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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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The functions and regulation of the PTEN tumour suppressor
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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
SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
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MC1R Is a Potent Regulator of PTEN after UV Exposure in Melanocytes
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“Although PTEN is frequently lost through genomic alterations, post-transcriptional acetylation, ubiquitination and phosphorylation of PTEN have also been shown to impair PTEN stabilization, localization and/or phosphatase activity, while a number of regulatory proteins have also been shown to interact with PTEN at var…”
BackgroundProtein monoubiquitylation: targets and diverse functions
Nakagawa, T., & Nakayama, K. (2015) · Genes to Cells · doi:10.1111/gtc.12250 · Cited by 76
“PTEN thus antagonizes AKT-dependent cellular activities such as survival, growth and proliferation (Hopkins et al. 2014).”
BackgroundPTEN Inhibition in Human Disease Therapy
Pulido, R. (2018) · Molecules · doi:10.3390/molecules23020285 · Cited by 77
“Regulation of PTEN expression levels, protein conformation, and subcellular localization, is achieved by a variety of genetic, epigenetic, postranscriptional, and postranslational mechanisms affecting PTEN gene, mRNA, and protein [1,2,22].”
BackgroundMeng, Q.-L., Du, X.-Z., Wang, H., Gu, H.-M., Zhan, J.-P., & Zhou, Z.-P. (2017) · Apoptosis · doi:10.1007/s10495-017-1387-x · Cited by 69
“Gene of phosphate and tension homology deleted on chromosome ten (PTEN) is considered an effective negative regulatory factor for PI3K/Akt signaling [24, 42].”
BackgroundPoint mutations of the mTOR-RHEB pathway in renal cell carcinoma
Ghosh, A. P., Marshall, C. B., Coric, T., Shim, E., Kirkman, R. L., Ballestas, M. E., Ikura, M., Bjornsti, M., & Sudarshan, S. (2015) · Oncotarget · doi:10.18632/oncotarget.4963 · Cited by 78
“, the gene encoding the PI3K catalytic subunit p110α) [51] or deletion/inactivation of tumor suppressors, including PTEN (phosphatase and tensin homolog) [52] , LKB1 (liver kinase B1) [53], and the protein phosphatase PP2A, which dephosphorylates and inactivates AKT [54].”
BackgroundINPP4B is an oncogenic regulator in human colon cancer
Guo, S. T., Chi, M., Yang, R.-H., Guo, X., Zan, L., Wang, C.-Y., Xi, Y.-F., Jin, L., Croft, A., Tseng, H.-Y., et al. (2015) · Oncogene · doi:10.1038/onc.2015.361 · Cited by 68
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Hensel, N., Rademacher, S., & Claus, P. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00198 · Cited by 71
“Therefore, it is possible that beneficial effects of ROCK-inhibition in EAE are not only based on inhibition of neuroinflammation but are also mediated neuron-intrinsically.”
BackgroundPTEN arginine methylation by PRMT6 suppresses PI3K–AKT signaling and modulates pre-mRNA splicing
Feng, J., Dang, Y., Zhang, W., Zhao, X., Zhang, C., Hou, Z., Jin, Y., McNutt, M. A., Marks, A. R., & Yin, Y. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1811028116 · Cited by 82
Elkholi, R., Renault, T. T., Serasinghe, M. N., & Chipuk, J. E. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-16 · Cited by 77
Chen, Y., Wang, T.-T., Du, J., Li, Y.-C., Wang, X., Zhou, Y., Yu, X., Fan, W., Zhu, Q., Tong, X.-M., et al. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000490142 · Cited by 61
Gu, P., Sun, M., Li, L., Yang, Y., Jiang, Z., Ge, Y., Wang, W., Mu, W., & Wang, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.657158 · Cited by 64
MicroRNA-26b Modulates the NF-κB Pathway in Alveolar Macrophages by Regulating PTEN
Zhang, L., Huang, C., Guo, Y., Gou, X., Hinsdale, M. E., Lloyd, P. G., & Liu, L. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402933 · Cited by 56
“stream signaling (11), leading to increased cell proliferation and”
BackgroundDoghish, A., Hegazy, M., Ismail, A., El-Mahdy, H. A., Elsakka, E. G. E., Elkhawaga, S. Y., Elkady, M. A., Yehia, A. M., Abdelmaksoud, N. M., & Mokhtar, M. (2023) · Pathology, Research and Practice · doi:10.1016/j.prp.2023.154442 · Cited by 56
Zhou, Z., Tu, Z., Zhang, J., Tan, C., Shen, X., Wan, B.-B., Li, Y., Wang, A., Zhao, L.-Q., Hu, J.-J., et al. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02714-1 · Cited by 56
“The genetic changes in PTEN lead to disorders of protein synthesis, DNA repair, and survival signals [16].”
