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 301–400 of 401

Maduramicin-activated protein phosphatase 2A results in extracellular signal-regulated kinase 1/2 inhibition, leading to cytotoxicity in myocardial H9c2 cells
Chen, X., & Jiang, S. (2017) · Toxicology Letters · doi:10.1016/j.toxlet.2017.12.003 · Cited by 8
Regulation of β-Catenin Phosphorylation by PR55β in Adenoid Cystic Carcinoma
Ishibashi, K., Ishii, K., Sugiyama, G., Kamata, Y., SUZUKI, A., Kumamaru, W., Ohyama, Y., Nakano, H., Kiyoshima, T., Sumida, T., et al. (2018) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20064 · Cited by 8
Small-molecule modulators of B56-PP2A restore 4E-BP function to suppress eIF4E-dependent translation in cancer cells
Lum, M. A., Jonas, K. A., Parmar, S., Black, A. R., O’Connor, C. M., Dobersch, S., Yamamoto, N., Robertson, T. M., Schutter, A., Giambi, M., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci176093 · Cited by 7
PP2A-Mediated GSK3β Dephosphorylation Is Required for Protocadherin-7-Dependent Regulation of Small GTPase RhoA in Osteoclasts
Kim, H., Takegahara, N., & Choi, Y. (2023) · Cells · doi:10.3390/cells12151967 · Cited by 7
Genetic Events Other than BCR-ABL1
Neviani, P. (2014) · Current Hematologic Malignancy Reports · doi:10.1007/s11899-013-0194-x · Cited by 9
Self-citation
Calycosin stimulates the proliferation of endothelial cells, but not breast cancer cells, via a feedback loop involving RP11-65M17.3, BRIP1 and ERα
Wang, Y., Xie, W., Hou, M., Tian, J., Zhang, X., Ren, Q., Huang, Y., & Chen, J. (2021) · Aging · doi:10.18632/aging.202641 · Cited by 7
Protein phosphatase 2A regulated by USP7 is polyubiquitinated and polyneddylated
Do, H., & Baek, K. (2022) · Oncology Reports · doi:10.3892/or.2022.8335 · Cited by 7
PME-1 sensitizes glioblastoma cells to oxidative stress-induced cell death by attenuating PP2A-B55α-mediated inactivation of MAPKAPK2-RIPK1 signaling
Guffens, L., Derua, R., & Janssens, V. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01572-1 · Cited by 7
Beyond tyrosine kinase inhibitors: Combinations and other agents
Cayssials, É., & Guilhot, F. (2016) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2016.10.017 · Cited by 7
Synthesis and Biological Evaluation of FTY720 (Fingolimod) Derivatives with Aromatic Head Group as Anticancer Agents
Lee, T., Moon, H. S., Kim, S. W., Shrestha, J., Shin, S. M., Lee, J., Kim, S., Park, E., & Baek, D. J. (2018) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c18-00065 · Cited by 7
PATZ1 induces PP4R2 to form a negative feedback loop on IKK/NF-κB signaling in lung cancer
Ho, M., Liang, C., & Liang, S. (2016) · Oncotarget · doi:10.18632/oncotarget.10427 · Cited by 6
Retracted
Differential Expression of Genes for Ubiquitin Ligases in Medulloblastoma Subtypes
Vriend, J. P., & TATE, R. B. (2019) · The Cerebellum · doi:10.1007/s12311-019-1009-y · Cited by 6
GRB10 sustains AR activity by interacting with PP2A in prostate cancer cells
Hao, J., Ci, X., Wang, Y., Choi, S. Y. C., Sullivan, S. E., Xue, H., Wu, R., Dong, X., Haegert, A. M., Collins, C. C., et al. (2020) · International Journal of Cancer · doi:10.1002/ijc.33335 · Cited by 6
Cancer stem cell phosphatases
Momeny, M., Arsiola, T., & Westermarck, J. K. (2021) · Biochemical Journal · doi:10.1042/bcj20210254 · Cited by 6
A phase I study of the combination of palbociclib and dexamethasone for the treatment of relapsed or refractory B-cell acute lymphoblastic leukemia
