PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)

Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

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A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells

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CIP2A inhibits PP2A in human malignancies

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Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation

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The tumor suppressor PP2A is functionally inactivated in blast crisis CML through the inhibitory activity of the BCR/ABL-regulated SET protein

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Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme

Cho, U. S., & Xu, W. (2007) · Nature · doi:10.1038/nature05351 · Cited by 459 · see citing works

Structure of the Protein Phosphatase 2A Holoenzyme

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The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs

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PP2A: the expected tumor suppressor

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Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast

Jiang, Y., & Broach, J. (1999) · EMBO Journal · doi:10.1093/emboj/18.10.2782 · Cited by 363 · see citing works

Molecular mechanisms of theprotein serine/threonine phosphatases

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Multiple pathways regulated by the tumor suppressor PP2A in transformation

Westermarck, J., & Hahn, W. C. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.02.001 · Cited by 344 · see citing works

Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins

Xing, Y., Xu, Y., Chen, Y., Jeffrey, P. D., Chao, Y., Lin, Z., Li, Z., Strack, S., Stock, J. B., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.09.025 · Cited by 334 · see citing works

Protein phosphatase 2A: the Trojan Horse of cellular signaling

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Identification of specific PP2A complexes involved in human cell transformation

Chen, W., Possemato, R., Campbell, K. T., Plattner, C. A., Pallas, D. C., & Hahn, W. C. (2004) · Cancer Cell · doi:10.1016/s1535-6108(04)00026-1 · Cited by 325 · see citing works

Protein phosphatase 2A positively regulates Ras signaling by dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites

Ory, S., Zhou, M., Conrads, T. P., Veenstra, T. D., & Morrison, D. K. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00535-9 · Cited by 296 · see citing works

Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits

Silverstein, A. M., Barrow, C. A., Davis, A. J., & Mumby, M. C. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072071699 · Cited by 276 · see citing works

Involvement of PP2A in viral and cellular transformation

Arroyo, J. D., & Hahn, W. C. (2005) · Oncogene · doi:10.1038/sj.onc.1209038 · Cited by 237 · see citing works

Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits

Tolstykh, T., Lee, J., Vafai, S. B., & Stock, J. B. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5682 · Cited by 233 · see citing works

Protein phosphatase 2A methyltransferase links homocysteine metabolism with tau and amyloid precursor protein regulation

Sontag, E., Nunbhakdi-Craig, V., Sontag, J.-M., Diaz-Arrastia, R., Ogris, E., Dayal, S., Lentz, S. R., Arning, E., & Bottiglieri, T. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3316-06.2007 · Cited by 225 · see citing works

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

Letourneux, C., Rocher, G., & Porteu, F. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600980 · Cited by 224 · see citing works

Cyclin G Recruits PP2A to Dephosphorylate Mdm2

Okamoto, K., Li, H., Jensen, M. R., Zhang, T., Taya, Y., Thorgeirsson, S. S., & Prives, C. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00504-x · Cited by 215 · see citing works

Cyclin G2 Associates with Protein Phosphatase 2A Catalytic and Regulatory B′ Subunits in Active Complexes and Induces Nuclear Aberrations and a G1/S Phase Cell Cycle Arrest

Bennin, D. A., Don, A. S. A., Brake, T., McKenzie, J. L., Rosenbaum, H., Ortiz, L., DePaoli-Roach, A. A., & Horne, M. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111693200 · Cited by 210 · see citing works

The Tumor Suppressor PP2A Aβ Regulates the RalA GTPase

Sablina, A. A., Chen, W., Arroyo, J. D., Corral, L. G., Hector-Greene, M., Bulmer, S. E., DeCaprio, J. A., & Hahn, W. C. (2007) · Cell · doi:10.1016/j.cell.2007.03.047 · Cited by 203 · see citing works

WD40 Repeat Proteins Striatin and S/G2 Nuclear Autoantigen Are Members of a Novel Family of Calmodulin-binding Proteins That Associate with Protein Phosphatase 2A

