Cited by 401Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingPI3K/AKT/mTOR signaling in cancer

The DOI matches its Crossref record; 100 of the 103 references it cites were found in a registry or an index.

Protein phosphatase 2A: a target for anticancer therapy

Open access

Perrotti, Danilo, Neviani, Paolo·2013·The Lancet Oncology

DOI 10.1016/s1470-2045(12)70558-2PMC PMC3913484

Open this paper in CoChat — free account

Abstract

Protein phosphatase 2A (PP2A), one of the main serine-threonine phosphatases in mammalian cells, maintains cell homoeostasis by counteracting most of the kinase-driven intracellular signalling pathways. Unrestrained activation of oncogenic kinases together with inhibition of tumour suppressors is often required for development of cancer. PP2A has been shown to be genetically altered or functionally inactivated in many solid cancers and leukaemias, and is therefore a tumour suppressor. For example, the phosphatase activity of PP2A is suppressed in chronic myeloid leukaemia and other malignancies characterised by aberrant activity of oncogenic kinases. Preclinical studies show that pharmacological restoration of PP2A tumour-suppressor activity by PP2A-activating drugs (eg, FTY720) effectively antagonises cancer development and progression. Here, we discuss PP2A as a druggable tumour suppressor in view of the possible introduction of PP2A-activating drugs into anticancer therapeutic protocols.

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 · 10.1016/s1470-2045(12)70558-2

Cites

100 of 100 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.

1 retracted

Antitumor effects of OSU-2S, a nonimmunosuppressive analogue of FTY720, in hepatocellular carcinoma
Omar, H. A., Chou, C.-C., Berman-Booty, L. D., Ma, Y., Hung, J., Wang, D.-S., Kogure, T., Patel, T. C., Terracciano, L., Muthusamy, N., et al. (2011) · Hepatology · doi:10.1002/hep.24293 · Cited by 74
Retracted
The genomic and transcriptomic architecture of 2,000 breast tumours reveals novel subgroups
METABRIC Group, Curtis, C., Shah, S. P., Chin, S.-F., Turashvili, G., Rueda, O. M., Dunning, M. J., Speed, D., Lynch, A. G., Samarajiwa, S., et al. (2012) · Nature · doi:10.1038/nature10983 · Cited by 6,097
Oncogenic Transcription Factors in the Human Acute Leukemias
Look, A. T. (1997) · Science · doi:10.1126/science.278.5340.1059 · Cited by 1,181
Principles of Tumor Suppression
Sherr, C. J. (2004) · Cell · doi:10.1016/s0092-8674(03)01075-4 · Cited by 1,028
Bcl-2 family proteins and cancer
Yip, K. W., & Reed, J. C. (2008) · Oncogene · doi:10.1038/onc.2008.307 · Cited by 913
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
CIP2A inhibits PP2A in human malignancies
Junttila, M. R., Puustinen, P., Niemelä, M., Ahola, R., Arnold, H., Böttzauw, T., Ala-aho, R., Nielsen, C., Ivaska, J., Taya, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.044 · Cited by 677
The biology of CML blast crisis
Calabretta, B., & Perrotti, D. (2004) · Blood · doi:10.1182/blood-2003-12-4111 · Cited by 608
Self-citation
Protein phosphatase 2A regulatory subunits and cancer
Eichhorn, P. J. A., Creyghton, M. P., & Bernards, R. (2009) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2008.05.005 · Cited by 513
The tumor suppressor PP2A is functionally inactivated in blast crisis CML through the inhibitory activity of the BCR/ABL-regulated SET protein
Neviani, P., Santhanam, R., Trotta, R., Notari, M., Blaser, B. W., Liu, S., Mao, H. C., Chang, J. S., Galietta, A., Uttam, A., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.015 · Cited by 481
Self-citation

