].”
BackgroundMolecular mechanisms of microRNA-301a during tumor progression and metastasis
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PTEN: An Emerging Potential Target for Therapeutic Intervention in Respiratory Diseases
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“Alterations of PTEN expression and activity were comprehensively reviewed elsewhere [23, 25].”
Tang, J., Xiao, X., Jiang, Y.-F., Tian, Y., Peng, Z.-T., Yang, M.-C., Xu, Z., & Gong, G. (2020) · Journal of Hepatocellular Carcinoma · doi:10.2147/jhc.s271091 · Cited by 19
“Cancer Genome Atlas lists 1120 PTEN mutations in 27 tumor types.(29) Loss of the PTEN gatekeeper function is a pivotal part of promoting carcinogenesis.”
BackgroundSignaling roles of phosphoinositides in the retina
Rajala, R. V. S. (2020) · Journal of Lipid Research · doi:10.1194/jlr.tr120000806 · Cited by 20
“These 5-phosphatases regulate several aspects of cellular function, including synaptic vesicle recycling, cell proliferation, embryonic development, control of hematopoietic development, and insulinmediated signaling (233).”
BackgroundLi, H., Yuan, S., Yang, M., Zha, H., Li, X.-R., Sun, H., Duan, L., Gu, Y., Li, A., Weng, Y., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.10433 · Cited by 17
“(2) miR-21 affects pathways partially overlapping those regulated by PTEN, particularly those involved in cell migration [38, 39].”
BackgroundMolecular Analysis of AFP and HSA Interactions with PTEN Protein
Zhu, M.-Y., Lin, B., Zhou, P., & Li, M.-S. (2015) · BioMed Research International · doi:10.1155/2015/256916 · Cited by 19
Malaney, P., Uversky, V. N., & Davé, V. (2015) · Methods · doi:10.1016/j.ymeth.2014.10.005 · Cited by 18
Huang, R., Huang, Y., Zeng, G., Li, M.-F., & Jin, Y. (2020) · Cell Cycle · doi:10.1080/15384101.2020.1732514 · Cited by 18
PTEN: History of a Tumor Suppressor.
Salmena, L. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3299-3_1 · Cited by 18
Xuan, L., Jinming, G., Guan, Y., Wang, H., Wu, H., & Chang, Y. (2021) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2021.11.014 · Cited by 21
Tiwari, A., Iida, M., Kosnopfel, C., Abbariki, M., Menegakis, A., Fehrenbacher, B., Maier, J., Schaller, M., Brucker, S. Y., Wheeler, D. L., et al. (2020) · Cancers · doi:10.3390/cancers12102795 · Cited by 22
“Genetic alterations in PTEN lead to deregulation of protein synthesis, cell cycle, migration, growth, DNA repair, and survival signaling [25].”
BackgroundPrecise Immunodetection of PTEN Protein in Human NeoplasiaPreprint
Pulido, R., Mingo, J., Gaafar, A., Nunes‐Xavier, C. E., Luna, S., Torices, L., Angulo, J. C., & Lopez, J. I. (2019) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a036293 · Cited by 14
“4B; Table 5; Hopkins et al. 2014; Fragoso and Barata 2015; Lee et al. 2018).”
BackgroundCorrection of PTEN mutations in glioblastoma cell lines via AAV-mediated gene editing
Hill, V. K., Kim, J.-S., James, C. D., & Waldman, T. (2017) · PLoS ONE · doi:10.1371/journal.pone.0176683 · Cited by 17
Colis, L. C., Hegan, D. C., Kaneko, M., Glazer, P. M., & Herzon, S. B. (2015) · Journal of the American Chemical Society · doi:10.1021/ja513117p · Cited by 19
Yang, T., Wu, X., Hu, J., Hu, M.-B., Xu, H., Jiang, H., & Ding, Q. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000491066 · Cited by 16
Yu, Z., Wu, H., & Wang, Y. (2022) · Human & Experimental Toxicology · doi:10.1177/09603271221111345 · Cited by 16
“protein synthesis, cell cycle, survival, growth, migration, and DNA repair signaling.(23) PTEN has the ability to antagonize PI3K/Akt signaling by inhibiting PIP3dependent processes, thereby inhibiting cell growth, survival, and proliferation progression.”