Moreno, C. S., Park, S., Nelson, K., Ashby, D., Hubalek, F., Lane, W. S., & Pallas, D. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5257 · Cited by 194 · see citing works

Downregulation of Protein Phosphatase 2A Carboxyl Methylation and Methyltransferase May Contribute to Alzheimer Disease Pathogenesis

Sontag, E., Hladik, C. L., Montgomery, L. G., Luangpirom, A., Mudrak, I., Ogris, E., & White, C. L. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.10.1080 · Cited by 191 · see citing works

A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A

Ogris, E., Du, X., Nelson, K. C., Mak, E. K., Yu, X. X., Lane, W. S., & Pallas, D. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.14382 · Cited by 191 · see citing works

Role for the PP2A/B56δ Phosphatase in Regulating 14-3-3 Release from Cdc25 to Control Mitosis

Margolis, S. S., Perry, J. A., Forester, C. M., Nutt, L. K., Guo, Y., Jardim, M. J., Thomenius, M. J., Freel, C. D., Darbandi, R., Ahn, J., et al. (2006) · Cell · doi:10.1016/j.cell.2006.10.035 · Cited by 187 · see citing works

Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo

Wu, J., Tolstykh, T., Lee, J., Boyd, K., Stock, J. B., & Broach, J. R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5672 · Cited by 186 · see citing works

Selection of protein phosphatase 2A regulatory subunits is mediated by the C terminus of the catalytic Subunit

Longin, S., Zwaenepoel, K., Louis, J. V., Dilworth, S., Goris, J., & Janssens, V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704059200 · Cited by 184 · see citing works

Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory A subunit: abundant expression of both forms in cells

Kremmer, E., Ohst, K., Kiefer, J., Brewis, N., & Walter, G. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.3.1692 · Cited by 175 · see citing works

Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Bα subunit

BRYANT, J. C., Westphal, R. S., & Wadzinski, B. E. (1999) · Biochemical Journal · doi:10.1042/bj3390241 · Cited by 173 · see citing works

Dynamic nucleosomes and gene transcription

Mellor, J. (2006) · Trends in Genetics · doi:10.1016/j.tig.2006.03.008 · Cited by 168 · see citing works

Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A.

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Critical Role for Protein Phosphatase 2A Heterotrimers in Mammalian Cell Survival*

Strack, S., Cribbs, J., & Gomez, L. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408015200 · Cited by 160 · see citing works

Methylation of the Protein Phosphatase 2A Catalytic Subunit Is Essential for Association of Bα Regulatory Subunit But Not SG2NA, Striatin, or Polyomavirus Middle Tumor Antigen

Yu, X. X., Du, X., Moreno, C. S., Green, R. E., Ogris, E., Feng, Q., Chou, L., McQuoid, M. J., & Pallas, D. C. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.1.185 · Cited by 160 · see citing works

Disruption of protein phosphatase 2A subunit interaction in human cancers with mutations in the Aα subunit gene

Ruediger, R., Pham, H. T., & Walter, G. (2001) · Oncogene · doi:10.1038/sj.onc.1204059 · Cited by 149 · see citing works

Purification of Porcine Brain Protein Phosphatase 2A Leucine Carboxyl Methyltransferase and Cloning of the Human Homologue,

BAERE, I. D., Derua, R., Janssens, V., Hoof, C. A. V., Waelkens, E., Merlevede, W. J., & Goris, J. (1999) · Biochemistry · doi:10.1021/bi991646a · Cited by 145 · see citing works

B56-Associated Protein Phosphatase 2A Is Required For Survival and Protects from Apoptosis in Drosophila melanogaster

Li, X., Scuderi, A., Letsou, A., & Virshup, D. M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3674-3684.2002 · Cited by 135 · see citing works

Protein phosphatase 2A subunit assembly: The catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen

Ogris, E., Gibson, D. M., & Pallas, D. C. (1997) · Oncogene · doi:10.1038/sj.onc.1201259 · Cited by 134 · see citing works