Wilde, L. R., Porazzi, P., Trotta, R., Dominici, M. D., Palmisiano, N. D., Keiffer, G., Rancani, K., Yingling, K., Calabretta, B., & Kasner, M. T. (2023) · Leukemia Research · doi:10.1016/j.leukres.2023.107075 · Cited by 6
Unraveling the complexity: A comprehensive analysis of the PP2A in cancer and its potential for novel targeted therapies
Ivovič, D., Kabelíková, P., & Jurkovičová, D. (2023) · Neoplasma · doi:10.4149/neo_2023_230806n411 · Cited by 7
Identification of PP2A and S6 Kinase as Modifiers of Leucine-Rich Repeat Kinase-Induced Neurotoxicity
Sim, J. P. L., Wang, Z., Basil, A. H., Lin, S., Chen, Z., Zhang, C., Zeng, L., Cai, Y., & Lim, K. (2019) · NeuroMolecular Medicine · doi:10.1007/s12017-019-08577-z · Cited by 6
UBE4B promotes the development of lung adenocarcinoma by enhancing proliferation, migration and glycolysis via PP2A/AKT signaling
Song, W. C., Xie, L., Cheng, S., Fan, Z., Sang, H., & Li, Q. (2022) · Pathology - Research and Practice · doi:10.1016/j.prp.2022.153762 · Cited by 6
Comprehensive analysis reveals the potential value of inflammatory response genes in the prognosis, immunity, and drug sensitivity of lung adenocarcinoma
Song, C., Pan, S., Li, D., Hao, B., Lu, Z., Lai, K., Li, N., & Geng, Q. (2022) · BMC Medical Genomics · doi:10.1186/s12920-022-01340-7 · Cited by 6
Inhibition of PP2A by LB100 sensitizes bladder cancer cells to chemotherapy by inducing p21 degradation
Gao, S., Shan, L., Zhang, M., Wang, Y., Zhan, X., Yin, Y., Jiang, Z., Tao, X., Li, X., Ye, M., et al. (2022) · Cellular Oncology · doi:10.1007/s13402-022-00710-8 · Cited by 6
News in the studies of multidrug resistance of breast cancer cells
Stavrovskaya, A. A., & Guens, G. P. (2015) · Advances in molecular oncology · doi:10.17650/2313-805x.2015.2.1.039-051 · Cited by 6
Aneuploidy related transcriptional changes in endometrial cancer link low expression of chromosome 15q genes to poor survival
Mauland, K. K., Wik, E., Høivik, E. A., Kusonmano, K., Halle, M. K., Berg, A., Haugland, H. K., Oyan, A. M., Kalland, K., Stefansson, I. M., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.14201 · Cited by 6
A Novel Mouse Model of Combined Hepatocellular-Cholangiocarcinoma Induced by Diethylnitrosamine and Loss of Ppp2r5d
Omella, J. D., Cortesi, E. E., Verbinnen, I., Remmerie, M., Wu, H., Cubero, F. J., Roskams, T., & Janssens, V. (2023) · Cancers · doi:10.3390/cancers15164193 · Cited by 6
Genome-wide association analyses of ovarian cancer patients undergoing primary debulking surgery identify candidate genes for residual disease
Ramachandran, D., Tyrer, J. P., Kommoss, S., DeFazio, A., Riggan, M. J., AOCS Group, Bowtell, D. D. L., Fereday, S., Traficante, N., Hung, J. A., et al. (2024) · npj Genomic Medicine · doi:10.1038/s41525-024-00395-y · Cited by 5
Novel PP2A-Activating Compounds in Neuroblastoma
Nazam, N., Bownes, L. V., Julson, J. R., Quinn, C. H., Erwin, M. H., Marayati, R., Markert, H. R., Shirley, S., Stewart, J. E., Yoon, K. J., et al. (2024) · Cancers · doi:10.3390/cancers16223836 · Cited by 6
CircRNA encoded-peptide: Potential stock in the transcriptomics market
Ma, S., Su, S., Zhang, X., Wang, X., & Yi, H. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123643 · Cited by 5
Synthesis, spectroscopic characterization, pH dependent redox mechanism and DNA binding behavior of chlorohydroxyaniline derivatives
Shahzad, S., Shah, A., Sirajuddin, M., Adhikari, B., Ahmad, K., Rana, U. A., Ali, S., Khan, G. S., Qureshi, R., & Kraatz, H. (2014) · RSC Advances · doi:10.1039/c4ra03434a · Cited by 5