Show all 103 references

Sorted by citations

Items 101–200 of 401

Puerarin ameliorates acute lung injury by modulating NLRP3 inflammasome-induced pyroptosis
Cai, D., Zhao, Y., & Yu, F. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01137-8 · Cited by 44
Hyperphosphorylation of BCL-2 family proteins underlies functional resistance to venetoclax in lymphoid malignancies
Chong, S. J. F., Zhu, F., Dashevsky, O., Mizuno, R., Lai, J. X. H., Hackett, L. R., Ryan, C. E., Collins, M. C., Iorgulescu, J. B., Guièze, R., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci170169 · Cited by 44
Sphingosine kinase 1 in breast cancer
Geffken, K., & Spiegel, S. (2017) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.10.005 · Cited by 43
Sphingosine-1-phosphate signaling: A novel target for simultaneous adjuvant treatment of triple negative breast cancer and chemotherapy-induced neuropathic pain
Singh, S. K., & Spiegel, S. (2019) · Advances in Biological Regulation · doi:10.1016/j.jbior.2019.100670 · Cited by 43
PP2A Inactivation Mediated by PPP2R4 Haploinsufficiency Promotes Cancer Development
Sents, W., Meeusen, B., Kalev, P., Radaelli, E., Sagaert, X., Miermans, E., Haesen, D., Lambrecht, C., Dewerchin, M., Carmeliet, P., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2911 · Cited by 42
Microcystin-LR promotes cell proliferation in the mice liver by activating Akt and p38/ERK/JNK cascades
Liu, J., Wang, B., Huang, P., Wang, H., Xu, K., Wang, X., Xu, L., & Guo, Z. (2016) · Chemosphere · doi:10.1016/j.chemosphere.2016.08.002 · Cited by 43
A novel FTY720 analogue targets SET-PP2A interaction and inhibits growth of acute myeloid leukemia cells without inducing cardiac toxicity
Vicente, C., Arriazu, E., Martínez‐Balsalobre, E., Peris, I., Marcotegui, N., Ramírez, P. G., Pippa, R., Rabal, O., Oyarzábal, J., Guruceaga, E., et al. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.10.007 · Cited by 42
Altering phosphorylation in cancer through PP2A modifiers
Johnson, H., Narayan, S., & Sharma, A. K. (2024) · Cancer Cell International · doi:10.1186/s12935-023-03193-1 · Cited by 42
PP2A is a therapeutically targetable driver of cell fate decisions via a c-Myc/p21 axis in human and murine acute myeloid leukemia
Goswami, S., Mani, R., Nunes, J. J., Chiang, C., Zapolnik, K., Hu, E. Y., Frissora, F. W., Mo, X., Walker, L. A., Yan, P. S., et al. (2021) · Blood · doi:10.1182/blood.2020010344 · Cited by 41
BRCA1 deficiency in ovarian cancer is associated with alteration in expression of several key regulators of cell motility – A proteomics study
Gau, D. M., Lesnock, J. L., Hood, B. L., Bhargava, R., Sun, M., Darcy, K. M., Luthra, S., Chandran, U. R., Conrads, T. P., Edwards, R. P., et al. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1036203 · Cited by 40
Inhibitors of the PI3K/mTOR pathway prevent STAT5 phosphorylation inJAK2V617Fmutated cells through PP2A/CIP2A axis
Bartalucci, N., Calabresi, L., Balliu, M., Martinelli, S., Rossi, M. C., Villeval, J., Annunziato, F., Guglielmelli, P., & Vannucchi, A. M. (2017) · Oncotarget · doi:10.18632/oncotarget.18073 · Cited by 39
Protein phosphatase 2A-B55δ enhances chemotherapy sensitivity of human hepatocellular carcinoma under the regulation of microRNA-133b
Zhuang, Q., Zhou, T., He, C., Zhang, S., Qiu, Y., Luo, B., Zhao, R., Liu, H., Lin, Y., & Lin, Z. (2016) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-016-0341-z · Cited by 38
Targeting RNA N6-methyladenosine to synergize with immune checkpoint therapy
Zhou, X., Li, C., Chen, T., Li, W., Wang, X., & Yang, Q. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01746-6 · Cited by 38
Basal protein phosphatase 2A activity restrains cytokine expression: role for MAPKs and tristetraprolin
Rahman, M. M., Rumzhum, N. N., Morris, J. C., Clark, A. R., Verrills, N. M., & Ammit, A. J. (2015) · Scientific Reports · doi:10.1038/srep10063 · Cited by 38
Antihelminthic drug niclosamide inhibits CIP2A and reactivates tumor suppressor protein phosphatase 2A in non-small cell lung cancer cells
Kim, M.-O., Choe, M. H., Yoon, Y. N., Ahn, J., Yoo, M., Jung, K., An, S., Hwang, S., Oh, J. S., & Kim, J. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.08.009 · Cited by 39
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 38
