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B56‐containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX‐1 and ERK

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AKT/PKB Signaling: Navigating the Network

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MiR-222 Overexpression Confers Cell Migratory Advantages in Hepatocellular Carcinoma through Enhancing AKT Signaling

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Ceramides in Alzheimer’s Disease: Key Mediators of Neuronal Apoptosis Induced by Oxidative Stress and A <b> <i>β</i> </b> Accumulation

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Multiple functions of p27 in cell cycle, apoptosis, epigenetic modification and transcriptional regulation for the control of cell growth: A double-edged sword protein

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Activation of tumor suppressor protein PP2A inhibits KRAS-driven tumor growth

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Identification of Integrator-PP2A complex (INTAC), an RNA polymerase II phosphatase

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New insights into Notch1 regulation of the PI3K–AKT–mTOR1 signaling axis: Targeted therapy of γ-secretase inhibitor resistant T-cell acute lymphoblastic leukemia

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LncRNA-HGBC stabilized by HuR promotes gallbladder cancer progression by regulating miR-502-3p/SET/AKT axis

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Regulation of FOXO Factors in Mammalian Cells

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A PP2A Regulatory Subunit Regulates C. elegans Insulin/IGF-1 Signaling by Modulating AKT-1 Phosphorylation

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Cell survival and metastasis regulation by Akt signaling in colorectal cancer

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REDD1 enhances protein phosphatase 2A-mediated dephosphorylation of Akt to repress mTORC1 signaling

Dennis, M. D., Coleman, C. S., Berg, A., Jefferson, L. S., & Kimball, S. R. (2014) · Science Signaling · doi:10.1126/scisignal.2005103 · Cited by 159 · see citing works

The broken “Off” switch in cancer signaling: PP2A as a regulator of tumorigenesis, drug resistance, and immune surveillance

Ruvolo, P. P. (2016) · BBA Clinical · doi:10.1016/j.bbacli.2016.08.002 · Cited by 143 · see citing works

Both Decreased and Increased SRPK1 Levels Promote Cancer by Interfering with PHLPP-Mediated Dephosphorylation of Akt

Wang, P., Zhou, Z., Hu, A., de Albuquerque, C. P., Zhou, Y., Hong, L., Sierecki, E., Ajiro, M., Kruhlak, M. J., Harris, C. C., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.007 · Cited by 142 · see citing works

New Insights into Protein Kinase B/Akt Signaling: Role of Localized Akt Activation and Compartment-Specific Target Proteins for the Cellular Radiation Response

Szymonowicz, K., Oeck, S., Malewicz, N. M., & Jendrossek, V. (2018) · Cancers · doi:10.3390/cancers10030078 · Cited by 134 · see citing works

SET oncoprotein overexpression in B-cell chronic lymphocytic leukemia and non-Hodgkin lymphoma: a predictor of aggressive disease and a new treatment target

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PHLPP-1 Negatively Regulates Akt Activity and Survival in the Heart

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Akt: a key transducer in cancer

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Apolipoprotein E and Peptide Mimetics Modulate Inflammation by Binding the SET Protein and Activating Protein Phosphatase 2A

Christensen, D. J., Ohkubo, N., Oddo, J., Van Kanegan, M. J., Neil, J., Li, F., Colton, C. A., & Vitek, M. P. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002847 · Cited by 125 · see citing works

Akt Pathway Inhibitors

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Two hits are better than one: targeting both phosphatidylinositol 3-kinase and mammalian target of rapamycin as a therapeutic strategy for acute leukemia treatment

Martelli, A. M., Chiarini, F., Evangelisti, C., Cappellini, A., Buontempo, F., Bressanin, D., Fini, M., & McCubrey, J. A. (2012) · Oncotarget · doi:10.18632/oncotarget.477 · Cited by 120 · see citing works

Tumor Microenvironment Metabolism: A New Checkpoint for Anti-Tumor Immunity

Scharping, N. E., & Delgoffe, G. M. (2016) · Vaccines · doi:10.3390/vaccines4040046 · Cited by 119 · see citing works

B55β-Associated PP2A Complex Controls PDK1-Directed Myc Signaling and Modulates Rapamycin Sensitivity in Colorectal Cancer

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Intrapericardial Exosome Therapy Dampens Cardiac Injury via Activating Foxo3