Arsenic Sulfide Promotes Apoptosis in Retinoid Acid Resistant Human Acute Promyelocytic Leukemic NB4-R1 Cells through Downregulation of SET Protein
Tian, Y., Liu, Y., He, P., Liu, F., Zhou, N.-C., Cheng, X., Shi, L., Zhu, H., Zhao, J., Wang, Y., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0083184 · Cited by 5
A two-stage approach of gene network analysis for high-dimensional heterogeneous data
Lee, S., Liang, F., Cai, L., & Xiao, G. (2017) · Biostatistics · doi:10.1093/biostatistics/kxx033 · Cited by 5
HBV Remodels PP2A Complexes to Rewire Kinase Signaling in Hepatocellular Carcinoma
Turnham, R. E., Pitea, A., Jang, G. Μ., Xu, Z., Lim, H. C., Choi, A. L., Dollen, J. V., Levin, R. S., Webber, J. T., McCarthy, E. E., et al. (2024) · Cancer Research · doi:10.1158/0008-5472.can-24-0456 · Cited by 4
Regulatory variants in cancer-related pathway genes predict survival of patients with surgically resected non-small cell lung cancer
Shin, K. M., Hong, M. J., Lee, S. Y., Jin, C., Baek, S. A., Lee, J. H., Choi, J. E., Kang, H., Lee, W. K., Seok, Y., et al. (2017) · Gene · doi:10.1016/j.gene.2017.12.055 · Cited by 4
Marine Polyether Phycotoxin Palytoxin Induces Apoptotic Cell Death via Mcl-1 and Bcl-2 Downregulation
Kim, J., Ji, S., Lee, J., Lorquin, J., Orlikova-Boyer, B., Cerella, C., Mazumder, A., Muller, F., Dicato, M. A., Detournay, O., et al. (2023) · Marine Drugs · doi:10.3390/md21040233 · Cited by 5
A translational study for biomarker identification of PEP-010, a pro-apoptotic peptide restoring apoptosis in cancer models
Germini, D., Farhat, R., Dadon, L., Lacroix, A., Némati, F., Rebollo, A., Decaudin, D., Wiels, J., & Brenner, C. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167492 · Cited by 4
Identifying the SUMO1 modification of FAM122A leading to the degradation of PP2A-Cα by ubiquitin-proteasome system
Fan, F., Zhao, J., Liu, Y., Zhao, H., Weng, L., Li, Q., Chen, G., & Xu, Y. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.04.135 · Cited by 4
Nitration of protein phosphatase 2A increases via Epac1/PLCε/CaMKII/HDAC5/iNOS cascade in human endometrial stromal cell decidualization
Lee, S. Y., Lee, Y. Y., Choi, J. S., Kim, K. S., Min, D. S., Park, S., & Han, J. (2020) · The FASEB Journal · doi:10.1096/fj.202001212r · Cited by 4
Nanocatalyst Complex Can Dephosphorylate Key Proteins in MAPK Pathway for Cancer Therapy
Tang, R., Jia, Y., Zheng, W., Feng, Q., Zheng, W., & Jiang, X. (2018) · Advanced Healthcare Materials · doi:10.1002/adhm.201800533 · Cited by 4
Genome-wide identification of PP2A gene family in Camellia sinensis reveals the potential role of CsPP2A-TON2/FASS1 in abiotic stress
Bhattacharjee, S., Paul, A., Jana, A., Unnati, G. M., Deepak, R., Miao, Y., Lu, H., Shen, G., & Mishra, N. (2025) · PeerJ · doi:10.7717/peerj.19431 · Cited by 3
Prognostic Impact of PPP2R5C Gene Expression in Adult Acute Myeloid Leukemia Patients with Normal Cytogenetics
Taweel, M. A. E., Gawdat, R. M., & Abdelfattah, R. (2019) · Indian Journal of Hematology and Blood Transfusion · doi:10.1007/s12288-019-01142-5 · Cited by 3
Phosphatases: Their Roles in Cancer and Their Chemical Modulators
Fontanillo, M., & Köhn, M. (2015) · Springer eBooks · doi:10.1007/978-3-319-22473-2_10 · Cited by 3
Transcriptomics analyses reveal the effects of Pentagamaboronon-0-ol on PI3K/Akt and cell cycle of HER2+ breast cancer cells
Hermawan, A., Wulandari, F., Utomo, R. Y., Susidarti, R. A., Kirihata, M., & Meiyanto, E. (2023) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2023.101847 · Cited by 3