The phosphorylated form of FTY720 activates PP2A, represses inflammation and is devoid of S1P agonism in A549 lung epithelial cells
Rahman, M. M., Prünte, L., Lebender, L. F., Patel, B. S., Gelissen, I. C., Hansbro, P. M., Morris, J. C., Clark, A. R., Verrills, N. M., & Ammit, A. J. (2016) · Scientific Reports · doi:10.1038/srep37297 · Cited by 37
Biased holoenzyme assembly of protein phosphatase 2A (PP2A): From cancer to small molecules
Haanen, T. J., O’Connor, C. M., & Narla, G. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102656 · Cited by 38
The protein phosphatase 2A regulatory subunit B55α is a modulator of signaling and microRNA expression in acute myeloid leukemia cells
Ruvolo, P. P., Ruvolo, V. R., Jacamo, R. O., Burks, J. K., Zeng, Z., Duvvuri, S. R., Zhou, L., Qiu, Y., Coombes, K. R., Zhang, N., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.05.006 · Cited by 36
PP2A inhibition with LB100 enhances cisplatin cytotoxicity and overcomes cisplatin resistance in medulloblastoma cells
Ho, W. S., Feldman, M. J., Maric, D., Amable, L., Hall, M. D., Feldman, G. M., Ray‐Chaudhury, A., Lizak, M. J., Vera, J.-C., Robison, A., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.6970 · Cited by 36
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
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
RABL6A inhibits tumor-suppressive PP2A/AKT signaling to drive pancreatic neuroendocrine tumor growth
Umesalma, S., Kaemmer, C. A., Kohlmeyer, J. L., Letney, B. L., Schab, A. M., Reilly, J. A., Sheehy, R. M., Hagen, J., Tiwari, N., Zhan, F., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci123049 · Cited by 35
To be or not to be: PP2A as a dual player in CNS functions, its role in neurodegeneration, and its interaction with brain insulin signaling
Javadpour, P., Dargahi, L., Ahmadiani, A., & Ghasemi, R. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03063-y · Cited by 35
Monotherapy efficacy of blood–brain barrier permeable small molecule reactivators of protein phosphatase 2A in glioblastoma
Merisaari, J., Denisova, O. V., Doroszko, M., Joncour, V. L., Johansson, P., Leenders, W. P. J., Kastrinsky, D. B., Zaware, N., Narla, G., Laakkonen, P., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa002 · Cited by 35
Persistence of Drug-Resistant Leukemic Stem Cells and Impaired NK Cell Immunity in CML Patients Depend on MIR300 Antiproliferative and PP2A-Activating Functions
Silvestri, G., Trotta, R., Stramucci, L., Ellis, J. J., Harb, J. G., Neviani, P., Wang, S., Eisfeld, A., Walker, C. J., Zhang, B., et al. (2020) · Blood Cancer Discovery · doi:10.1158/0008-5472.bcd-19-0039 · Cited by 37
Self-citation
SETting OP449 into the PP2A-Activating Drug Family
Neviani, P., & Perrotti, D. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-0166 · Cited by 36
Self-citation
PLA2G16 promotes osteosarcoma metastasis and drug resistance via the MAPK pathway
Li, L., Liang, S., Wasylishen, A. R., Zhang, Y., Yang, X., Zhou, B., Shan, L., Han, X., Mu, T., Wang, G., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7694 · Cited by 35
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 33
Hyperphosphorylation of PP2A in colorectal cancer and the potential therapeutic value showed by its forskolin-induced dephosphorylation and activation
Cristóbal, I., Rincón, R., Manso, R., Madoz‐Gúrpide, J., Caramés, C., del Puerto‐Nevado, L., Rojo, F., & García‐Foncillas, J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.06.032 · Cited by 34
Withanolides: Promising candidates for cancer therapy
Zhang, Q., Yuan, Y., Cao, S., Kang, N., & Qiu, F. (2024) · Phytotherapy Research · doi:10.1002/ptr.8090 · Cited by 35
FAM122A, a new endogenous inhibitor of protein phosphatase 2A
Fan, L., Liu, M.-H., Guo, M., Hu, C. X., Yan, Z.-W., Chen, J., Chen, G., & Huang, Y. (2016) · Oncotarget · doi:10.18632/oncotarget.11698 · Cited by 32
PRG-1 relieves pain and depressive-like behaviors in rats of bone cancer pain by regulation of dendritic spine in hippocampus
Liu, X., Xie, Z., Li, S., He, J., Cao, S., & Xiao, Z. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.59032 · Cited by 33
MYC-dependent recruitment of RUNX1 and GATA2 on the SET oncogene promoter enhances PP2A inactivation in acute myeloid leukemia
Pippa, R., Dominguez, A., Malumbres, R., Endo, A., Arriazu, E., Marcotegui, N., Guruceaga, E., & Odero, M. D. (2016) · Oncotarget · doi:10.18632/oncotarget.9840 · Cited by 32