Carboxymethylation of the PP2A Catalytic Subunit in Saccharomyces cerevisiae Is Required for Efficient Interaction with the B-type Subunits Cdc55p and Rts1p

Wei, H., Ashby, D. G., Moreno, C. S., Ogris, E., Yeong, F. M., Corbett, A. H., & Pallas, D. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008694200 · Cited by 128 · see citing works

Alterations in protein phosphatase 2A subunit interaction in human carcinomas of the lung and colon with mutations in the Aβ subunit gene

Ruediger, R., Pham, H. T., & Walter, G. (2001) · Oncogene · doi:10.1038/sj.onc.1204279 · Cited by 125 · see citing works

Structural Basis of PP2A Inhibition by Small t Antigen

Cho, U., Morrone, S. R., Sablina, A. A., Arroyo, J. D., Hahn, W. C., & Xu, W. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050202 · Cited by 124 · see citing works

Drosophila mutants in the 55 kDa regulatory subunit of protein phosphatase 2A show strongly reduced ability to dephosphorylate substrates of p34cdc2

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A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivoPreprint

Fellner, T., Lackner, D. H., Hombauer, H., Piribauer, P., Mudrak, I., Zaragoza, K., Juno, C., & Ogris, E. (2003) · Genes & Development · doi:10.1101/gad.259903 · Cited by 105 · see citing works

Specificity of the polycation‐stimulated (type‐2A) and ATP, Mg‐dependent (type‐1) protein phosphatases toward substrates phosphorylated by P34cdc2 kinase

Agostinis, P., Derua, R., Sarno, S., Goris, J., & Merlevede, W. J. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16774.x · Cited by 105 · see citing works

The Protein Phosphatase 2A Phosphatase Activator Is a Novel Peptidyl-Prolyl cis/trans-Isomerase

Jordens, J., Janssens, V., Longin, S., Stevens, I., Martens, E., Bultynck, G., Engelborghs, Y., Lescrinier, E., Waelkens, E., Goris, J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507760200 · Cited by 105 · see citing works

The B″/PR72 subunit mediates Ca 2+ -dependent dephosphorylation of DARPP-32 by protein phosphatase 2A

Ahn, J., Sung, J. Y., McAvoy, T., Nishi, A., Janssens, V., Goris, J., Greengard, P., & Nairn, A. C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703589104 · Cited by 102 · see citing works

An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator

Longin, S., Jordens, J., MARTENS, E., Stevens, I., Janssens, V., Rondelez, E., BAERE, I. D., Derua, R., Waelkens, E., Goris, J., et al. (2004) · Biochemical Journal · doi:10.1042/bj20031643 · Cited by 101 · see citing works

Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: Differences in expression, subunit interaction, and evolution

ZHOU, J., PHAM, H. T., RUEDIGER, R., & WALTER, G. (2003) · Biochemical Journal · doi:10.1042/bj20021244 · Cited by 95 · see citing works

Mutation of Tyr307 and Leu309 in the Protein Phosphatase 2A Catalytic Subunit Favors Association with the α4 Subunit Which Promotes Dephosphorylation of Elongation Factor-2

Chung, H., Nairn, A. C., Murata, K., & Brautigan, D. L. (1999) · Biochemistry · doi:10.1021/bi990902g · Cited by 90 · see citing works

Identification and functional analysis of two Ca2+-binding EF-hand motifs in the B″/PR72 subunit of protein phosphatase 2A

Janssens, V., Jordens, J., Stevens, I., Van Hoof, C., Martens, E., De Smedt, H., Engelborghs, Y., Waelkens, E., & Goris, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211717200 · Cited by 89 · see citing works

Generation of Active Protein Phosphatase 2A Is Coupled to Holoenzyme Assembly

Hombauer, H., Weismann, D., Mudrak, I., Stanzel, C., Fellner, T., Lackner, D. H., & Ogris, E. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050155 · Cited by 88 · see citing works

Structure of Protein Phosphatase Methyltransferase 1 (PPM1), a Leucine Carboxyl Methyltransferase Involved in the Regulation of Protein Phosphatase 2A Activity