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The role of PI3K/Akt in human herpesvirus infection: From the bench to the bedside

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Targeting Inhibitors of the Tumor Suppressor PP2A for the Treatment of Pancreatic Cancer

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Anesthesia Induces Phosphorylation of Tau

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Mitochondrial-Targeted Curcuminoids: A Strategy to Enhance Bioavailability and Anticancer Efficacy of Curcumin

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MicroRNA-587 antagonizes 5-FU-induced apoptosis and confers drug resistance by regulating PPP2R1B expression in colorectal cancer

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USP49 negatively regulates tumorigenesis and chemoresistance through FKBP51‐AKT signaling

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Molecular aspects of glucose homeostasis in skeletal muscle – A focus on the molecular mechanisms of insulin resistance

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Protein phosphatase-1 regulates Akt1 signal transduction pathway to control gene expression, cell survival and differentiation

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Tumor suppressive protein phosphatases in human cancer: Emerging targets for therapeutic intervention and tumor stratification

Meeusen, B., & Janssens, V. (2018) · The International Journal of Biochemistry &amp; Cell Biology · doi:10.1016/j.biocel.2017.10.002 · Cited by 96 · see citing works

Overexpression of PP2A inhibitor SET oncoprotein is associated with tumor progression and poor prognosis in human non-small cell lung cancer

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PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer

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The Role and Therapeutic Potential of Ser/Thr Phosphatase PP2A in Apoptotic Signalling Networks in Human Cancer Cells

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Imbalance of p75NTR/TrkB protein expression in Huntington’s disease: implication for neuroprotective therapies

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Low expression of PP2A regulatory subunit B55α is associated with T308 phosphorylation of AKT and shorter complete remission duration in acute myeloid leukemia patients

Ruvolo, P. P., Qui, Y. H., Coombes, K. R., Zhang, N., Ruvolo, V. R., Borthakur, G. M., Konopleva, M. Y., Andreeff, M., & Kornblau, S. M. (2011) · Leukemia · doi:10.1038/leu.2011.146 · Cited by 89 · see citing works

PTEN dephosphorylates AKT to prevent the expression of GLUT1 on plasmamembrane and to limit glucose consumption in cancer cells

Phadngam, S., Castiglioni, A., Ferraresi, A., Morani, F., Follo, C., & Isidoro, C. (2016) · Oncotarget · doi:10.18632/oncotarget.13113 · Cited by 86 · see citing works

Resistance of Akt kinases to dephosphorylation through ATP-dependent conformational plasticity

Chan, T. O., Zhang, J., Rodeck, U., Pascal, J. M., Armen, R. S., Spring, M., Dumitru, C. D., Myers, V. D., Li, X., Cheung, J. Y., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109879108 · Cited by 86 · see citing works

RhoB loss induces Rac1-dependent mesenchymal cell invasion in lung cells through PP2A inhibition

Bousquet, E., Calvayrac, O., Mazières, J., Lajoie‐Mazenc, I., Boubekeur, N., Favre, G., & Pradines, A. (2015) · Oncogene · doi:10.1038/onc.2015.240 · Cited by 85 · see citing works

MYC Acts via the PTEN Tumor Suppressor to Elicit Autoregulation and Genome-Wide Gene Repression by Activation of the Ezh2 Methyltransferase

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AKT Regulates NLRP3 Inflammasome Activation by Phosphorylating NLRP3 Serine 5

Zhao, W., Shi, C.-S., Harrison, K., Hwang, I., Nabar, N. R., Wang, M., & Kehrl, J. H. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000649 · Cited by 83 · see citing works

Adaptations in Hippo-Yap signaling and myofibroblast fate underlie scar-free ear appendage wound healing in spiny mice

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Discovery of Small Molecule Inhibitors of the PH Domain Leucine-Rich Repeat Protein Phosphatase (PHLPP) by Chemical and Virtual Screening

Sierecki, E., Sinko, W., McCammon, J. A., & Newton, A. C. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100331d · Cited by 81 · see citing works

The AMPK-PP2A axis in insect fat body is activated by 20-hydroxyecdysone to antagonize insulin/IGF signaling and restrict growth rate

Yuan, D., Zhou, S., Liu, S., Li, K., Zhao, H., Long, S., Liu, H., Xie, Y., Su, Y., Yu, F., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000963117 · Cited by 79 · see citing works

PP2A: The Wolf in Sheep’s Clothing?