BackgroundComprehensive characterization of PTEN mutational profile in a series of 34,129 colorectal cancers
Serebriiskii, I. G., Pavlov, V., Tricarico, R., Andrianov, G., Nicolas, E., Parker, M. I., Newberg, J., Frampton, G., Meyer, J. E., & Golemis, E. A. (2022) · Nature Communications · doi:10.1038/s41467-022-29227-2 · Cited by 55
RGS12 Represses Oral Cancer via the Phosphorylation and SUMOylation of PTEN
Fu, C.-Y., Yuan, G.-S., Yang, S.-Y., Zhang, D., & Yang, S. (2020) · Journal of dentistry research · doi:10.1177/0022034520972095 · Cited by 54
“3A) and found that PTEN possesses a C-terminal 4 amino acid binding motif (ITKV) that can be recognized by a specific set of PDZ domains of some regulatory proteins (Hopkins et al. 2014).”
BackgroundPTEN: A yin-yang master regulator protein in health and disease
Pulido, R. (2015) · Methods · doi:10.1016/j.ymeth.2015.02.009 · Cited by 59
Redox Regulation of PTEN by Peroxiredoxins
Huu, T. N., Park, J., Zhang, Y., Park, I., Yoon, H. J., Woo, H. A., & Lee, S.-R. (2021) · Antioxidants · doi:10.3390/antiox10020302 · Cited by 59
“The C2 domain (amino acids 186-351) can bind phospholipid membrane independent of calcium because it lacks the canonical Ca2+ chelating residues in vitro, which makes PTEN inhibit cell migration [31].”
BackgroundThe emerging roles of the polycistronic miR-106b∼25 cluster in cancer – A comprehensive review
Mehlich, D., Garbicz, F., & Wlodarski, P. K. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.08.097 · Cited by 66
Bhattacharya, S., Mahato, R. K., Singh, S., Bhatti, G. K., Mastana, S. S., & Bhatti, J. S. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.122110 · Cited by 60
Wang, Y., Liu, Y., Du, X., Ma, H., & Yao, J. (2020) · OncoTargets and Therapy · doi:10.2147/ott.s241632 · Cited by 58
RetractedConjunctival Melanoma: Genetic and Epigenetic Insights of a Distinct Type of Melanoma
Rossi, E., Schinzari, G., Maiorano, B., Pagliara, M., Stefani, A. D., Bria, E., Peris, K., Blasi, M., & Tortora, G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215447 · Cited by 47
“The nuclear PTEN plays an oncosuppressive role [90,91]; it is abrogated in neoplastic cells by nuclear-cytoplasmic shuttling.”
BackgroundZhu, L.-L., Mou, Q.-J., Wang, Y., Zhu, Z., & Cheng, M. (2020) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2020.4748 · Cited by 44
The Role of MicroRNA in the Pathogenesis of Diabetic Nephropathy
Szostak, J., Gorący, A., Durys, D., Dec, P., Modrzejewski, A., & Pawlik, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076214 · Cited by 46
“In addition to dephosphorylation of phosphatidylinositol (3,4,5)-triphosphate (PIP3), it is a vital negative regulator of the proto-oncogenic phosphatidylinositol 3-kinase (PI3K)–protein kinase B (Akt) and mammalian target of rapamycin (mTOR) pathways [65].”
