Targeting SET/I2PP2A oncoprotein functions as a multi-pathway strategy for cancer therapy

Switzer, C H; Cheng, R Y S; Vitek, T M; Christensen, D J; Wink, D A; Vitek, M P

doi:10.1038/onc.2010.622

Cited by 172Protein Kinase Regulation and GTPase SignalingMechanisms of cancer metastasisCancer Mechanisms and Therapy

Targeting SET/I2PP2A oncoprotein functions as a multi-pathway strategy for cancer therapy

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Switzer, C H, Cheng, R Y S, Vitek, T M, Christensen, D J, Wink, D A, Vitek, M P·2011·Oncogene

DOI 10.1038/onc.2010.622PMC PMC3107340

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Abstract

The SET oncoprotein participates in cancer progression by affecting multiple cellular processes, inhibiting the tumor suppressor protein phosphatase 2A (PP2A), and inhibiting the metastasis suppressor nm23-H1. On the basis of these multiple activities, we hypothesized that targeted inhibition of SET would have multiple discrete and measurable effects on cancer cells. Here, the effects of inhibiting SET oncoprotein function on intracellular signaling and proliferation of human cancer cell lines was investigated. We observed the effects of COG112, a novel SET interacting peptide, on PP2A activity, Akt signaling, nm23-H1 activity and cellular migration/invasion in human U87 glioblastoma and MDA-MB-231 breast adenocarcinoma cancer cell lines. We found that COG112 interacted with SET protein and inhibited the association between SET and PP2A catalytic subunit (PP2A-c) and nm23-H1. The interaction between COG112 and SET caused PP2A phosphatase and nm23-H1 exonuclease activities to increase. COG112-mediated increases in PP2A activity resulted in the inhibition of Akt signaling and cellular proliferation. Additionally, COG112 inhibited SET association with Ras-related C(3) botulinum toxin substrate 1 (Rac1), leading to decreased cellular migration and invasion. COG112 treatment releases the SET-mediated inhibition of the tumor suppressor PP2A, as well as the metastasis suppressor nm23-H1. These results establish SET as a novel molecular target and that the inhibition of SET may have beneficial effects in cancer chemotherapy.

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SET is a physiological PP2A inhibitor that binds directly to PP2A/C and appears to act as an oncogene.
“SET is a physiologic PP2A inhibitor that binds directly to the PP2A/C subunit (Switzer et al., 2011). Consistent with the prevalent view that a fraction of PP2A holoenzymes exhibit tumor suppressor functions, SET appears to act as an oncogene.”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Switzer et al., 2011