Bailey‐Whyte, M., & Kiely, P. (2015) · Cancers · doi:10.3390/cancers7020648 · Cited by 78 · see citing works

Upregulation of miR-136 in human non-small cell lung cancer cells promotes Erk1/2 activation by targeting PPP2R2A

Shen, S., Yue, H., Li, Y., Qin, J., Li, K., Liu, Y., & Wang, J. (2013) · Tumor Biology · doi:10.1007/s13277-013-1087-2 · Cited by 77 · see citing works

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

Dopamine D2 receptor signalling controls inflammation in acute pancreatitis via a PP2A‐dependent Akt/NF‐κB signalling pathway

Han, X., Li, B., Ye, X., Mulatibieke, T., Wu, J., Dai, J., Wu, D., Ni, J., Zhang, R., Xue, J., et al. (2017) · British Journal of Pharmacology · doi:10.1111/bph.14057 · Cited by 77 · see citing works

Protein phosphatase 2A – structure, function and role in neurodevelopmental disorders

Sandal, P., Jong, C. J., Merrill, R. A., Song, J., & Strack, S. (2021) · Journal of Cell Science · doi:10.1242/jcs.248187 · Cited by 72 · see citing works

Loss of hepatic aldolase B activates Akt and promotes hepatocellular carcinogenesis by destabilizing the Aldob/Akt/PP2A protein complex

He, X., Li, M., Yu, H., Liu, G., Wang, N., Yin, C., Tu, Q., Narla, G., Tao, Y., Cheng, S., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000803 · Cited by 74 · see citing works

In vitro and in vivo anti-inflammatory effects of ethanol extract from Acer tegmentosum

Yu, T., Lee, J., Lee, Y. G., Byeon, S. E., Kim, M. H., Sohn, E., Lee, Y. J., Lee, S. G., & Cho, J. Y. (2010) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2009.12.042 · Cited by 74 · see citing works

An aPPARent functional consequence in skeletal muscle physiology via peroxisome proliferator-activated receptors

Phua, W. W. T., Wong, M. X. Y., Liao, Z., & Tan, N. S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051425 · Cited by 72 · see citing works

Bioinformatics-based analysis reveals elevated MFSD12 as a key promoter of cell proliferation and a potential therapeutic target in melanoma

Wei, C., Zhu, M.-X., Lu, N., Peng, R., Yang, X., Zhang, P.-F., Wang, L., & Gu, J. (2018) · Oncogene · doi:10.1038/s41388-018-0531-6 · Cited by 72 · see citing works

Reengineered tricyclic anti-cancer agents

Kastrinsky, D. B., Sangodkar, J., Zaware, N., Izadmehr, S., Dhawan, N. S., Narla, G., & Ohlmeyer, M. H. J. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.07.007 · Cited by 68 · see citing works

The ability of an ethanol extract of Cinnamomum cassia to inhibit Src and spleen tyrosine kinase activity contributes to its anti-inflammatory action

Yu, T., Lee, S., Yang, W. S., Jang, H., Lee, Y. J., Kim, T., Kim, S. Y., Lee, J., & Cho, J. Y. (2011) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2011.11.051 · Cited by 70 · see citing works

Ceramide Acyl Chain Length and Its Relevance to Intracellular Lipid Regulation

Ho, Q. W. C., Zheng, X., & Ali, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179697 · Cited by 68 · see citing works

AKT signaling in ERBB2-amplified breast cancer

Carmona, F. J., Montemurro, F., Kannan, S., Rossi, V., Verma, C. S., Baselga, J. M., & Scaltriti, M. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.11.013 · Cited by 68 · see citing works

Heparanase, cell signaling, and viral infections

Koganti, R., Suryawanshi, R., & Shukla, D. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03559-y · Cited by 67 · see citing works

PP2A-Mediated Regulation of Ras Signaling in G2 Is Essential for Stable Quiescence and Normal G1 Length

Naetar, N., Soundarapandian, V., Litovchick, L., Goguen, K. L., Sablina, A. A., Bowman-Colin, C., Siciński, P., Hahn, W. C., DeCaprio, J. A., & Livingston, D. M. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.04.023 · Cited by 67 · see citing works