Targeted co-delivery of Beclin 1 siRNA and FTY720 to hepatocellular carcinoma by calcium phosphate nanoparticles for enhanced anticancer efficacy
Wu, J., Wang, Z., Zhang, G., Lu, X., Qiang, G.-H., Hu, W. M., Ji, A., Wu, J., & Jiang, C. (2018) · International Journal of Nanomedicine · doi:10.2147/ijn.s156328 · Cited by 33
Activation of the Tumor Suppressor PP2A Emerges as a Potential Therapeutic Strategy for Treating Prostate Cancer
Cristóbal, I., Gónzález-Alonso, P., Daoud, L., Solano, E. C., Torrejón, B., Manso, R., Madoz‐Gúrpide, J., Rojo, F., & García‐Foncillas, J. (2015) · Marine Drugs · doi:10.3390/md13063276 · Cited by 32
The role of exosomes and MYC in therapy resistance of acute myeloid leukemia: Challenges and opportunities
Mudgapalli, N., Nallasamy, P., Chava, H., Chava, S. P., Pathania, A. S., Gunda, V., Gorantla, S., Pandey, M. K., Gupta, S. C., & Challagundla, K. B. (2019) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.10.001 · Cited by 31
PPP2R2A prostate cancer haploinsufficiency is associated with worse prognosis and a high vulnerability to B55α/PP2A reconstitution that triggers centrosome destabilization
Zhao, Z., Kurimchak, A., Nikonova, A. S., Feiser, F., Wasserman, J. S., Fowle, H. A., Varughese, T., Connors, M., Johnson, K. J., Makhov, P. B., et al. (2019) · Oncogenesis · doi:10.1038/s41389-019-0180-9 · Cited by 31
Inhibiting protein phosphatase 2A increases the antitumor effect of protein arginine methyltransferase 5 inhibition in models of glioblastoma
Otani, Y., Sur, H. P., Rachaiah, G., Namagiri, S., Chowdhury, A. K., Lewis, C. T., Shimizu, T., Gangaplara, A., Wang, X., Vézina, A., et al. (2021) · Neuro-Oncology · doi:10.1093/neuonc/noab014 · Cited by 33
Protein phosphatase complex PP5/PPP2R3C dephosphorylates P-glycoprotein/ABCB1 and down-regulates the expression and function
Katayama, K., Yamaguchi, M., Noguchi, K., & Sugimoto, Y. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.12.007 · Cited by 32
Development of novel PP2A activators for use in the treatment of acute myeloid leukaemia
Toop, H. D., Dun, M. D., Ross, B., Flanagan, H. M., Verrills, N. M., & Morris, J. C. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob00556j · Cited by 32
Therapeutic relevance of the protein phosphatase 2A in cancer
Cunningham, C. E., Li, S., Vizeacoumar, F. S., Bhanumathy, K. K., Lee, J. S., Parameswaran, S., Furber, L. A., Abuhussein, O., Paul, J. M., McDonald, M., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.11399 · Cited by 32
Isoliensinine induces dephosphorylation of NF-κB p65 subunit at Ser536 via a PP2A-dependent mechanism in hepatocellular carcinoma cells: roles of impairing PP2A/I2PP2A interaction
Shu, G., Zhang, L., Jiang, S., Cheng, Z., Wang, G., Huang, X., & Yang, X. (2016) · Oncotarget · doi:10.18632/oncotarget.9603 · Cited by 31
miR-650 promotes motility of anaplastic thyroid cancer cells by targeting PPP2CA
Orlandella, F. M., Mariniello, R. M., Iervolino, P. L. C., Imperlini, E., Mandola, A., Verde, A., Stefano, A. E. D., Pane, K., Franzese, M., Esposito, S., et al. (2019) · Endocrine · doi:10.1007/s12020-019-01910-3 · Cited by 31
Sphingosine 1-Phosphate Signaling and Metabolism in Chemoprevention and Chemoresistance in Colon Cancer
Grbčić, P., & Sedić, M. (2020) · Molecules · doi:10.3390/molecules25102436 · Cited by 31
Polyphyllin VII induces mitochondrial apoptosis by regulating the PP2A/AKT/DRP1 signaling axis in human ovarian cancer
Zhao, L., Liu, Z., Deng, X., Wang, J., Sun, L., Fan, L., & Zhang, Y. (2020) · Oncology Reports · doi:10.3892/or.2020.7879 · Cited by 33
Downregulation of PPP2R5E is a common event in acute myeloid leukemia that affects the oncogenic potential of leukemic cells
Cristóbal, I., Cirauqui, C., Castelló-Cros, R., García-Ortí, L., Calasanz, M. J., & Odero, M. D. (2013) · Haematologica · doi:10.3324/haematol.2013.084731 · Cited by 31
Novel B55α-PP2A mutations in AML promote AKT T308 phosphorylation and sensitivity to AKT inhibitor-induced growth arrest
Shouse, G., de Necochea-Campion, R., Mirshahidi, S., Liu, X., & Chen, C.-S. (2016) · Oncotarget · doi:10.18632/oncotarget.11209 · Cited by 30
A Role for the Twins Protein Phosphatase (PP2A-B55) in the Maintenance of Drosophila Genome Integrity