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Circular MTHFD2L RNA-encoded CM-248aa inhibits gastric cancer progression by targeting the SET-PP2A interaction
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Deregulation of the PP2A inhibitor SET shows promising therapeutic implications and determines poor clinical outcome in patients with metastatic colorectal cancer
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Stable SET knockdown in head and neck squamous cell carcinoma promotes cell invasion and the mesenchymal-like phenotype in vitro, as well as necrosis, cisplatin sensitivity and lymph node metastasis in xenograft tumor models
Sobral, L. M., Sousa, L. O., Coletta, R. D., Cabral, H., Greene, L. J., Tajara, E. H., Gutkind, J. S., Curti, C., & Leopoldino, A. M. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-32 · Cited by 76 · see citing works
Differential Processing of let-7a Precursors Influences RRM2 Expression and Chemosensitivity in Pancreatic Cancer: Role of LIN-28 and SET Oncoprotein
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Nitric oxide and protein phosphatase 2A provide novel therapeutic opportunities in ER-negative breast cancer
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The basic biology of PP2A in hematologic cells and malignancies
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Effect of FTY720 on the SET–PP2A complex in acute myeloid leukemia; SET binding drugs have antagonistic activity
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Protein phosphatase 2A and tau: an orchestrated ‘Pas de Deux’
Taleski, G., & Sontag, E. (2017) · FEBS Letters · doi:10.1002/1873-3468.12907 · Cited by 70 · see citing works
Rac1 activation links tau hyperphosphorylation and Aβ dysmetabolism in Alzheimer’s disease
Borin, M., Saraceno, C., Catania, M., Lorenzetto, E., Pontelli, V., Paterlini, A., Fostinelli, S., Avesani, A., Di Fede, G., Zanusso, G., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0567-4 · Cited by 68 · see citing works
Protein Phosphatase 2A as a Therapeutic Target in Acute Myeloid Leukemia
Arriazu, E., Pippa, R., & Odero, M. D. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00078 · Cited by 67 · see citing works
Viewing serine/threonine protein phosphatases through the eyes of drug designers
Zhang, M., Yogesha, S. D., Mayfield, J. E., Gill, G. N., & Zhang, Y. (2013) · FEBS Journal · doi:10.1111/febs.12481 · Cited by 66 · see citing works
Maintenance of higher H2O2 levels, and its mechanism of action to induce growth in breast cancer cells: Important roles of bioactive catalase and PP2A
Sen, S., Kawahara, B., & Chaudhuri, G. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.06.030 · Cited by 65 · see citing works
Erlotinib derivative inhibits hepatocellular carcinoma by targeting CIP2A to reactivate protein phosphatase 2A
Yu, H.-C., Hung, M.-H., Chen, Y.-L., Chu, P.-Y., Wang, C. Y., Chao, T.-T., Liu, C.-Y., Shiau, C.-W., & Chen, K.-F. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.325 · Cited by 63 · see citing works
Circular RNA hsa_circ_0000673 promotes hepatocellular carcinoma malignance by decreasing miR-767-3p targeting SET
Jiang, W., Wen, D., Gong, L., Wang, Y., Liu, Z., & Yin, F. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.04.041 · Cited by 62 · see citing works
Using the MCoTI-II Cyclotide Scaffold To Design a Stable Cyclic Peptide Antagonist of SET, a Protein Overexpressed in Human Cancer
D’Souza, C., Henriques, S. T., Wang, C. K. L., Cheneval, O., Chan, L. Y., Bokil, N. J., Sweet, M. J., & Craik, D. J. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00529 · Cited by 61 · see citing works
PP2A-Mediated Anticancer Therapy
Chen, W., Wang, Z., Jiang, C., & Ding, Y. (2013) · Gastroenterology Research and Practice · doi:10.1155/2013/675429 · Cited by 57 · see citing works
SET protein accumulates in HNSCC and contributes to cell survival: Antioxidant defense, Akt phosphorylation and AVOs acidification
Leopoldino, A. M., SQUARIZE, C. H., Garcia, C. B., Almeida, L. O., Pestana, C. R., Sobral, L. M., Uyemura, S. A., Tajara, E. H., Gutkind, J. S., & Curti, C. (2012) · Oral Oncology · doi:10.1016/j.oraloncology.2012.05.014 · Cited by 56 · see citing works
27-hydroxycholesterol: A novel player in molecular carcinogenesis of breast and prostate cancer
Marwarha, G., Raza, S., Hammer, K. D. P., & Ghribi, O. (2017) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2017.05.012 · Cited by 56 · see citing works
Semaphorin 3A elevates endothelial cell permeability through PP2A inactivation
Le Guelte, A., Galan-Moya, E.-M., Dwyer, J., Treps, L., Kettler, G., Hebda, J. K., Dubois, S., Auffray, C., Chneiweiss, H., Bidere, N., et al. (2012) · Journal of Cell Science · doi:10.1242/jcs.108282 · Cited by 80 · see citing works
Targeting SET to restore PP2A activity disrupts an oncogenic CIP2A-feedforward loop and impairs triple negative breast cancer progression
Liu, C., Huang, T., Chen, Y., Chen, J.-L., Chu, P., Huang, C.-T., Wang, W.-L., Lau, K.-Y., Dai, M., Shiau, C., et al. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2018.12.032 · Cited by 51 · see citing works