BackgroundFeng, Y.-B., Hua, X., Niu, R., Du, Y., Shi, C.-J., Zhou, R.-P., & Chen, F.-H. (2019) · Biological Research · doi:10.1186/s40659-019-0232-9 · Cited by 43
Flavonoid-Based Cancer Therapy: An Updated Review.
Hosseinzadeh, E., Hassanzadeh, A., Marofi, F., Alivand, M., & Solali, S. (2020) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520620666200423071759 · Cited by 42
Perspectives on the role of PTEN in diabetic nephropathy: an update
Khokhar, M., Roy, D., Modi, A., Agarwal, R. G., Yadav, D., Purohit, P., & Sharma, P. (2020) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2020.1746735 · Cited by 43
Fu, L., Zhu, P., Qi, S., Li, C., & Zhao, K. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.08.040 · Cited by 48
PTEN: A potential prognostic marker in virus-induced hepatocellular carcinoma
Khalid, A., Hussain, T., Manzoor, S., Saalim, M., & Khaliq, S. (2017) · Tumor Biology · doi:10.1177/1010428317705754 · Cited by 39
Zhang, Y.-Q., Liang, Y.-K., Wu, Y., Chen, M., Chen, W.-L., Li, R., Zeng, Y.-Z., Huang, W.-H., Wu, J.-D., Zeng, D., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03735-3 · Cited by 41
Fang, F., Li, Z., Yu, J., Long, Y., Zhao, Q., Ding, X., Wu, L. H., Shao, S., Zhang, L., & Xiang, W. (2021) · Journal of Advanced Research · doi:10.1016/j.jare.2021.01.003 · Cited by 57
“Both MYC and PETN genes are involved in numerous biological functions, like the regulation of cell cycle, proliferation, growth and differentiation [49,50].”
BackgroundDual-specificity phosphatases in mental and neurological disorders
An, N., Bassil, K. C., Jowf, G. I. A., Steinbusch, H. W. M., Rothermel, M., de Nijs, L., & Rutten, B. P. F. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2020.101906 · Cited by 47
“The active catalytic site is HCxxGxxR (adapted from review (Hopkins et al., 2014; Worby and Dixon, 2014)).”
BackgroundNOS1 S-nitrosylates PTEN and inhibits autophagy in nasopharyngeal carcinoma cells
Zhu, L.-Q., Li, L.-L., Zhang, Q.-B., Yang, X., Zou, Z.-W., Hao, B.-T., Marincola, F., Liu, Z.-J., Zhong, Z., Wang, M., et al. (2017) · Cell Death Discovery · doi:10.1038/cddiscovery.2017.11 · Cited by 40
Chen, Y., Yu, H., Zhu, D., Liu, P., Yin, J., Liu, D., Zheng, M., Gao, J., Zhang, C., & Gao, Y. (2020) · The FASEB Journal · doi:10.1096/fj.201902463rr · Cited by 42
Regulation of the tumor suppressor PTEN by natural anticancer compounds
Kim, D., Suh, J., Surh, Y., & Na, H. (2017) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13422 · Cited by 48
Genetic Mutations of Pancreatic Cancer and Genetically Engineered Mouse Models
Saiki, Y., Jiang, C., Ohmuraya, M., & Furukawa, T. (2021) · Cancers · doi:10.3390/cancers14010071 · Cited by 38
“Furthermore, they develop benign tumors in various organs and cancers of the thyroid, prostate, or breast [55].”
BackgroundHuan, J., Grivas, P. D., Birch, J., & Hansel, D. E. (2022) · Cancers · doi:10.3390/cancers14061555 · Cited by 45
“Phosphatase and tensin homolog (PTEN), a tumor suppressor critical in mTOR pathway signaling [36], can function to dephosphorylate PIP3 at this stage, essentially turning “off” the cell signaling cascade prior to activation of mTOR.”