PP2A negatively regulates NK cell T-bet expression and anti-tumor effector function
Shinzawa, Y., Hara, D., Shinguryo, Y., Yokoyama, S., Kawada, M., & Hayakawa, Y. (2024) · International Immunology · doi:10.1093/intimm/dxae057 · Cited by 3
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
Protocadherin-7 Regulates Monocyte Migration Through Regulation of Small GTPase RhoA and Rac1
Kim, H., Takegahara, N., & Choi, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020572 · Cited by 2
Endogenous inhibitors of PP2A activate oncogenic and DNA damage response kinases in glioblastoma
Jacob, J., Nimjee, S. M., Elder, J. B., Chakravarti, A., & Palanichamy, K. (2026) · Cancer Letters · doi:10.1016/j.canlet.2026.218325 · Cited by 2
Theophylline represses IL-8 secretion from ASM cells independently of PDE inhibition: novel role as a PP2A activator
Patel, B. S., Rahman, M. M., Rumzhum, N. N., Oliver, B. G. G., Verrills, N. M., & Ammit, A. J. (2015) · Cited by 2
In vitro anticancer evaluation of micelles containing N-(4-(2-((4-methoxybenzyl)amino)ethyl)phenyl)heptanamide, an analogue of fingolimod
Yoon, M. S., Lee, Y. J., Park, C., Hong, J. T., Baek, D. J., & Shin, D. H. (2020) · Archives of Pharmacal Research · doi:10.1007/s12272-020-01276-5 · Cited by 2
Synthesis and anticancer profile of novel FTY720 analogues with azobenzene frameworks
Fazekašová, S., Gonda, J., Martinková, M., Pilátová, M. B., Majirská, M., Turčanová, V., & Jáger, D. (2023) · Tetrahedron · doi:10.1016/j.tet.2023.133391 · Cited by 2
In Silico and In Vivo Studies of a Tumor-Penetrating and Interfering Peptide with Antitumoral Effect on Xenograft Models of Breast Cancer
Marin, G. H., Murail, S., Andrini, L. B., García, M. N., Loisel, S., Tufféry, P., & Rebollo, A. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15041180 · Cited by 2
An LC–MS/MS Method for Simultaneous Determination of LB-100 and Its Active Metabolite, Endothall, in Human Plasma
Feng, Y., Massarelli, E., Forman, E., Kovach, J. S., Salgia, R., & Synold, T. W. (2023) · Bioanalysis · doi:10.4155/bio-2023-0078 · Cited by 2
Identifying key genes and functionally enriched pathways in acute myeloid leukemia by weighted gene co-expression network analysis
Jian, J., Yuan, C., & Hao, H. (2024) · Journal of Applied Genetics · doi:10.1007/s13353-024-00881-0 · Cited by 2
SIV-Mediated Synaptic Dysfunction Is Associated with an Increase in Synapsin Site 1 Phosphorylation and Impaired PP2A Activity
Shekarabi, M., Robinson, J. A., Smith, M. D., & Burdo, T. H. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.0178-19.2019 · Cited by 2
A PP2A-mtATR-tBid axis links DNA damage-induced CIP2A degradation to apoptotic dormancy and therapeutic resistance in PDAC
Luo, Y., Biswas, H., Makinwa, Y., Liu, S., Dong, Z., Liu, J., Zhang, J., & Zou, Y. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217790 · Cited by 1
A study conducted in breast cancer cells found that (valproic acid) inhibits CIP2A/c-MYC/PI3K/Akt/mTOR signaling molecules and PD-L1
Zeinali, E., Bagheri, V., Rostami, E., Mansouri, A., & Sarab, G. A. (2025) · Human Gene · doi:10.1016/j.humgen.2025.201437 · Cited by 2
PR55α subunit of protein phosphatase 2A supports KRASG12D-driven tumorigenesis that requires YAP activation
Jenkins, C. B., Camero, A. L., Graff, B. T., Madduri, L. S. V., O’Connell, K. A., Hein, A. L., Smith, L. M., Enke, C. A., Dong, J., Hollingsworth, M. A., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03477-y · Cited by 1