Upregulation of the oncoprotein SET determines poor clinical outcomes in hepatocellular carcinoma and shows therapeutic potential
Hung, M.-H., Chen, Y.-L., Chu, P.-Y., Shih, C.-T., Yu, H.-C., Tai, W.-T., Shiau, C.-W., & Chen, K.-F. (2016) · Oncogene · doi:10.1038/onc.2016.21 · Cited by 49 · see citing works
The concept of the okadaic acid class of tumor promoters is revived in endogenous protein inhibitors of protein phosphatase 2A, SET and CIP2A, in human cancers
Fujiki, H., Sueoka, E., Watanabe, T., & Suganuma, M. (2018) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-018-2765-7 · Cited by 49 · see citing works
Deregulation of the protein phosphatase 2A, PP2A in cancer: complexity and therapeutic options
Grech, G., Baldacchino, S., Saliba, C., Grixti, M. P., Gauci, R., Magri, V. P., Fenech, A. G., & Scerri, C. A. (2016) · Tumor Biology · doi:10.1007/s13277-016-5145-4 · Cited by 48 · see citing works
Lyn sustains oncogenic signaling in chronic lymphocytic leukemia by strengthening SET-mediated inhibition of PP2A
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The Rac1 hypervariable region in targeting and signaling
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Paclitaxel resistance in MCF-7/PTX cells is reversed by paeonol through suppression of the SET/phosphatidylinositol 3-kinase/Akt pathway
Zhang, W., Cai, J., Chen, S., Zheng, X., Hu, S., Dong, W., Lü, J., Xing, J., & Dong, Y. (2012) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3468 · Cited by 44 · see citing works
PP2A Inhibits Cervical Cancer Cell Migration by Dephosphorylation of p-JNK, p-p38 and the p-ERK/MAPK Signaling Pathway
Zheng, H., Shen, F., Tong, Y., & Li, Y. (2018) · Current Medical Science · doi:10.1007/s11596-018-1854-9 · Cited by 44 · see citing works
Mitochondrial-associated nitric oxide synthase activity inhibits cytochrome c oxidase: Implications for breast Cancer
Sen, S., Kawahara, B., & Chaudhuri, G. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.545 · Cited by 42 · see citing works
A comprehensive and perspective view of oncoprotein SET in cancer
Bayarkhangai, B., Noureldin, S., Yu, L., Zhao, N., Gu, Y., Xu, H., & Guo, C. (2018) · Cancer Medicine · doi:10.1002/cam4.1526 · Cited by 38 · see citing works
Strategies for Targeting Serine/Threonine Protein Phosphatases with Small Molecules in Cancer
Zhang, Q., Fan, Z., Zhang, L., You, Q., & Wang, L. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00631 · Cited by 38 · see citing works
Inhibition of Pten deficient Castration Resistant Prostate Cancer by Targeting of the SET - PP2A Signaling axis
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The Role of MYC and PP2A in the Initiation and Progression of Myeloid Leukemias
Pippa, R., & Odero, M. D. (2020) · Cells · doi:10.3390/cells9030544 · Cited by 36 · see citing works
SET-mediated NDRG1 inhibition is involved in acquisition of epithelial-to-mesenchymal transition phenotype and cisplatin resistance in human lung cancer cell
Liu, H., Gu, Y., Yin, J., Zheng, G., Wang, C., Zhang, Z., Deng, M., Liu, J., Jia, X., & He, Z. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.08.010 · Cited by 36 · see citing works
SET antagonist enhances the chemosensitivity of non-small cell lung cancer cells by reactivating protein phosphatase 2A
Hung, M., Wang, C., Chen, Y., Chu, P., Hsiao, Y., Tai, W., Chao, T.-T., Yu, H.-C., Shiau, C., & Chen, K. (2015) · Oncotarget · doi:10.18632/oncotarget.6313 · Cited by 35 · see citing works
Endogenous inhibitor proteins that connect Ser/Thr kinases and phosphatases in cell signaling
Eto, M., & Brautigan, D. L. (2012) · IUBMB Life · doi:10.1002/iub.1067 · Cited by 34 · see citing works
Combined targeting of SET and tyrosine kinases provides an effective therapeutic approach in human T-cell acute lymphoblastic leukemia
Richard, N. P., Pippa, R., Cleary, M. M., Puri, A., Tibbitts, D., Mahmood, S., Christensen, D. J., Jeng, S., McWeeney, S. K., Look, A. T., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.12394 · Cited by 34 · see citing works
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The interaction of SET and protein phosphatase 2A as target for cancer therapy
Dacol, E. C., Wang, S., Chen, Y., & Lepique, A. P. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188578 · Cited by 34 · see citing works
Discovery of a small molecule targeting SET-PP2A interaction to overcome BCR-ABLT315I mutation of chronic myeloid leukemia
Wang, S., Xie, W., Wang, D., Peng, Z., Zheng, Y., Liu, N., Dai, W., Wang, Y., Wang, Z., Yang, Y., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3665 · Cited by 32 · see citing works
Cytoplasmic targeting of the proto‐oncogene SET promotes cell spreading and migration
Lam, B. D., Anthony, E. C., & Hordijk, P. L. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.11.013 · Cited by 30 · see citing works
Therapeutic Re-Activation of Protein Phosphatase 2A in Acute Myeloid Leukemia
Ramaswamy, K., Spitzer, B. G., & Kentsis, A. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00016 · Cited by 30 · see citing works
Potential anti-tumor effects of FTY720 associated with PP2A activation: a brief review