Leulliot, N., Quevillon‐Chéruel, S., Sorel, I., de la Sierra-Gallay, I. L., Collinet, B., Graille, M., Blondeau, K., Bettache, N., Anne Poupon, B., Janin, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311484200 · Cited by 86 · see citing works

Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40

Chen, Y., Xu, Y., Bao, Q., Xing, Y., Li, Z., Lin, Z., Stock, J. B., Jeffrey, P. D., & Shi, Y. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1254 · Cited by 84 · see citing works

Protein Phosphatase 2A Holoenzyme Assembly

Strack, S., Ruediger, R., Walter, G., Dagda, R. K., Barwacz, C. A., & Cribbs, J. T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202992200 · Cited by 83 · see citing works

Two conserved domains in regulatory B subunits mediate binding to the A subunit of protein phosphatase 2A

Li, X., & Virshup, D. M. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02680.x · Cited by 83 · see citing works

Identification of a PP2A-interacting protein that functions as a negative regulator of phosphatase activity in the ATM/ATR signaling pathway

McConnell, J. L., Gomez, R. J., McCorvey, L. R. A., Law, B. K., & Wadzinski, B. E. (2007) · Oncogene · doi:10.1038/sj.onc.1210406 · Cited by 80 · see citing works

Localization ofSaccharomyces cerevisiaeProtein Phosphatase 2A Subunits throughout Mitotic Cell Cycle

Gentry, M. S., & Hallberg, R. L. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.02-05-0065 · Cited by 79 · see citing works

Expression of protein phosphatase 2A mutants and silencing of the regulatory Bα subunit induce a selective loss of acetylated and detyrosinated microtubules

Nunbhakdi‐Craig, V., Schüchner, S., Sontag, J., Montgomery, L. G., Pallas, D. C., Juno, C., Mudrak, I., Ogris, E., & Sontag, E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04503.x · Cited by 72 · see citing works

Spatial control of protein phosphatase 2A (de)methylation

Longin, S., Zwaenepoel, K., Martens, E., Louis, J. V., Rondelez, E., Goris, J., & Janssens, V. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.07.030 · Cited by 58 · see citing works

Genomic organisation, chromosomal localisation tissue distribution and developmental regulation of the PR61/B′ regulatory subunits of protein phosphatase 2A in mice

Martens, E., Stevens, I., Janssens, V., Vermeesch, J., Götz, J., Goris, J., & Van Hoof, C. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.12.047 · Cited by 57 · see citing works

Crystal Structure of the PP2A Phosphatase Activator: Implications for Its PP2A-Specific PPIase Activity

Leulliot, N., Vicentini, G., Jordens, J., Quevillon‐Chéruel, S., Schiltz, M., Barford, D., TILBEURGH, H. V., & Goris, J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.008 · Cited by 49 · see citing works

Binding Specificity of Protein Phosphatase 2A Core Enzyme for Regulatory B Subunits and T Antigens

Ruediger, R., Fields, K., & Walter, G. (1999) · Journal of Virology · doi:10.1128/jvi.73.1.839-842.1999 · Cited by 48 · see citing works

Mutation of the C-terminal leucine residue of PP2Ac inhibits PR55/B subunit binding and confers supersensitivity to microtubule destabilization in Saccharomyces cerevisiae

Evans, D. R., & Hemmings, B. A. (2000) · Molecular Genetics and Genomics · doi:10.1007/s004380000302 · Cited by 47 · see citing works

A Novel Assay for Protein Phosphatase 2A (PP2A) Complexes In Vivo Reveals Differential Effects of Covalent Modifications on Different Saccharomyces cerevisiae PP2A Heterotrimers

Gentry, M. S., Li, Y., Wei, H., Syed, F. F., Patel, S. H., Hallberg, R. L., & Pallas, D. C. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.6.1029-1040.2005 · Cited by 45 · see citing works

ATM-dependent Dissociation of B55 Regulatory Subunit from Nuclear PP2A in Response to Ionizing Radiation