Essential role of PH domain and leucine-rich repeat protein phosphatase 2 in Nrf2 suppression via modulation of Akt/GSK3β/Fyn kinase axis during oxidative hepatocellular toxicity

Rizvi, F., Shukla, S., & Kakkar, P. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.118 · Cited by 67 · 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

PR55α subunit of protein phosphatase 2A supports the tumorigenic and metastatic potential of pancreatic cancer cells by sustaining hyperactive oncogenic signaling

Hein, A. L., Seshacharyulu, P., Rachagani, S., Sheinin, Y. M., Ouellette, M. M., Ponnusamy, M. P., Mumby, M. C., Batra, S. K., & Yan, Y. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2119 · Cited by 66 · see citing works

AMBRA1 Controls Regulatory T-Cell Differentiation and Homeostasis Upstream of the FOXO3-FOXP3 Axis

Becher, J., Simula, L., Volpe, E., Procaccini, C., Rocca, C. L., D’Acunzo, P., Cianfanelli, V., Strappazzon, F., Caruana, I., Nazio, F., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.11.010 · Cited by 66 · see citing works

GAPDH binds to active Akt, leading to Bcl-xL increase and escape from caspase-independent cell death

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Restricted Protein Phosphatase 2A Targeting by Merkel Cell Polyomavirus Small T Antigen

Kwun, H. J., Shuda, M., Camacho, C. J., Gamper, A. M., Thant, M., Chang, Y., & Moore, P. S. (2015) · Journal of Virology · doi:10.1128/jvi.00157-15 · Cited by 66 · see citing works

Evaluation of PPP2R2A as a prostate cancer susceptibility gene: A comprehensive germline and somatic study

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Combination treatment with triptolide and hydroxycamptothecin synergistically enhances apoptosis in A549 lung adenocarcinoma cells through PP2A-regulated ERK, p38 MAPKs and Akt signaling pathways

Meng, G., Wang, W., Chai, K., YANG, S., Li, F., & JIANG, K. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.2814 · Cited by 62 · see citing works

PME-1 Modulates Protein Phosphatase 2A Activity to Promote the Malignant Phenotype of Endometrial Cancer Cells

Wandzioch, E., Pusey, M., Werda, A., Bail, S., Bhaskar, A., Nestor, M., Yang, J., & Rice, L. M. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-3130 · Cited by 62 · see citing works

KIBRA Protein Phosphorylation Is Regulated by Mitotic Kinase Aurora and Protein Phosphatase 1

Xiao, L., Chen, Y., Ji, M. H., Volle, D. J., Lewis, R. E., Tsai, M.-Y., & Dong, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.246850 · Cited by 61 · see citing works

Downregulation of MicroRNA miR-520h by E1A Contributes to Anticancer Activity

Su, J.-L., Chen, P. B., Chen, Y.-H., Chen, S., Chang, Y.-W., Jan, Y., Cheng, X., Hsiao, M., & Hung, M. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4148 · Cited by 60 · see citing works

Circumventing cellular control of PP2A by methylation promotes transformation in an Akt-dependent manner

Jackson, J. B., & Pallas, D. C. (2012) · Neoplasia · doi:10.1593/neo.12768 · Cited by 60 · see citing works

Greatwall promotes cell transformation by hyperactivating AKT in human malignancies

Vera, J., Lartigue, L., Vigneron, S., Gadéa, G., Gire, V., Rio, M. D., Soubeyran, I., Chibon, F., Lorca, T., & Castro, A. (2015) · eLife · doi:10.7554/elife.10115 · Cited by 56 · see citing works

Overexpressed CISD2 has prognostic value in human gastric cancer and promotes gastric cancer cell proliferation and tumorigenesis via AKT signaling pathway

Wang, L., Ouyang, F., Liu, X., Wu, S., Wu, H., Xu, Y., Wang, B., Zhu, J., Xu, X., & Zhang, L. (2015) · Oncotarget · doi:10.18632/oncotarget.6302 · Cited by 58 · see citing works

Innate Immune Signaling in Drosophila Blocks Insulin Signaling by Uncoupling PI(3,4,5)P3 Production and Akt Activation

Roth, S. W., Bitterman, M. D., Birnbaum, M. J., & Bland, M. L. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.033 · Cited by 58 · see citing works

EZH2-mediated PP2A inactivation confers resistance to HER2-targeted breast cancer therapy