BackgroundLi, Z.-W., Li, B., Li, L., Wang, G.-Y., Li, Y.-Y., Fu, R.-Q., Yue, M., Ni, R., Wang, J.-M., Ye, G., et al. (2020) · OncoTargets and Therapy · doi:10.2147/ott.s281397 · Cited by 15
Approaches to Investigating the Protein Interactome of PTEN
Smith, S. L., Pitt, A. R., & Spickett, C. M. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00570 · Cited by 16
Eph signaling controls mitotic spindle orientation and cell proliferation in neuroepithelial cells
Franco, M., & Carmena, A. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201807157 · Cited by 15
Prognostic Significance of mTOR and PTEN in Patients with Esophageal Squamous Cell Carcinoma
Lu, J., Pan, Y., Xia, X., Gu, Y., & Lei, Y.-Y. (2015) · BioMed Research International · doi:10.1155/2015/417210 · Cited by 15
Yeast-based methods to assess PTEN phosphoinositide phosphatase activity in vivo.
Rodríguez-Escudero, I., Fernández-Acero, T., Bravo, I., Leslie, N., Pulido, R., Molina, M., & Cid, V. J. (2015) · Methods · doi:10.1016/j.ymeth.2014.10.020 · Cited by 15
Modular protein-DNA hybrid nanostructures as a drug delivery platform.
Ryu, Y., Hong, C. A., Song, Y., Beak, J., Seo, B. A., Lee, J.-J., & Kim, H.-S. (2020) · Nanoscale · doi:10.1039/c9nr08519j · Cited by 14
Anaplastic thyroid cancer – an overview of genetic variations and treatment modalities
Reddi, H. V., Kumar, A., & Kulstad, R. (2015) · Advances in Genomics and Genetics · doi:10.2147/agg.s53448 · Cited by 14
“58 ,48,50 (Table 1 and Figure 2A).”
Wang, P., Lai, D., Jin, L., & Xue, Y. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1570128 · Cited by 11
“PTEN plays a key role in various processes such as proliferation, apoptosis and in fl ammation, and can inhibit the PI3K/AKT signaling pathway (110).”
A WWP2–PTEN–KLF5 signaling axis regulates odontoblast differentiation and dentinogenesis in mice
Fu, J., Zhang, X., Zheng, H., Yang, G., Chen, Z., & Yuan, G. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102220 · Cited by 13
“PTEN has been found to mediate multiple cellular processes (18), but its expression pattern and function in tooth development remained unclear.”
BackgroundCCN1 stimulated the osteoblasts via PTEN/AKT/GSK3β/cyclinD1 signal pathway in Myeloma Bone Disease
Yan, S., Liu, H., Liu, Z., Peng, F., Jiang, F., Li, L., & Fu, R. (2019) · Cancer Medicine · doi:10.1002/cam4.2608 · Cited by 14
Wu, C.-W., Wang, S., Lin, M., & Chen, S. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.04.052 · Cited by 13
Deregulation of the Hippo pathway in mouse mammary stem cells promotes mammary tumorigenesis
Li, H., & Gumbiner, B. M. (2016) · Mammalian Genome · doi:10.1007/s00335-016-9662-7 · Cited by 15
“EGFR signaling and PI3K signaling have both been strongly implicated in mammary tumorigenesis, both in mice and humans (Guy et al. 1992; Hardy et al. 2010; Hopkins et al. 2014; Kim and Muller 1999; Koren and Bentires-Alj 2013; Troyer and Lee 2001; Wickenden and Watson 2010).”
PI3K/AKT/mTOR axis in vascular malformations: from molecular insights to targeted clinical trials
Zheng, Y.-Y., Hua, C., & Lin, X.-X. (2025) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-025-04115-2 · Cited by 13
“Additionally, PTEN loss often results from epigenetic or transcriptional silencing, which further complicates direct gene targeting [158, 161–164].”