Merigliano, C., Marzio, A., Renda, F., Somma, M. P., Gatti, M., & Vernı̀, F. (2016) · Genetics · doi:10.1534/genetics.116.192781 · Cited by 30
Modulation of Mutant KrasG12D -Driven Lung Tumorigenesis In Vivo by Gain or Loss of PCDH7 Function
Zhou, X., Padanad, M. S., Evers, B. M., Smith, B., Novaresi, N., Suresh, S., Richardson, J. A., Stein, E., Zhu, J., Hammer, R. E., et al. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-18-0739 · Cited by 30
Functional importance of PP2A regulatory subunit loss in breast cancer
Watt, L. F., Panicker, N., Mannan, A., Copeland, B., Kahl, R. G. S., Dun, M. D., Young, B., Roselli, S., & Verrills, N. M. (2017) · Breast Cancer Research and Treatment · doi:10.1007/s10549-017-4403-5 · Cited by 29
Protein Phosphatase 2A as a Drug Target in the Treatment of Cancer and Alzheimer’s Disease
Wei, H., Zhang, H., Xie, J., Meng, D., Wang, X., Ke, D., Zeng, J., & Liu, R. (2020) · Current Medical Science · doi:10.1007/s11596-020-2140-1 · Cited by 30
PP2A-activating Drugs Enhance FLT3 Inhibitor Efficacy through AKT Inhibition–Dependent GSK-3β–Mediated c-Myc and Pim-1 Proteasomal Degradation
Scarpa, M., Singh, P., Bailey, C. M., Lee, J. K., Kapoor, S., Lapidus, R. G., Niyongere, S., Sangodkar, J., Wang, Y., Perrotti, D., et al. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-20-0663 · Cited by 30
Self-citation
Cancer TARGETases: DSB repair as a pharmacological target
Samadder, P., Aithal, R., Beláň, O., & Krejčí, L. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.02.007 · Cited by 31
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
Phosphatase inhibition increases AQP2 accumulation in the rat IMCD apical plasma membrane
Ren, H., Yang, B., Ruiz, J. A., Efe, O., Ilori, T. O., Sands, J. M., & Klein, J. D. (2016) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00150.2016 · Cited by 29
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 29
Emerging roles for LPP in metastatic cancer progression
Ngan, E., Kiepas, A., Brown, C. M., & Siegel, P. M. (2017) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-017-0415-5 · Cited by 28
Protein phosphatase 2A inhibition enhances radiation sensitivity and reduces tumor growth in chordoma
Hao, S., Song, H., Zhang, W., Seldomridge, A. N., Jung, J., Giles, A. J., Hutchinson, M.-K. N. D., Cao, X., Colwell, N. A., Lita, A., et al. (2017) · Neuro-Oncology · doi:10.1093/neuonc/nox241 · Cited by 28
Cucurbitacin B induces inhibitory effects via CIP2A/PP2A/Akt pathway in glioblastoma multiforme
Qin, S., Li, J., Si, Y., He, Z., Zhang, T., Wang, D., Liu, X., Guo, Y., Zhang, L. N., Li, S., et al. (2018) · Molecular Carcinogenesis · doi:10.1002/mc.22789 · Cited by 28
Berberine attenuates pulmonary arterial hypertension via protein phosphatase 2A signaling pathway both in vivo and in vitro
Luo, J., Gu, Y., Liu, P., Jiang, X., Yu, W., Ye, P., Chao, Y., Yang, H., Zhu, L., Zhou, L., et al. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26940 · Cited by 28
Regulation and role of the PP2A-B56 holoenzyme family in cancer
Peris, I., Romero-Murillo, S., Vicente, C., Narla, G., & Odero, M. D. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188953 · Cited by 30
Unraveling MYC’s Role in Orchestrating Tumor Intrinsic and Tumor Microenvironment Interactions Driving Tumorigenesis and Drug Resistance
Doha, Z. O., & Sears, R. C. (2023) · Pathophysiology · doi:10.3390/pathophysiology30030031 · Cited by 27
Oxidative stress is two‐sided in the treatment of acute myeloid leukemia
Fan, C., Yang, X., Yan, L., & Shi, Z. (2024) · Cancer Medicine · doi:10.1002/cam4.6806 · Cited by 27
MEF2A Regulates the MEG3-DIO3 miRNA Mega Cluster-Targeted PP2A Signaling in Bovine Skeletal Myoblast Differentiation
Wang, Y., Mei, C., Su, X., Wang, H., Yang, W., & Zan, L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112748 · Cited by 27
Cell-autonomous regulation of epithelial cell quiescence by calcium channel Trpv6
Xin, Y., Malick, A., Hu, M., Liu, C., Batah, H., Xu, H., & Duan, C. (2019) · eLife · doi:10.7554/elife.48003 · Cited by 27
Hypoxia-Induced miR-675-5p Supports β-Catenin Nuclear Localization by Regulating GSK3-β Activity in Colorectal Cancer Cell Lines
Saieva, L., Barreca, M. M., Zichittella, C., Prado, M. G., Tripodi, M., Alessandro, R., & Conigliaro, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113832 · Cited by 28