BackgroundLai, X., Wei, J., Gu, X.-Z., Yao, X.-M., Zhang, D.-S., Li, F., & Sun, Y.-Y. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16478 · Cited by 37
Ding, Z., Ogata, D., Roszik, J., Qin, Y. W., Kim, S., Tetzlaff, M. T., Lazar, A. J., Davies, M. A., Ekmekçioglu, S., & Grimm, E. A. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.631766 · Cited by 40
Targeting Protein Kinases to Enhance the Response to anti-PD-1/PD-L1 Immunotherapy
García‐Aranda, M., & Redondo, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092296 · Cited by 44
“PT EN PTEN This dual-specificity protein and lipid phosphatase blocks PI3K signaling by inhibiting PI3P-dependent processes such as AKT membrane recruitment and activation [108], which results in the inhibition of cell proliferation and survival [43].”
BackgroundSALL Proteins; Common and Antagonistic Roles in Cancer
Álvarez, C., Quiroz, A., Benítez-Riquelme, D., Riffo, E., Castro, A. F., & Pincheira, R. (2021) · Cancers · doi:10.3390/cancers13246292 · Cited by 37
“One of the central mechanisms is the inhibition of PTEN, a phosphatase that blocks the PI3K signaling pathway, inhibiting cell migration, proliferation, and survival [52].”
BackgroundFeng, Y., An, Q., Zhao, Z., Wu, M., Yang, C., Liang, W., Xu, X., Jiang, T., & Zhang, G. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116266 · Cited by 42
Wang, C., Wang, S., Ma, F., & Zhang, W.-D. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9478 · Cited by 36
“PTEN serves its tumor suppressor role by negatively regulating the phosphatidylinositol 3‑kinase (PI3K)‑RAC‑ α serine/threonine‑protein kinase (AKT) signaling pathway (15).”
Structure, Activity and Function of the Protein Arginine Methyltransferase 6
Gupta, S., Kadumuri, R. V., Singh, A. K., Chavali, S., & Dhayalan, A. (2021) · Life · doi:10.3390/life11090951 · Cited by 40
“PTEN negatively regulates AKT signaling by dephosphorylating the phosphatidylinositol-3,4,5-trisphosphate (PIP3) [145,146].”
BackgroundMolecular landscape of Hereditary Melanoma
Arnaut, J. R. M. B., Guimarães, I. D. S., dos Santos, A. C. E., da Silva, F. D. M. L., Machado, J. R. D. S., & de Melo, A. C. (2021) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2021.103425 · Cited by 41
Wen, X., Li, H., Sun, H. X., Zeng, A., Lin, R., Zhao, J., & Zhang, Z. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117718 · Cited by 37
Circulating microRNAs in human obesity: a systematic review
Ortiz-Dosal, A., Rodil-García, P., & Salazar‐Olivo, L. A. (2019) · Biomarkers · doi:10.1080/1354750x.2019.1606279 · Cited by 44
“As an example, PTEN is a tumour suppressor gene; the loss of function in this gene is associated with the constitutive activation of Akt and the increased risk of breast, thyroid, uterine, and other types of cancer (Hopkins et al. 2014).”
BackgroundSun, J., Yan, J.-Q., Yuan, X.-Z., Yang, R., Dan, T.-Y., Wang, X.-S., Kong, G.-Q., & Gao, S.-G. (2016) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-016-0022-0 · Cited by 34
“These crucial molecules involved in signaling pathways represent attractive targets for cancer therapy [54 – 57].”
BackgroundGene-based mediation analysis in epigenetic studies
Fang, R., Yang, H., Gao, Y., Cao, H., Goode, E. L., & Cui, Y. (2020) · Briefings in Bioinformatics · doi:10.1093/bib/bbaa113 · Cited by 30
“This gene has been identified as a PTEN-binding protein [53] and attenuates PTEN functions by binding to PTEN, which is a potent tumor suppressor gene.”