Liu, J., Liang, Q., Wang, T., Ma, B., Wang, X., Li, P., Shaukat, A., Guo, X.-F., & Deng, G.-Z. (2022) · Scientific Reports · doi:10.1038/s41598-022-12681-9 · Cited by 12
Ferreira, R. G., Narvaez, L. E. M., Espíndola, K. M. M., Rosario, A. C. R. S., Lima, W. G. N., & Monteiro, M. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.594917 · Cited by 12
Guo, H., & Zhang, L.-L. (2021) · Biochemical Genetics · doi:10.1007/s10528-021-10075-6 · Cited by 12
“The balance of phosphatidylinositol 3-kinase (Pl3K)/protein kinase B (AKT) and mitogen-activated protein kinase (MAPK) signaling pathways is critical for the major regulation of the PTEN gene (Hopkins et al. 2014).”
BackgroundMa, Z.-K., Wang, Y., Wang, W., Sun, W.-Y., Wang, R., Ding, X., Chen, Z.-B., Li, X.-D., Li, Z.-Y., Ye, Y.-L., et al. (2026) · Cancer Cell · doi:10.1016/j.ccell.2026.01.012 · Cited by 11
Current and Emerging Therapies for Targeting the ERK1/2 & PI3K Pathways in Cancer
Abizadeh, E., Berglas, E., Abizadeh, A., Glatman, J., Lavi, A. B., Spivak, M., Sapir, T., & Shifteh, D. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178696 · Cited by 13
“Given PTEN’s critical role in regulating cell growth it comes as no surprise that mutations of this tumor suppressor protein are a common cause of cancer formation [127,129,130].”
Targeting WEE1 Kinase for Breast Cancer Therapeutics: An Update
Zhang, Z., Harish, R., Elahi, N., Saini, S., Telia, A., Kundlas, M., Koroleva, A., Umoh, I., Lota, M., Bilkhu, M., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26125701 · Cited by 11
“Alterations in PTEN are frequently observed in cancers [134].”
Song, Z., Xue, Z., Wang, Y., Imran, M., Assiri, M. A., & Fahad, S. (2024) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2024.130567 · Cited by 11
Ubiquitin E3 ligases in cancer: somatic mutation and amplification
Jo, E.-H., Kim, M., Lee, H.-J., & Park, H.-S. (2023) · BMB Reports · doi:10.5483/bmbrep.2023-0037 · Cited by 12
Yuan, D., Jia, C., Yan, M.-Y., & Wang, J. (2021) · Kaohsiung Journal of Medical Sciences · doi:10.1002/kjm2.12443 · Cited by 11
Azzi, A. (2020) · FEBS Open Bio · doi:10.1002/2211-5463.12967 · Cited by 11
Toward Systems Pathology for PTEN DiagnosticsPreprint
Haddadi, N., Travis, G., Nassif, N. T., Simpson, A. M., & Marsh, D. J. (2019) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a037127 · Cited by 10
Lian, Z., Hu, Z., Xian, H., Jiang, R., Huang, H., Jiang, Y., Zheng, Z., Lloyd, R. S., Yuan, J., Sha, Y., et al. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.125496 · Cited by 12
PTEN interacts with RNA polymerase II to dephosphorylate polymerase II C-terminal domain
Abbas, A., Romigh, T., & Eng, C. (2019) · OncoTarget · doi:10.18632/oncotarget.27128 · Cited by 11
RSRC1 suppresses gastric cancer cell proliferation and migration by regulating PTEN expression
Yu, S.-J., Gautam, N., Quan, M., & Gao, Y. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10409 · Cited by 11
Wu, J., & Song, Y. (2018) · Oncology Letters · doi:10.3892/ol.2018.7799 · Cited by 9
Impaired striatal function in Huntington's disease is due to aberrant p75NTR signaling
Plotkin, J. L., & Surmeier, D. J. (2014) · Rare Diseases · doi:10.4161/2167549x.2014.968482 · Cited by 11
“Though pathological p75NTR signaling in HD iSPNs seems to be a consequence of elevated PTEN expression, it is a poor therapeutic target because of its role as a tumor suppressor.(22) Interestingly, a recent epidemiological study showed that the incidence of cancer is lower in HD patients,(23) a phenomenon that is cons…”
Mechanisms of Immune Evasion in PTEN Loss Prostate Cancer
Esteban-Villarrubia, J., Ballesteros, P. Á., Martín-Serrano, M., Vico, M. R., Funes, J. M., de Velasco, G., Castro, E., Olmos, D., Castellano, D., & González‐Billalabeitia, E. (2024) · Immuno · doi:10.3390/immuno4040028 · Cited by 8
“Another approach involves overcoming the post-transcriptional repression of PTEN by targeting negative regulators, such as miRNAs that downregulate PTEN expression [47].”