Guo, C. Y., Brautigan, D. L., & Larner, J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110092200 · Cited by 43 · see citing works

The Structure of Tap42/α4 Reveals a Tetratricopeptide Repeat-like Fold and Provides Insights into PP2A Regulation,

Yang, J., Roe, S. M., Prickett, T. D., Brautigan, D. L., & Barford, D. (2007) · Biochemistry · doi:10.1021/bi7007118 · Cited by 37 · see citing works

MCM3-binding GANP DNA-primase is associated with a novel phosphatase component G5PR

Kono, Y., Maeda, K., Kuwahara, K., Yamamoto, H., Miyamoto, E., Yonezawa, K., Takagi, K., & Sakaguchi, N. (2002) · Genes to Cells · doi:10.1046/j.1365-2443.2002.00562.x · Cited by 35 · see citing works

Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B)

Ikehara, T., Ikehara, S., Imamura, S., Shinjo, F., & Yasumoto, T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.01.085 · Cited by 33 · see citing works

The Formation and Activity of PP2A Holoenzymes Do Not Depend on the Isoform of the Catalytic Subunit

Zhou, J., Pham, H. T., & Walter, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211181200 · Cited by 29 · see citing works

The Scaffolding A/Tpd3 Subunit and High Phosphatase Activity Are Dispensable for Cdc55 Function in the Saccharomyces cerevisiae Spindle Checkpoint and in Cytokinesis

Koren, R. N., Rainis, L., & Kleinberger, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409359200 · Cited by 28 · see citing works

Identification and characterization of B′′‐subunits of protein phosphatase 2 A in Xenopus laevis oocytes and adult tissues

Stevens, I., Janssens, V., Martens, E., Dilworth, S., Goris, J., & HOOF, C. V. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03398.x · Cited by 22 · see citing works

Domains Necessary for Gα12 Binding and Stimulation of Protein Phosphatase-2A (PP2A): Is Gα12 a Novel Regulatory Subunit of PP2A?

Zhu, D., Tate, R. I., Ruediger, R., Meigs, T. E., & Denker, B. M. (2007) · Molecular Pharmacology · doi:10.1124/mol.106.033555 · Cited by 22 · see citing works

11 Reversible methylation of protein phosphatase 2A

Longin, S., & Goris, J. (2006) · The Enzymes · doi:10.1016/s1874-6047(06)80013-2 · Cited by 8 · see citing works

Serine/threonine phosphatases: mechanism through structure

Shi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.10.006 · Cited by 1,488 · see citing works

Wnt/β-catenin signaling in cancers and targeted therapies

Yu, F., Yu, C., Li, F., Zuo, Y., Wang, Y., Yao, L., Wu, C., Wang, C., & Ye, L. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00701-5 · Cited by 734 · see citing works

From Promiscuity to Precision: Protein Phosphatases Get a Makeover

Virshup, D. M., & Shenolikar, S. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.015 · Cited by 643 · see citing works

Brassinosteroid Signal Transduction: From Receptor Kinase Activation to Transcriptional Networks Regulating Plant Development

Clouse, S. D. (2011) · The Plant Cell · doi:10.1105/tpc.111.084475 · Cited by 573 · see citing works

The extended PP1 toolkit: designed to create specificity

Bollen, M., Peti, W., Ragusa, M. J., & Beullens, M. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.03.002 · Cited by 503 · see citing works

PP2A activates brassinosteroid-responsive gene expression and plant growth by dephosphorylating BZR1

Tang, W., Yuan, M., Wang, R., Yang, Y., Wang, C., Osés-Prieto, J. A., Kim, T., Zhou, H., Deng, Z., Gampala, S. S. L., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2151 · Cited by 499 · see citing works

Protein phosphatase 2A: a target for anticancer therapy

Perrotti, D., & Neviani, P. (2013) · The Lancet Oncology · doi:10.1016/s1470-2045(12)70558-2 · Cited by 400 · see citing works

PP2A as a master regulator of the cell cycle

Wlodarchak, N., & Xing, Y. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2016.1143913 · Cited by 366 · see citing works

Physiological regulation of Akt activity and stability.