PP2A binds to the LIM domains of lipoma-preferred partner through its PR130/B″ subunit to regulate cell adhesion and migration
Janssens, V., Zwaenepoel, K., Rossé, C., Petit, M. M. R., Goris, J., & Parker, P. J. (2016) · Journal of Cell Science · doi:10.1242/jcs.175778 · Cited by 27
The evolution of small molecule enzyme activators
Dow, L. F., Case, A. M., Paustian, M. P., Pinkerton, B. R., Simeon, P., & Trippier, P. C. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00399j · Cited by 29
Microcystin-LR induces a wide variety of biochemical changes in the A549 human non-small cell lung cancer cell line: Roles for protein phosphatase 2A and its substrates
Wang, H., Xu, K., Wang, B., Liu, J., Wang, X., Xing, M., Huang, P., Guo, Z., & Xu, L. (2016) · Environmental Toxicology · doi:10.1002/tox.22305 · Cited by 26
Structure-Function Studies of the bHLH Phosphorylation Domain of TWIST1 in Prostate Cancer Cells
Gajula, R. P., Chettiar, S. T., Williams, R. D., Nugent, K. M., Katō, Y., Wang, H., Malek, R. A., Taparra, K., Cades, J., Annadanam, A., et al. (2015) · Neoplasia · doi:10.1016/j.neo.2014.10.009 · Cited by 25
Zinc-mediated activation of CREB pathway in proliferation of pulmonary artery smooth muscle cells in pulmonary hypertension
Xiao, G., Lian, G., Wang, T., Chen, W., Zhuang, W., Luo, L., Wang, H., & Xie, L. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00779-y · Cited by 25
Sphingosine Kinase 1 Signaling in Breast Cancer: A Potential Target to Tackle Breast Cancer Stem Cells
Hii, L., Chung, F. F., Mai, C., Ng, P. Y., & Leong, C. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.748470 · Cited by 25
Is there a link between autism and glyphosate-formulated herbicides?
Beecham, J. E., & Seneff, S. (2016) · Journal of Autism · doi:10.7243/2054-992x-3-1 · Cited by 24
Cardiomyocyte specific deletion of PP2A causes cardiac hypertrophy.
Li, L., Fang, C., Xu, D., Xu, Y., Fu, H., & Li, J. (2016) · PubMed Central · Cited by 25
PP2A deactivation is a common event in oral cancer and reactivation by FTY720 shows promising therapeutic potential
Velmurugan, B. K., Lee, C., Chiang, S., Hua, C., Chen, M., Lin, S., Yeh, K., & Ko, Y. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26001 · Cited by 24
PP2A Phosphatases Take a Giant Leap in the Post-Genomics Era
Bheri, M., & Pandey, G. K. (2019) · Current Genomics · doi:10.2174/1389202920666190517110605 · Cited by 24
Activation of the PP2A-B56α heterocomplex synergizes with venetoclax therapies in AML through BCL2 and MCL1 modulation
Peris, I., Romero-Murillo, S., Martínez‐Balsalobre, E., Farrington, C. C., Arriazu, E., Marcotegui, N., Jiménez-Muñoz, M., Alburquerque-Prieto, C., Torres-López, A., Fresquet, V. J., et al. (2022) · Blood · doi:10.1182/blood.2022016466 · Cited by 24
Frequent hypermethylation of WNT pathway genes in laryngeal squamous cell carcinomas
Paluszczak, J., Hemmerling, D., Kostrzewska‐Poczekaj, M., Jarmuż‐Szymczak, M., Grenman, R. A., Wierzbicka, M., & Baer‐Dubowska, W. (2014) · Journal of Oral Pathology and Medicine · doi:10.1111/jop.12178 · Cited by 24
A systematic evaluation of the safety and toxicity of fingolimod for its potential use in the treatment of acute myeloid leukaemia
Enjeti, A. K., D’Crus, A., Melville, K., Verrills, N. M., & Rowlings, P. (2016) · Anti-Cancer Drugs · doi:10.1097/cad.0000000000000358 · Cited by 23
Cucurbitacin B reverses multidrug resistance by targeting CIP2A to reactivate protein phosphatase 2A in MCF-7/Adriamycin cells
Cai, F., Zhang, L., Xiao, X., Duan, C., Huang, Q., Fan, C., Li, J., Liu, X., Li, S., & Liu, Y. (2016) · Oncology Reports · doi:10.3892/or.2016.4892 · Cited by 23
Pleiotropy of PP2A Phosphatases in Cancer with a Focus on Glioblastoma IDH Wildtype
Kashani, E., & Vassella, E. (2022) · Cancers · doi:10.3390/cancers14215227 · Cited by 22
ERK-mediated NELF-A phosphorylation promotes transcription elongation of immediate-early genes by releasing promoter-proximal pausing of RNA polymerase II
Ohe, S., Kubota, Y., Yamaguchi, K., Takagi, Y., Nashimoto, J., Kozuka‐Hata, H., Oyama, M., Furukawa, Y., & Takekawa, M. (2022) · Nature Communications · doi:10.1038/s41467-022-35230-4 · Cited by 23
YTHDF2 exerts tumor-suppressor roles in gastric cancer via up-regulating PPP2CA independently of m6A modification
Zhou, Y., Fan, K., Dou, N., Li, L., Wang, J., Chen, J., Li, Y., & Gao, Y. (2023) · Biological Procedures Online · doi:10.1186/s12575-023-00195-1 · Cited by 23