Cristóbal, I., Madoz‐Gúrpide, J., Manso, R., Gónzález-Alonso, P., Rojo, F., & García‐Foncillas, J. (2016) · Current Medical Research and Opinion · doi:10.1185/03007995.2016.1162774 · Cited by 29 · see citing works
Targeting few to help hundreds: JAK, MAPK and ROCK pathways as druggable targets in atypical chronic myeloid leukemia
Rocca, S., Carrà, G., Poggio, P., Morotti, A., & Brancaccio, M. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0774-4 · Cited by 28 · see citing works
Reprogramming the oncogenic response: SET protein as a potential therapeutic target in cancer
Hung, M., & Chen, K. (2017) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1336226 · Cited by 28 · see citing works
Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c
Rivero-Rodríguez, F., Dı́az-Quintana, A., Velázquez‐Cruz, A., González‐Arzola, K., Gavilán, M. P., Velázquez‐Campoy, A., Rios, R. M., la Rosa, M. Á. D., & Díaz‐Moreno, I. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101967 · Cited by 27 · see citing works
A Vesicular Stomatitis Virus‐Inspired DNA Nanocomplex for Ovarian Cancer Therapy
Zhao, W., Yang, Y., Song, L., Kang, T., Du, T., Wu, Y., Xiong, M., Luo, L., Long, J., Men, K., et al. (2017) · Advanced Science · doi:10.1002/advs.201700263 · Cited by 25 · see citing works
PP2A and Its Inhibitors in Helper T-Cell Differentiation and Autoimmunity
Khan, M. M., Ullah, U., Khan, M. H., & Lahesmaa, R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.786857 · Cited by 25 · see citing works
Identification of miR-145 targets through an integrated omics analysis
Huang, T., Renuse, S., Pinto, S. M., Kumar, P., Yang, Y., Chaerkady, R., Godsey, B., Mendell, J. T., Halushka, M. K., Civin, C. I., et al. (2014) · Molecular BioSystems · doi:10.1039/c4mb00585f · Cited by 25 · see citing works
3-Bromopyruvate treatment induces alterations of metabolic and stress-related pathways in glioblastoma cells
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Cellular inhibitors of Protein Phosphatase PP2A in cancer.
Haesen, D., Sents, W., Ivanova, E., Lambrecht, C., & Janssens, V. (2012) · Lirias · Cited by 24 · see citing works
Deregulation of SET is Associated with Tumor Progression and Predicts Adverse Outcome in Patients with Early-Stage Colorectal Cancer
Cristóbal, I., Torrejón, B., Rubio, J., Santos, A., Pedregal, M., Caramés, C., Zazo, S., Luque, M., Sanz-Álvarez, M., Madoz‐Gúrpide, J., et al. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8030346 · Cited by 23 · see citing works
Targeting inhibitor 2 of protein phosphatase 2A as a therapeutic strategy for prostate cancer treatment
Mukhopadhyay, A., Tabanor, K., Chaguturu, R., & Aldrich, J. V. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.25943 · Cited by 23 · see citing works
Pathologic significance of SET/I2PP2A-mediated PP2A and non-PP2A pathways in polycystic ovary syndrome (PCOS)
Jiang, S., Xu, S., Chen, H., Liu, X., Tang, Z., Cui, Y., & Liu, J. (2016) · Clinica Chimica Acta · doi:10.1016/j.cca.2016.11.010 · Cited by 23 · see citing works
Protocadherin 7 is overexpressed in castration resistant prostate cancer and promotes aberrant MEK and AKT signaling
Shishodia, G., Koul, S., & Koul, H. K. (2019) · The Prostate · doi:10.1002/pros.23898 · Cited by 22 · see citing works
Vascular smooth muscle RhoA counteracts abdominal aortic aneurysm formation by modulating MAP4K4 activity
Molla, M. R., Shimizu, A., Komeno, M., Rahman, N. I. A., Soh, J. E. C., Nguyen, L. K. C., Khan, M. R., Tesega, W. W., Chen, S., Pang, X., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-04042-z · Cited by 22 · see citing works
Targeting phosphatases: From molecule design to clinical trials
Guo, M., Li, Z., Gu, M., Gu, J., You, Q., & Wang, L. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.116031 · Cited by 23 · see citing works
Proteomics Identified Overexpression of SET Oncogene Product and Possible Therapeutic Utility of Protein Phosphatase 2A in Alveolar Soft Part Sarcoma
Kubota, D., Yoshida, A., Kawai, A., & Kondo, T. (2014) · Journal of Proteome Research · doi:10.1021/pr400929h · Cited by 22 · see citing works
Functional modulation of the metastatic suppressor Nm23-H1 by oncogenic viruses
Saha, A., & Robertson, E. S. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.08.007 · Cited by 22 · see citing works
Downregulation of microRNA-199b predicts unfavorable prognosis and emerges as a novel therapeutic target which contributes to PP2A inhibition in metastatic colorectal cancer
Cristóbal, I., Caramés, C., Rincón, R., Manso, R., Madoz‐Gúrpide, J., Torrejón, B., Gónzález-Alonso, P., Rojo, F., & García‐Foncillas, J. (2016) · Oncotarget · doi:10.18632/oncotarget.11174 · Cited by 22 · see citing works
Exploring and exploiting plant cyclic peptides for drug discovery and development
Zhang, J., Yuan, J., Li, Z., Fu, C., Xu, M., Yang, J., Jiang, X. M., Zhou, B., Ye, X., & Xu, C. (2021) · Medicinal Research Reviews · doi:10.1002/med.21792 · Cited by 21 · see citing works
A Potential Therapeutic Application of SET/I2PP2A Inhibitor OP449 for Canine T-cell Lymphoma