BackgroundWang, X.-H., Pang, L., Zhang, Y.-Q., Xu, J., Ding, D., Yang, T., Zhao, Q.-M., Wu, F., Li, F., Meng, H.-W., et al. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2499-6 · Cited by 32
“The AKT/mTOR signaling pathway is crucial for cell survival [11].”
BackgroundMarkowski, M. C., Marzo, A. M. D., & Antonarakis, E. S. (2017) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2017.1393518 · Cited by 33
“conversion of phosphatidylinositol-(3,4,5]-trisphosphate (PIP3) to phosphatidylinositol-(4,5)-bisphosphonate (PIP2) [38].”
TSPAN7 Exerts Anti-Tumor Effects in Bladder Cancer Through the PTEN/PI3K/AKT Pathway
Yu, X., Li, S.-L., Pang, M., Du, Y., Xu, T., Bai, T., Yang, K., Hu, J.-C., Zhu, S., Wang, L., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.613869 · Cited by 31
Steinbach, N., Hasson, D., Mathur, D., Στρατικόπουλος, Η., Sachidanandam, R., Bernstein, E., & Parsons, R. E. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz272 · Cited by 37
“To reveal novel functions of nuclear PTEN, we performed a yeast-2-hybrid (Y2H) screen using the PTEN C2TAILdomain, which is thought to facilitate most of PTEN’s known interactions with other proteins (43), as the baitfragment against a library of prey-fragments of the human fetal brain.”
MethodSelf-citationYu, W.-C., Li, D.-W., Ding, X., Sun, Y., Liu, Y., Cong, J.-P., Yang, J., Sun, J., Ning, X.-C., Wang, H., et al. (2019) · Aging · doi:10.18632/aging.101846 · Cited by 31
“com 1481 AGING approach to predict the target genes for miR-510a, and putatively identified PTEN, a tumor suppressor gene that is frequently mutated/deleted in cancers after the p53 and Rb genes [26].”
BackgroundJohnston, S. B., & Raines, R. T. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00028 · Cited by 31
PTEN Hamartoma Tumor Syndrome and Immune Dysregulation
Eissing, M., Ripken, L., Schreibelt, G., Westdorp, H., Ligtenberg, M., Netea-Maier, R., Netea, M., de Vries, I. D., & Hoogerbrugge, N. (2018) · Translational Oncology · doi:10.1016/j.tranon.2018.11.003 · Cited by 30
Miyata, H., Ashizawa, T., Iizuka, A., Kondou, R., Nonomura, C., Sugino, T., Urakami, K., Asai, A., Hayashi, N., Mitsuya, K., et al. (2017) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20021 · Cited by 39
Dilmaghani, N. A., Safaroghli‐Azar, A., Pourbagheri‐Sigaroodi, A., & Bashash, D. (2021) · IUBMB Life · doi:10.1002/iub.2446 · Cited by 30
“31).(57) Although it may be involved in a wide spectrum of cellular functions, PTEN intelligently blocks the PI3K/Akt signaling axis by depleting the cell reservoir from PIP3.”
BackgroundRegulatory non-coding RNAs in nervous system development and disease.
Oe, S., Kimura, T., & Yamada, H. (2019) · Frontiers in Bioscience · doi:10.2741/4776 · Cited by 29
“PTEN is a well-characterized tumor suppressor that is frequently mutated in various cancers (167).”
BackgroundZhu, C., Zhu, Q., Wu, Z., Yin, Y., Kang, D., Lu, S., & Liu, P. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25968 · Cited by 29
Xu, S.-Q., Qin, Y., Pan, D.-B., Ye, G.-X., Wu, C.-J., Wang, S., Jiang, J.-Y., Fu, J., & Wang, C.-J. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.4771 · Cited by 29
Wang, S., Liu, J. C., Kim, D., Datti, A., & Zacksenhaus, E. (2016) · Breast Cancer Research · doi:10.1186/s13058-015-0668-y · Cited by 29
“The latter is a phosphatase that converts phosphatidylinositol (3, 4, 5)-trisphosphate (PIP3) into phosphatidylinositol (4, 5)-disphosphate (PIP2), thereby antagonizing phoshotidylinositol-3 kinase (PI3K) pathway activation [6–8].”