Shank‑associated RH domain interactor signaling in tumorigenesis (Review)
Zeng, C., Xiong, D., Zhang, K., & Yao, J. (2020) · Oncology Letters · doi:10.3892/ol.2020.11850 · Cited by 11
Li, K., Liu, Y., Zhou, Y., Zhang, R., Zhao, N., Yan, Z., Zhang, Q., Zhang, S., Qiu, F., & Xu, Y. (2015) · Scientific Reports · doi:10.1038/srep11567 · Cited by 9
O'Malley, D. E., Raspin, K., Melton, P. E., Burdon, K. P., Dickinson, J. L., & FitzGerald, L. M. (2023) · British Journal of Cancer · doi:10.1038/s41416-023-02485-7 · Cited by 11
“Genetic alterations in PTEN lead to dysregulation of protein synthesis, the cell cycle, cell migration and growth, as well as DDR and survival signalling pathways [16].”
Dautle, M., Zhang, S., & Chen, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713339 · Cited by 11
“PTEN encodes an enzyme that acts as a tumor suppressor by inhibiting the P13K/AKT signaling pathway, which is known to promote PCa survival and growth [41,55].”
BackgroundSavitri, C. M. A., Rahmawati, L., Awalia, Romadhon, P. Z., Waskito, L. A., Hidayat, A. A., Rezkitha, Y. A. A., Miftahussurur, M., & Yamaoka, Y. (2025) · Journal of Research in Medical Sciences · doi:10.4103/jrms.jrms_705_22 · Cited by 8
Li, W., Leng, Y., Xiong, Y.-H., Li, W.-Y., Cai, Y., Xue, R., Chen, R., Lei, S., Xia, Z., & Xia, Z.-Y. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01638-2 · Cited by 8
“PTEN was originally identified as a tumor suppressor gene frequently lost from a region of chromosome 10q23 in a variety of human tumors [25], and two major mechanisms underlying the posttranslational regulation of PTEN are phosphorylation and oxidation [26].”
BackgroundMultiple roles of PTEN isoforms PTENα and PTENβ in cellular activities and tumor development
Liang, H., & Yin, Y.-X. (2019) · Science China Life Sciences · doi:10.1007/s11427-019-1595-2 · Cited by 8
Lengyel, K., Young, F., Kucukmetin, A., Cresti, N., Plummer, R., Ralte, A., & O'Donnell, R. (2019) · International Journal of Gynecological Pathology · doi:10.1097/pgp.0000000000000614 · Cited by 8
“PTEN modulates protein synthesis, cell cycle, migration, growth, DNA repair, and survival signalling by regulating phosphoinositide-3-kinase (PI3K) and the protein-Ser/Thr kinase (AKT) signalling pathway (24).”