Fujiwara, N., Kawasaki, H., Yabe, R., Christensen, D. J., Vitek, M. P., Mizuno, T., Sato, K., & Ohama, T. (2012) · Journal of Veterinary Medical Science · doi:10.1292/jvms.12-0366 · Cited by 21 · see citing works
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Pre-Clinical Study Evaluating Novel Protein Phosphatase 2A Activators as Therapeutics for Neuroblastoma
Bownes, L. V., Marayati, R., Quinn, C. H., Beierle, A. M., Hutchins, S. C., Julson, J. R., Erwin, M. H., Stewart, J. E., Mroczek‐Musulman, E., Ohlmeyer, M. H. J., et al. (2022) · Cancers · doi:10.3390/cancers14081952 · Cited by 20 · see citing works
CIP2A Constrains Th17 Differentiation by Modulating STAT3 Signaling
Khan, M. M., Ullah, U., Khan, M. H., Kong, L., Moulder, R., Välikangas, T., Bhosale, S. D., Komsi, E., Rasool, O., Chen, Z. J., et al. (2020) · iScience · doi:10.1016/j.isci.2020.100947 · Cited by 18 · see citing works
Stable SET knockdown in breast cell carcinoma inhibits cell migration and invasion
Li, J., Yang, X., Ren, X., Meng, X.-J., Huang, H., Zhao, Q.-H., Yuan, J., Hong, W., Xia, B., Huang, X., et al. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.09.013 · Cited by 19 · see citing works
Identification of PP2A/Set Binding Sites and Design of Interacting Peptides with Potential Clinical Applications
Tian, L., Zhang, X., Haesen, D., Bravo, J., Fominaya, J. M., Choquet, S., Zini, J. M., Loisel, S., Waelkens, E., Janssens, V., et al. (2017) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-017-9633-1 · Cited by 19 · see citing works
Bifunctional Therapeutic Peptides for Targeting Malignant B Cells and Hepatocytes: Proof of Concept in Chronic Lymphocytic Leukemia
Simón‐Gracia, L., Savier, É., Parizot, C., Brossas, J. Y., Loisel, S., Teesalu, T., Conti, F., Charlotte, F., Scatton, O., Aoudjehane, L., et al. (2020) · Advanced Therapeutics · doi:10.1002/adtp.202000131 · Cited by 18 · see citing works
SET alpha and SET beta mRNA isoforms in chronic lymphocytic leukaemia
Brander, D. M., Friedman, D. R., Volkheimer, A. D., Christensen, D. J., Rassenti, L. Z., Kipps, T. J., Guadalupe, E., Chen, Y., Zhang, D., Wang, X., et al. (2018) · British Journal of Haematology · doi:10.1111/bjh.15677 · Cited by 18 · see citing works
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Proteomic Analysis on Anti-Proliferative and Apoptosis Effects of Curcumin Analog, 1,5-bis(4-Hydroxy-3-Methyoxyphenyl)-1,4-Pentadiene-3-One-Treated Human Glioblastoma and Neuroblastoma Cells
Lee, Y. Q., Rajadurai, P., Abas, F., Othman, I., & Naidu, R. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.645856 · Cited by 18 · see citing works
SET protein overexpression contributes to paclitaxel resistance in MCF-7/S cells through PI3K/Akt pathway
Zhang, W., Zheng, X., Meng, T., You, H., Dong, Y., Xing, J., & Chen, S. (2016) · Journal of drug targeting · doi:10.1080/1061186x.2016.1245307 · Cited by 17 · see citing works
Identification and characterization of novel enhanced cell penetrating peptides for anti-cancer cargo delivery
Zhang, X., Brossas, J. Y., Parizot, C., Zini, J. M., & Rebollo, A. (2017) · Oncotarget · doi:10.18632/oncotarget.23179 · Cited by 17 · see citing works
Analysis of nucleo‐cytoplasmic shuttling of the proto‐oncogene SET/I2PP2A
Lam, B. D., Anthony, E. C., & Hordijk, P. L. (2011) · Cytometry Part A · doi:10.1002/cyto.a.21153 · Cited by 17 · see citing works
Oncoprotein SET-associated transcription factor ZBTB11 triggers lung cancer metastasis
Xu, W., Yao, H., Wu, Z., Yan, X., Jiao, Z., Liu, Y., Zhang, M., & Wang, D. (2024) · Nature Communications · doi:10.1038/s41467-024-45585-5 · Cited by 16 · see citing works
Subcellular Proteomics Reveals a Role for Nucleo-cytoplasmic Trafficking at the DNA Replication Origin Activation Checkpoint
Mulvey, C. M., Tudzarova, S., Crawford, M., Williams, G. H., Stoeber, K., & Godovac‐Zimmermann, J. (2013) · Journal of Proteome Research · doi:10.1021/pr3010919 · Cited by 16 · see citing works
OP449 inhibits breast cancer growth without adverse metabolic effects
Shlomai, G., Zelenko, Z., Antoniou, I. M., Stasinopoulos, M., Tobin‐Hess, A., Vitek, M. P., LeRoith, D., & Gallagher, E. J. (2017) · Endocrine Related Cancer · doi:10.1530/erc-17-0077 · Cited by 16 · see citing works
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PP2A as the Main Node of Therapeutic Strategies and Resistance Reversal in Triple-Negative Breast Cancer
Zhao, H., Li, D., Zhang, B., Qi, Y., Diao, Y.-P., Zhen, Y., & Shu, X. H. (2017) · Molecules · doi:10.3390/molecules22122277 · Cited by 16 · see citing works
Human apolipoprotein E genotypes differentially modify house dust mite-induced airway disease in mice
Yao, X., Dai, C., Fredriksson, K., Lam, J. Y., Gao, M., Keeran, K. J., Nugent, G. Z., Qu, X., Yu, Z., Jeffries, N. O., et al. (2011) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00110.2011 · Cited by 14 · see citing works
SET protein accumulation prevents cell death in head and neck squamous cell carcinoma through regulation of redox state and autophagy
Ouchida, A. T., Uyemura, V. T., Queiroz, A. L., Brauer, V. S., Neto, M. P. C., Sousa, L. O., Uyemura, S. A., Curti, C., & Leopoldino, A. M. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.01.005 · Cited by 15 · see citing works