Bao, Y., Oguz, G., Lee, W. C., Lee, P. L., Ghosh, K., Li, J., Wang, P., Lobie, P. E., Ehmsen, S., Ditzel, H. J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19704-x · Cited by 56 · see citing works

SET protein accumulates in HNSCC and contributes to cell survival: Antioxidant defense, Akt phosphorylation and AVOs acidification

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Free Fatty Acid-Induced PP2A Hyperactivity Selectively Impairs Hepatic Insulin Action on Glucose Metabolism

Galbo, T., Olsen, G. S., Quistorff, B., & Nishimura, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027424 · Cited by 56 · see citing works

Adipose tissue insulin resistance due to loss of PI3K p110α leads to decreased energy expenditure and obesity

Nelson, V. L., Jiang, Y., Dickman, K. G., Ballou, L. M., & Lin, R. Z. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00625.2013 · Cited by 56 · see citing works

A Novel Epac-Rap-PP2A Signaling Module Controls cAMP-dependent Akt Regulation

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Neuropilin-1 expression promotes invasiveness of melanoma cells through vascular endothelial growth factor receptor-2-dependent and -independent mechanisms

Ruffini, F., D’Atri, S., & Lacal, P. M. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1948 · Cited by 55 · see citing works

STRIPAK directs PP2A activity toward MAP4K4 to promote oncogenic transformation of human cells

Kim, J. W., Berrios, C. J., Kim, M., Schade, A. E., Adelmant, G., Yeerna, H., Damato, E., Iniguez, A. B., Swanson, S. K., Florens, L. A., et al. (2020) · eLife · doi:10.7554/elife.53003 · Cited by 54 · see citing works

PHLPP1 Gene Deletion Protects the Brain from Ischemic Injury

Chen, B., Winkle, J. A. V., Lyden, P. D., Brown, J. H., & Purcell, N. H. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.150 · Cited by 54 · see citing works

Growth hormone modulation of EGF-induced PI3K-Akt pathway in mice liver

Díaz, M. E., González, L., Miquet, J. G., Martinez, C. S., Sotelo, A. I., Bartke, A., & Turyn, D. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.10.001 · Cited by 54 · see citing works

Redox inhibition of protein phosphatase PP2A: Potential implications in oncogenesis and its progression

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Long noncoding RNA GMAN promotes hepatocellular carcinoma progression by interacting with eIF4B

Xu, J., Lu, Y., Liu, Q., Xia, A., Zhao, J., Xu, X., Sun, Q., Qi, F., & Sun, B. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.12.032 · Cited by 51 · see citing works

miR-19a-mediated downregulation of RhoB inhibits the dephosphorylation of AKT1 and induces osteosarcoma cell metastasis

Zou, Q., Xiao, X., Liang, Y. J., Peng, L., Guo, Z., Li, W., & Yu, W. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.04.027 · Cited by 47 · see citing works

InterAKTions with FKBPs - Mutational and Pharmacological Exploration

Fabian, A., März, A., Neimanis, S., Biondi, R. M., Kozany, C., & Hausch, F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057508 · Cited by 49 · see citing works

Suppression of PI3K/Akt/mTOR/c-Myc/mtp53 Positive Feedback Loop Induces Cell Cycle Arrest by Dual PI3K/mTOR Inhibitor PQR309 in Endometrial Cancer Cell Lines

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Aspirin sensitivity of PIK3CA-mutated Colorectal Cancer: potential mechanisms revisited

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Dual Function of Protein Kinase C (PKC) in 12-O-Tetradecanoylphorbol-13-acetate (TPA)-induced Manganese Superoxide Dismutase (MnSOD) Expression

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NFluc-FHA2-Aktpep-CFluc

Zhang, H. (2008) · Europe PMC (PubMed Central)

Distinct Protein Phosphatase 2A Heterotrimers Modulate Growth Factor Signaling to Extracellular Signal-regulated Kinases and Akt

Kanegan, M. J. V., Adams, D. G., Wadzinski, B. E., & Strack, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506986200 · Cited by 132 · see citing works

Clk2 and B56β mediate insulin-regulated assembly of the PP2A phosphatase holoenzyme complex on Akt

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Positive regulation of Raf1-MEK1/2-ERK1/2 signaling by protein serine/threonine phosphatase 2A holoenzymes

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Physiological regulation of Akt activity and stability.

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