BackgroundSecretion and fusion of biogeochemically active archaeal membrane vesicles
Johnson, T. B., Mach, C., Grove, R. A., Kelly, R. M., Cott, K. E. V., & Blum, P. (2018) · Geobiology · doi:10.1111/gbi.12306 · Cited by 7
Kool, M., Galac, S., van der Helm, N., Corradini, S., Kooistra, H., & Mol, J. A. (2015) · Journal of Veterinary Internal Medicine · doi:10.1111/jvim.12528 · Cited by 8
“Activation of the PI3K pathway also may occur downstream of the receptors, for instance as a result of mutations in the genes encoding PTEN or the PI3K catalytic subunit (PIK3CA) or because of decreased expression of PTEN.(12,13) In these cases, single or dual inhibitors of PIK3CA and mTOR could be employed.”
Current advances in non-viral nanoparticle-based gene therapy for effective management of cancer
Dhuri, A., Kanp, T., Rode, K., Bharath, M., Gupta, U., Guru, S. K., & Singh, P. K. (2024) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2024.106083 · Cited by 9
Karn, R., & Emerson, I. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1845802 · Cited by 7
“…since it is a tumour suppressor gene and once gets mutated, needs restoration or overexpression which is recently being tried to achieve by using micro RNAs (Xiao et al., 2019) and transfection with small interfering RNA (Qin & Qin, 2019) and PTEN mRNAs (Hopkins et al., 2014) in the affected cells.”
BackgroundSingle nucleotide polymorphism in PTEN-Long gene: A risk factor in chronic myeloid leukemia.
Ferri, C., Weich, N., Gutiérrez, L., Brasi, C. D. D., Bengió, M. R., Zapata, P., Fundia, A., & Larripa, I. (2019) · Gene · doi:10.1016/j.gene.2019.01.038 · Cited by 7
PTEN modulates gene transcription by redistributing genome-wide RNA polymerase II occupancy
Abbas, A., Padmanabhan, R., Romigh, T., & Eng, C. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz112 · Cited by 7
“PTEN interacts with a wide variety ofnuclearfactorsincludingp53,CENP-C,HIF1 α ,CREBandMCRS1 (21–23).”
Expression and Activity of Matrix Metalloproteinases in Leukemia
Asnafi, A. A., Bagheri, M., Zibara, K., Behzad, M. M., & Shahrabi, S. (2018) · Journal of Pediatric Hematology/Oncology · doi:10.1097/mph.0000000000001386 · Cited by 7
Díez, H., Benitez, M. J., Fernández, S., Torres‐Alemán, I., Garrido, J. J., & Wandosell, F. G. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.07.002 · Cited by 9
Hummadi, Y. M. A. A. M., Al-khfajy, W., & Jasem, M. A. (2025) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/j.jpet.2025.103654 · Cited by 6
Thrombomodulin regulates PTEN/AKT signaling axis in endothelial cells
Giri, H., Biswas, I., & Rezaie, A. R. (2023) · Arteriosclerosis, Thrombosis and Vascular Biology · doi:10.1161/atvbaha.123.320000 · Cited by 6
Role of microRNAs in embryo–endometrial interactions: biological functions and clinical applications
Qi, S., Kodithuwakku, S. P., Pang, R. T. K., Chiu, P. C. N., Tang, M. H. Y., & Lee, C. (2023) · Reproductive and Developmental Medicine · doi:10.1097/rd9.0000000000000073 · Cited by 6
“…were significantly lower in the culture media from cleavage embryos that resulted in successful pregnancy compared to those from embryos with failed pregnancy [76] . miR-26b-5p and miR-21-5p target MYC and PTEN, which control the cycle, proliferation, growth, and differentiation of cells [77,78] .”
BackgroundHyperphosphorylated PTEN exerts oncogenic properties
van Ree, J. V., Jeganathan, K. B., Velasco, R. O. F., Zhang, C., Can, I., Hamada, M., Li, H., Baker, D., & van Deursen, J. (2023) · Nature Communications · doi:10.1038/s41467-023-38740-x · Cited by 6
Burgers, L., Li, Y., Michalakis, S., Ciurus, S., Zahler, S., Müller, R., & Fürst, R. (2022) · Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · doi:10.1016/j.biopha.2022.113174 · Cited by 6
Zhang, C., Liu, Y.-W., Chi, Z., & Chen, B. (2020) · PPAR Research · doi:10.1155/2020/8864813 · Cited by 6
“As a negative regulator of the PI3K/AKT signaling pathway, the tumor suppressor gene PTEN can regulate cell growth, proliferation, and survival [16].”