Interplay Between Protein Phosphatase 2A (PP2A) and SE Translocation (SET) as Macromolecular Target of Anticancer Compounds: A Combined Computational and Experimental Study
Ribaudo, G., Pagano, M. A., Anyanwu, M., Giannangeli, M., Vezzoli, M., Visentin, A., Frezzato, F., Trentin, L., Brunati, A. M., & Gianoncelli, A. (2025) · Macromol—A Journal of Macromolecular Research · doi:10.3390/macromol5030043 · Cited by 1
H2AX phosphorylation driven by the SET-PP2A axis maintains glioma stem cell properties
Han, C., Li, N., Banerjee, A. T., Wang, L., Yang, Y., Zhong, Y., Wu, S., Manring, H. R., Zhang, N., Showalter, C. A., et al. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101961 · Cited by 1
PP2A regulation in acute myeloid leukemia: Mechanisms, stem cell biology, and therapeutic implication
Voronkov, M. V., Suslov, O., Parcha, P. K., Shastri, V. M., & Lamba, J. K. (2026) · ASPET Discovery · doi:10.1016/j.aspetd.2026.100026 · Cited by 1
Protein phosphatase 2A regulates senescence and immunogenicity in medulloblastoma models
Ho, W. S., Mondal, I., Liu, J., Sun, R., Huo, J., Gao, C., Das, O., Tieu, D., Sun, J., Lin, H., et al. (2026) · Journal of Clinical Investigation · doi:10.1172/jci196753 · Cited by 2
Role of Sphingolipids in Hematological Malignancies: Myeloproliferative Disorders
Moorthi, S., & Luberto, C. (2015) · Springer eBooks · doi:10.1007/978-3-319-20750-6_3 · Cited by 1
Endometrial Cancer Genetic Classification and Its Clinical Application
Ceppi, L., Dizon, D. S., & Birrer, M. J. (2019) · Springer eBooks · doi:10.1007/978-3-319-64513-1_3 · Cited by 1
Synthesis and Cytotoxic Activity of Fingolimod (FTY720) Analogs with Various Amide Head Groups
Kim, S. B., Kim, K. J., Shrestha, J., Oh, Y. S., Lee, J., Lee, S., Park, E., & Baek, D. J. (2022) · Pharmaceutical Chemistry Journal · doi:10.1007/s11094-022-02659-2 · Cited by 1
Letter by Cristóbal et al Regarding Article, “Protein Phosphatase 2A Regulates Cardiac Na + Channels”
Cristóbal, I., Sanz-Álvarez, M., Luque, M., Rojo, F., & García‐Foncillas, J. (2019) · Circulation Research · doi:10.1161/circresaha.119.314905 · Cited by 1
Monotherapy efficacy of BBB-permeable small molecule activators of PP2A in glioblastomaPreprint
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. M., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/777276 · Cited by 1
SET-PP2A complex as a new therapeutic target in KMT2A (MLL) rearranged AML.Preprint
Mambro, A. D., Arroyo-Berdugo, Y., Fioretti, T., Randles, M. J., Cozzuto, L., Rajeeve, V., Cevenini, A., Austin, M. J., Esposito, G., Ponomarenko, J. V., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-2583091/v1 · Cited by 1
Epigenetic reactivation of a neurodevelopmental phosphoprotein program in pituitary adenomasPreprint
Chittiboina, P., Mullaney, D., Bhatt, S., Mandal, D., Nwokoye, D., Stoica, S., Bhatt, D., Johnson, K. R., Elkhaloun, A. G., Dampier, C. H., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4768687/v1 · Cited by 1
Serine/Threonine-Protein Phosphatase 2A
Janssens, V. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101865-1
Human Oncoprotein and a Potential Cancer Therapy Target Cancerous Inhibitor of Protein Phosphatase 2A, an Emerging
Khanna, A., Pimanda, J. E., & Westermarck, J. K. (2013)
Ca2+ Controls the Epithelial Cell Quiescence-Proliferation Decision through Regulating IGF Signaling
Yi, X. (2020) · Deep Blue (University of Michigan)
Ras mutations in the Erk-MAPK pathway and Cancer
Li, J. (2020) · International Symposium on Artificial Intelligence for Medicine Sciences (ISAIMS) · doi:10.1145/3429889.3429891