BackgroundTenen, C. C., & Greenwald, I. (2019) · Current Biology · doi:10.1016/j.cub.2019.01.076 · Cited by 28
Diabetic Polyneuropathy: New Strategies to Target Sensory Neurons in Dorsal Root Ganglia
Miyashita, A., Kobayashi, M., Yokota, T., & Zochodne, D. W. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065977 · Cited by 30
Perdoncin, M., Konrad, A., Wyner, J. R., Lohana, S., Pillai, S. S., Pereira, D. G., Lakhani, H. V., & Sodhi, K. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.756499 · Cited by 39
Vidotto, T., Tiezzi, D. G., & Squire, J. A. (2018) · Molecular Cytogenetics · doi:10.1186/s13039-017-0348-y · Cited by 27
Xie, C.-Y., Kong, J., Zhao, C., Xiao, Y.-C., Peng, T., Liu, Y., & Wang, W.-N. (2016) · Developmental and Comparative Immunology · doi:10.1016/j.dci.2016.01.004 · Cited by 27
Jandy, M., Noor, A., Nelson, P. A., Dennys, C. N., Karabinas, I. M., Pestoni, J. C., Singh, G. D., Luc, L., Devyldere, R., Perdomo, N., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102247 · Cited by 26
“Interestingly, we also observed the activation of PTEN, an inhibitor of the PI3K/Akt pathway that acts through the dephosphorylation of phosphatidylinositol (3,4,5)-triphosphate (PIP3) to phosphatidylinositol (4,5)-bi-phosphate (PIP2) [54].”
BackgroundTargeting the PI3K/PTEN/AKT/mTOR Pathway in Treatment of Sarcoma Cell Lines.
Lim, H.-J., Wang, X., Crowe, P., Goldstein, D., & Yang, J.-L. (2016) · Anticancer Research · doi:10.21873/anticanres.11160 · Cited by 26
Wang, Y., Chen, B.-Y., Wang, Z., Zhang, W., Hao, K., Chen, Y., Li, K.-Q., Wang, T.-T., Xie, Y.-W., Huang, Z., et al. (2016) · OncoTarget · doi:10.18632/oncotarget.12654 · Cited by 26
“How does MTE promote the apoptosis of Jurkat cells? Since several studies have reported that phosphatases and tensin homolog (PTEN) is an essential tumor suppressor gene which encodes a phosphatase protein that antagonizes the PI3K/AKT/mTOR antiapoptotic pathway [12, 13], we next examined whether MTE promoted the apop…”
BackgroundNuclear PTEN’s Functions in Suppressing Tumorigenesis: Implications for Rare Cancers
Langdon, C. G. (2023) · Biomolecules · doi:10.3390/biom13020259 · Cited by 27
“Disrupting these PDZ-BD and PDZ interactions may lead to dysregulated subcellular localization as seen with MAST2 (microtubule associated serine/threonine kinase 2), PTEN, and the rabies viral glycoprotein or with MAGI-1b, -2, or -3 (membrane-associated guanylate kinase) scaffolding proteins and PTEN [54,64].”
Distinguishing between PTEN clinical phenotypes through mutation analysis
Portelli, S., Barr, L., de Sá, A. G. C., Pires, D. E. V., & Ascher, D. B. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.05.028 · Cited by 28
“PTEN activity is closely regulated by its subcellular localization, which is mediated by post-translational modifications (PTMs) including phosphorylation, SUMOylation and ubiquitination, as well as protein–protein interactions [1,2].”
BackgroundThe role of PTEN - HCV core interaction in hepatitis C virus replication
Wu, Q., Li, Z.-B., Mellor, P., Zhou, Y., Anderson, D. H., & Liu, Q. (2017) · Scientific Reports · doi:10.1038/s41598-017-03052-w · Cited by 25
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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