The interaction of SET and protein phosphatase 2A as target for cancer therapy
Dacol, E. C., Wang, S., Chen, Y., & Lepique, A. P. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188578 · Cited by 34 · see citing works
PP2A inhibitor SET promotes mTORC1 and Bmi1 signaling through Akt activation and maintains the colony-formation ability of cancer cells
Kohyanagi, N., Kitamura, N., Ikeda, S., Shibutani, S., Sato, K., & Ohama, T. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105584 · Cited by 11 · see citing works
Stable SET knockdown in breast cell carcinoma inhibits cell migration and invasion
Li, J., Yang, X., Ren, X., Meng, X.-J., Huang, H., Zhao, Q.-H., Yuan, J., Hong, W., Xia, B., Huang, X., et al. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.09.013 · Cited by 19 · see citing works
1HN, 13C, and 15N backbone resonance assignments of the SET/TAF-1β/I2PP2A oncoprotein (residues 23–225)
Roth, B. M., Palma, R. M. D., Cook, M. E., Varney, K. M., Weber, D. J., & Öğretmen, B. (2021) · Biomolecular NMR Assignments · doi:10.1007/s12104-021-10034-7 · Cited by 3 · see citing works
Overexpression of PP2A inhibitor SET oncoprotein is associated with tumor progression and poor prognosis in human non-small cell lung cancer
Liu, H., Gu, Y., Wang, H., Yin, J., Zheng, G., Zhang, Z., Lu, M., Wang, C., & He, Z. (2015) · Oncotarget · doi:10.18632/oncotarget.3818 · Cited by 94 · see citing works