Emerging Meningioma Therapies II: Immunotherapies, Novel Radiotherapy Techniques, and Other Experimental Approaches
Gill, C. M., & Brastianos, P. K. (2020) · Springer eBooks · doi:10.1007/978-3-030-59558-6_15
The Key Role of the Phosphatase PP2A in the Development of Acute Myeloid Leukemia
Marco, J., Peris, I., Vicente, C., & Arriazu, E. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.94380
Potential of phenothiazines to synergistically block calmodulin and reactivate PP2A in cancer cellsPreprint
Okutachi, S., Manoharan, G. B., & Abankwa, D. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.16.448716
Sec6 modulates PP2A phosphatase activity through alteration of the binding affinity of PP2A in A and C subunitsPreprint
Tanaka, T., Iino, M., & Goto, K. (2021) · Research Square · doi:10.21203/rs.3.rs-849519/v1
Overexpression of cancerous inhibitor ofPP2A (CIP2A) in acute myeloid leukemia
Hasanin, R., Mossallam, G. I., Elfishawi, S. M., Rabea, A. M., & Hamdy, N. (2022) · Expert Review of Hematology · doi:10.1080/17474086.2022.2072825
Identification of acute myeloid leukemia-driven genes by multi-dimensional approachPreprint
Jian, J., Hao, H., Liu, Q., Dong, W., Li, L., Liu, Y., Feng, G., Wang, J., Gao, S., Chen, L., et al. (2020) · doi:10.21203/rs.3.rs-29046/v1
Las PM10 inducen evasión de apoptosis a través de la activación de STAT3 vía las cinasas PKCζ y Src
Zárate, S. E. R. (2016) · doi:10.24275/uami.3484zg98v
Serine/Threonine-Protein Phosphatase 2A
Janssens, V. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101865
HBV rewires liver cancer signaling by altering PP2A complexesPreprint
Pitea, A., Turnham, R. E., Eckhardt, M., Jang, G. Μ., Zhong, X., Lim, H. C., Choi, A., Dollen, J. V., Levin, R. S., Webber, J. T., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.15.532845
Supplementary Tables and Figures from 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. (2023) · doi:10.1158/1535-7163.22522443.v1
Self-citation
Data from 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. (2023) · doi:10.1158/1535-7163.c.6543381
Self-citation
Data from 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. (2023) · doi:10.1158/1535-7163.c.6543381.v1
Self-citation
Data from Epstein-Barr Virus Induces Lymphangiogenesis and Lympth Node Metastasis via Upregulation of VEGF-C in Nasopharyngeal Carcinoma
Li, D., Chen, X., Wang, L., Wang, J., Wen, Y.-T., Zhou, Z., Li, J.-K., Liu, J., Cai, L., Zhong, S.-S., et al. (2023) · doi:10.1158/1541-7786.c.6545057.v1
Plat-M8 Prognostic Biomarker, its Related Genes, and Mechanistic Insights in Ovarian Cancer: A Systematic Review with Bioinformatic ValidationPreprint
Habiburrahman, M., & Flanagan, J. M. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4951684
The pro-tumorigenic role of protein phosphatase 2A via negative regulation of the cGAS-STING pathway in tumor-associated macrophages
Lu, R. O., Elguindy, M. M., Young, J. S., & Ho, W. S. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-14064-8.00022-9
Aging-dependent dysregulation of EXOSC2 is maintained in cancer as a dependencyPreprint
Skamagki, M., Zhang, C., Hacisuleyman, E., Galleti, G., Wu, C., Rajasekhar, V. K., Cha, H., Ata, D., Kim, J., Weisskittel, T., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.04.647279
Phosphoproteomic dysregulation drives tumor proliferation in Cushing’s diseasePreprint
Asuzu, D. T., Bhatt, D., Mullaney, D., Mandal, D., Nwokoye, D., Varghese, S., Lopez, D. T., Ramavenkat, N., Johnson, K., Elkahloun, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.28.679056