BackgroundModesto, P., Fernandez, J. L. C., Martini, I., Zoccola, R., Pugliano, M. C., Ciucis, C. G. D., Goria, M., Ferrari, A., & Razzuoli, E. (2020) · Animals · doi:10.3390/ani10111981 · Cited by 7
“When the gene is impaired, cells can reproduce without control [38] and the inhibition of the PI3K/AKT pathway is discontinued, resulting in the activation of the preferred glycolysis in the neoplastic cells for the ATP production compared to mitochondrial respiration [39].”
BackgroundPalumbo, E., Zhao, B., Xue, B., Uversky, V. N., & Davé, V. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1630005 · Cited by 9
Yankina, M. A., Saik, O., Иванисенко, В. А., Сергеевич, Д. П., & Хуснутдинова, Э. К. (2018) · Russian Journal of Genetics · doi:10.1134/s1022795418110170 · Cited by 8
“PTEN mutations are also associated with macrocephaly and autismspectrum disorders [24].”
BackgroundRamalho, T. C., de Castro, A. A., Tavares, T. S., Silva, M. D. C., Silva, D. R., Cesar, P. H., Santos, L. D. A., da Cunha, E. F. F., Nepovimová, E., & Kuča, K. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.06.011 · Cited by 6
“Intracellular signalling pathways triggered by N-methyl-D-aspartate receptor (NMDAR) are not well explored, however, it is known that this receptor is involved in the regulation mechanism of SMN2 gene expression and have, as mediators, the calcium/calmodulin-dependent kinase II, phosphatidylinositol 3-kinase, and seri…”
InfluentialVariation in Akt protein kinases in human populations
Rotwein, P. S. (2017) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00295.2017 · Cited by 7
“This gene encodes the enzyme that dephosphorylates phosphatidylinositol-3,4,5-trisphosphate (PIP3) to PIP2 and thus normally antagonizes activation of Akt by PIP3, the product of PI3 kinase (12).”
BackgroundThe Optimization of Soluble PTEN Expression in Escherichia coli
Hu, Y.-M., An, Y., Fang, N., Li, Y.-Z., Jin, H., Nazarali, A., & Ji, S.-P. (2015) · Open Biochemistry Journal · doi:10.2174/1874091x01509010042 · Cited by 6
“Compared to classical PTEN, the alternative PTEN protein has additional 173 amino acids containing secretion signal peptide added at its N-terminal, which allows the protein to be secreted into the extracellular environment and to enter in recipient cells, thereby inhibiting the PI3K-Akt pathway in a paracrine fashion…”
Metadata
- Authors
- Hopkins, B. D., Hodakoski, C., Barrows, D., Mense, S. M., & Parsons, R. E.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Parsons, Ramon E.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2014-04
- Volume
- 39
- Issue
- 4
- Pages
- 183-190
- ISSN
- 0968-0004 (ISSN-L)
- PMC
- PMC4043120
- OpenAlex
- W2109559424
- Cited by
- 309
- References
- 125
- Citations by year
- 2026: 13 · 2025: 26 · 2024: 29 · 2023: 21 · 2022: 24 · 2021: 35 · 2020: 36 · 2019: 32 · 2018: 22 · 2017: 22 · 2016: 13 · 2015: 25 · 2014: 11
- FWCI
- 2.23
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (P01CA097403, R01CA082783, R01CA155117, R01CA184016)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- PTEN, phosphatase and tensin homolog, tumor suppressor, phosphatase activity, protein-protein interaction, post-translational modification, protein stability, cancer, cell cycle regulation, DNA repair, cell migration
- MeSH terms
- Animals, Cell Cycle, Gene Expression Regulation, Humans, Protein Processing, Post-Translational, Genomic Instability, PTEN Phosphohydrolase
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