Authors: Switzer, C. H., Cheng, R. Y. S., Vitek, T. M., Christensen, D. J., Wink, D. A., & Vitek, M. P.
Affiliations: National Institutes of Health (US)
Cognosci (United States) (US)
Duke Medical Center (US)
Corresponding author: Wink, D A
Vitek, M P
ORCID: Switzer, C H
Cheng, R Y S
Christensen, D J
Wink, D A
Vitek, M P
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 2011-02-07
Volume: 30
Issue: 22
Pages: 2504-2513
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/onc.2010.622
PMC: PMC3107340
OpenAlex: W2021359328
Cited by: 171
References: 50
Citations by year: 2026: 2 · 2025: 6 · 2024: 3 · 2023: 11 · 2022: 12 · 2021: 12 · 2020: 9 · 2019: 10 · 2018: 11 · 2017: 16 · 2016: 15 · 2015: 14 · 2014: 15 · 2013: 14 · 2012: 15
FWCI: 6.49
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Cancer Institute (ZIASC007281, ZIABC010899)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mechanisms of cancer metastasis
Health Sciences › Medicine › Pathology and Forensic Medicine › Cancer Mechanisms and Therapy
Keywords: protein phosphatase 2A, nm23-H1, Akt signaling, cell proliferation, cell migration and invasion, Rac1, glioblastoma, breast adenocarcinoma, metastasis suppressor, tumor suppressor gene reactivation, cancer therapy targets
MeSH terms: Antineoplastic Agents, Cell Movement, DNA-Binding Proteins, Humans, Neoplasms, Peptides, Transcription Factors, Signal Transduction, rac1 GTP-Binding Protein, Cell Line, Tumor, Cell Proliferation, Proto-Oncogene Proteins c-akt, NM23 Nucleoside Diphosphate Kinases, Histone Chaperones

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Targeting SET/I2PP2A oncoprotein functions as a multi-pathway strategy for cancer therapy

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