Genome-Wide Identification, Functional Characterization of Protein Phosphatase 2A (PP2A) Gene Family in Cicer arietinum Reveals the Potential Role of CaPP2A-A1 Under Abiotic Stress
Fernandes, N., Bhattacharjee, S., Anusha, D., Pandey, A. K., & Mishra, N. (2025) · Tropical Plant Biology · doi:10.1007/s12042-025-09453-w
Synthesis and characterization of potential PP2A modulators structurally based on Fingolimod
Rodrigues, A. I. M. (2014) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) · doi:10.34626/948r-m039
PLAT-M8 prognostic biomarker, its related genes, and mechanistic insights in ovarian cancer: A systematic review with bioinformatic validation
Habiburrahman, M., & Flanagan, J. M. (2026) · Heliyon · doi:10.1016/j.heliyon.2026.e44652
Pharmacological Reactivation of PP2A by SET/CIP2A Inhibition Attenuates Triple Negative Breast Cancer Progression
Barraza, G. A., Mondaca, J. M., Fernandez-Muñoz, J. M., Vinante, B. M., Flamini, M. I., & Sanchez, A. M. (2026) · Kinases and Phosphatases · doi:10.3390/kinasesphosphatases4020012
SET protein expression in canine neoplasms: evaluation of predictive potential
Ribeiro, A. B. D. S., Pedro, G., Teodoro, T. G. W., Kobayashi, P. E., Fonseca‐Alves, C. E., & Laufer-Amorim, R. (2026) · Journal of Comparative Pathology · doi:10.1016/j.jcpa.2026.03.003
PPP2R2C promotes aerobic glycolysis and mediates pemetrexed resistance in lung adenocarcinomas by upregulating TCP1-dependent protein folding of glycolytic enzymes
Chen, J., Wang, X., Wang, Z., Li, G., & Han, F. (2026) · Respiratory Research · doi:10.1186/s12931-026-03681-8
PP2A Activation as a Senotherapeutic in Neuroblastoma
Nazam, N., Shirley, S. N., Opara, J. C., Manzoor, S., Shaikh, M. G., Brown, M. L., Nande, P., Eakes, A. M., Kaimari, A., Leavenworth, J. W., et al. (2026) · Cancers · doi:10.3390/cancers18193088
Phosphoproteomic dysregulation promotes tumor proliferation in Cushing’s disease
Asuzu, D. T., Bhatt, D., Mullaney, D., Mandal, D., Nwokoye, D., Varghese, S., Lopez, D. T., Ramavenkat, N., Johnson, K. R., Elkahloun, A. G., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2528513123
HIF-1–mediated PPME1 expression promotes breast cancer progression via AKT activation and β-catenin recruitment
Lyu, Y., Talwar, V., Yang, Y., Kang, S.-S., Li, S., Salman, S., Drehmer, D., Wang, Y., (19800947), C. C., Ramu, V., et al. (2026) · Journal of Clinical Investigation · doi:10.1172/jci205415
Mechanisms of phosphorylation in colitis regulation: PP2Acα as an emerging therapeutic target for inflammatory bowel disease
Wu, G., Wang, C., Fang, C., & Li, J. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12847-y
Association of Cbl-Interacting Protein CIN85 with Protein Phosphatase 2A (PP2A) Partly Confer Neoplastic Properties to Human Leukemia Cell Lines
Aldahami, M. A., Alfrayh, R., Basmaeil, Y. S., Kulayb, H. N. B., Fatima, S., Alahmari, B., & Khatlani, T. (2026) · Cells · doi:10.3390/cells15201897
BindingDB Entry 50017445: The Pursuit of Enzyme Activation: A Snapshot of the Gold Rush.
BindingDB (2023) · UC San Diego · doi:10.7270/q24j0k63
BindingDB Entry 50016393: Small molecule therapeutics for tauopathy in Alzheimer's disease: Walking on the path of most resistance.
BindingDB (2023) · UC San Diego · doi:10.7270/q2cv4nqf
BindingDB Entry 50020539: The evolution of small molecule enzyme activators.
BindingDB (2024) · UC San Diego · doi:10.7270/q2b56q63

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