The therapeutic effects of SET/I2PP2A inhibitors on canine melanoma
Enjoji, S., Yabe, R., Fujiwara, N., Tsuji, S., Vitek, M. P., Mizuno, T., Nakagawa, T., Usui, T., Ohama, T., & Sato, K. (2015) · Journal of Veterinary Medical Science · doi:10.1292/jvms.15-0193 · Cited by 23
CIP2A high expression is a poor prognostic factor in normal karyotype acute myeloid leukemia
Barragan, E., Chillon, M. C., Castello-Cros, R., Marcotegui, N., Prieto, M. I., Hoyos, M., Pippa, R., Llop, M., Etxabe, A., Cervera, J., et al. (2015) · Haematologica · doi:10.3324/haematol.2014.118117 · Cited by 22
Understanding the regulatory landscape of protein phosphatase 2A (PP2A): Pharmacological modulators and potential therapeutics
Neale, D. B., Morris, J. C., Verrills, N. M., & Ammit, A. J. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108834 · Cited by 25
Immediate‐early response 5 (IER5) interacts with protein phosphatase 2A and regulates the phosphorylation of ribosomal protein S6 kinase and heat shock factor 1
Kawabata, S., Ishita, Y., Ishikawa, Y., & Sakurai, H. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.013 · Cited by 21
Phosphorylation state of the histone variant H2A.X controls human stem and progenitor cell fate decisions
Orlando, L., Tanasijevic, B., Nakanishi, M., Reid, J. C., García‐Rodríguez, J. L., Chauhan, K. D., Porras, D. P., Aslostovar, L., Lu, J. D., Shapovalova, Z., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108818 · Cited by 21
Harnessing the power of sphingolipids: Prospects for acute myeloid leukemia
Ung, J., Tan, S., Fox, T. E., Shaw, J. J. P., Vass, L. R., Costa‐Pinheiro, P., Garrett-Bakelman, F. E., Keng, M. K., Sharma, A. K., Claxton, D. F., et al. (2022) · Blood Reviews · doi:10.1016/j.blre.2022.100950 · Cited by 24
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
Cellular and Molecular Networks in Chronic Myeloid Leukemia: The Leukemic Stem, Progenitor and Stromal Cell Interplay
Perrotti, D., Silvestri, G., Stramucci, L., Yu, J. E., & Trotta, R. (2016) · Current Drug Targets · doi:10.2174/1389450117666160615074120 · Cited by 22
Self-citation
Phosphoproteomics Profiling of Nonsmall Cell Lung Cancer Cells Treated with a Novel Phosphatase Activator
Wiredja, D. D., Ayati, M., Mazhar, S., Sangodkar, J., Maxwell, S., Schlatzer, D., Narla, G., Koyutürk, M., & Chance, M. R. (2017) · PROTEOMICS · doi:10.1002/pmic.201700214 · Cited by 22
Resveratrol inhibits Erk1/2‐mediated adhesion of cancer cells via activating PP2A–PTEN signaling network
Chen, X., Hu, X., Li, Y., Zhu, C., Dong, X., Zhang, R., Ma, J., Huang, S., & Chen, L. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27100 · Cited by 22
Synergistic Interaction of HOXB13 and CIP2A Predisposes to Aggressive Prostate Cancer
Sipeky, C., Gao, P. H., Zhang, Q., Wang, L., Ettala, O. O., Talala, K. M., Tammela, T. L. J., Auvinen, A. P., Wiklund, F. E., Wei, G., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-0444 · Cited by 22
FTY720-induced enhancement of autophagy protects cells from FTY720 cytotoxicity in colorectal cancer
Li, J., Wang, S., Zhang, D., Sun, Y., Zhu, C., FEI, Q., Hu, J., Zhang, C., & Sun, Y. (2016) · Oncology Reports · doi:10.3892/or.2016.4668 · Cited by 21
Inhibition of Protein Phosphatase 2A Sensitizes Mucoepidermoid Carcinoma to Chemotherapy via the PI3K-AKT Pathway in Response to Insulin Stimulus
Liu, L., Wang, H., Cui, J., Zhang, Q., Zhang, W. J., Xu, W., Lü, H., Liu, S., Shen, S., Fang, F. Y., et al. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000494008 · Cited by 21
Proliferation inhibition and apoptosis induction of imatinib-resistant chronic myeloid leukemia cells via PPP2R5C down-regulation
Shen, Q., Liu, S., Chen, Y., Yang, L., Chen, S., Wu, X., Li, B., Lu, Y., Zhu, K., & Li, Y. (2013) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-6-64 · Cited by 20
Ten years of research on the role of BVES/POPDC1 in human disease: a review
Han, P., Lei, Y., Li, D., Liu, J., Yan, W., & Tian, D. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s192364 · Cited by 20
MHC Phosphopeptides: Promising Targets for Immunotherapy of Cancer and Other Chronic Diseases
Mahoney, K. E., Shabanowitz, J., & Hunt, D. F. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100112 · Cited by 20

Authors: Perrotti, D., & Neviani, P.
Affiliations: The Ohio State University (US)
Corresponding author: Perrotti, Danilo
ORCID: Perrotti, Danilo
Neviani, Paolo
Venue: The Lancet Oncology
Publisher: Elsevier BV
Published: 2013-05
Volume: 14
Issue: 6
Pages: e229-e238
ISSN: 1470-2045 (ISSN-L)
DOI: 10.1016/s1470-2045(12)70558-2
PMC: PMC3913484
OpenAlex: W1987474302
Cited by: 400
References: 103
Citations by year: 2026: 13 · 2025: 17 · 2024: 16 · 2023: 33 · 2022: 31 · 2021: 26 · 2020: 33 · 2019: 35 · 2018: 29 · 2017: 37 · 2016: 62 · 2015: 29 · 2014: 28 · 2013: 11
FWCI: 3.99
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: The Lancet Oncology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Cancer Institute (P50CA140158, R01CA163800, R01CA095512, P30CA016058)
Topics: 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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Keywords: protein phosphatase 2A, tumour suppressor, cancer therapy, fingolimod, oncogenic kinase, serine/threonine phosphatase, chronic myeloid leukemia, therapeutic target
MeSH terms: Animals, Antineoplastic Agents, Enzyme Activation, Humans, Neoplasms, Drug Design, Signal Transduction, Enzyme Activators, Protein Phosphatase 2, Molecular Targeted Therapy

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

Protein phosphatase 2A: a target for anticancer therapy

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