Liao, Y., & Hung, M. (2010) · PubMed Central · Cited by 343 · see citing works

Multiple pathways regulated by the tumor suppressor PP2A in transformation

Westermarck, J., & Hahn, W. C. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.02.001 · Cited by 344 · see citing works

Live-cell imaging RNAi screen identifies PP2A–B55α and importin-β1 as key mitotic exit regulators in human cells

Schmitz, M. H. A., Held, M., Janssens, V., Hutchins, J. R. A., Hudecz, O., Ivanova, E., Goris, J., Trinkle‐Mulcahy, L., Lamond, A. I., Poser, I., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2092 · Cited by 316 · see citing works

All roads lead to <scp>PP</scp>2A: exploiting the therapeutic potential of this phosphatase

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Protein phosphatase 2A dysfunction in Alzheimer’s disease

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Phosphatases: providing safe passage through mitotic exit

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Protein Kinases and Phosphatases in the Control of Cell Fate

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Regulated activity of PP2A–B55δ is crucial for controlling entry into and exit from mitosis in Xenopus egg extracts

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Host Cell Subversion by Toxoplasma GRA16, an Exported Dense Granule Protein that Targets the Host Cell Nucleus and Alters Gene Expression

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Evolution of protein phosphatases in plants and animals

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Tau protein phosphatases in Alzheimer's disease: The leading role of PP2A

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Regulation of autophagy by coordinated action of mTORC1 and protein phosphatase 2A

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Phosphatase PP2A is requisite for the function of regulatory T cells

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The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity

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PKA/AKAP1 and PP2A/Bβ2 Regulate Neuronal Morphogenesis via Drp1 Phosphorylation and Mitochondrial Bioenergetics

Dickey, A. S., & Strack, S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3159-11.2011 · Cited by 197 · see citing works

Brassinosteroids

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Protein Serine/Threonine Phosphatases: Keys to Unlocking Regulators and Substrates

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The M Phase Kinase Greatwall (Gwl) Promotes Inactivation of PP2A/B55δ, a Phosphatase Directed Against CDK Phosphosites

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A PP1-PP2A phosphatase relay controls mitotic progression

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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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Negative control of BAK1 by protein phosphatase 2A during plant innate immunity

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

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Regulation and Function of Protein Kinases and Phosphatases

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A protein phosphatase 2A complex spatially controls plant cell division

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HEAT repeats – versatile arrays of amphiphilic helices working in crowded environments?

Yoshimura, S. H., & Hirano, T. (2016) · Journal of Cell Science · doi:10.1242/jcs.185710 · Cited by 157 · see citing works

Arctigenin attenuates diabetic kidney disease through the activation of PP2A in podocytes

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Sodium selenate reduces hyperphosphorylated tau and improves outcomes after traumatic brain injury

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Protein Phosphatase 6 Interacts with the DNA-Dependent Protein Kinase Catalytic Subunit and Dephosphorylates γ-H2AX

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A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination

Lee, D.-H., Pan, Y., Kanner, S., Sung, P., Borowiec, J. A., & Chowdhury, D. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1769 · Cited by 157 · see citing works

A Ras Signaling Complex Controls the RasC-TORC2 Pathway and Directed Cell Migration

Charest, P. G., Shen, Z., Lakoduk, A. M., Sasaki, A. T., Briggs, S. P., & Firtel, R. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.03.017 · Cited by 152 · 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

Methylation of a Phosphatase Specifies Dephosphorylation and Degradation of Activated Brassinosteroid Receptors

Wu, G., Wang, X., Li, X., Kamiya, Y., Otegui, M. S., & Chory, J. (2011) · Science Signaling · doi:10.1126/scisignal.2001258 · Cited by 142 · see citing works

Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases

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PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysis

Grinthal, A., Adamovic, I., Weiner, B. M., Karplus, M., & Kleckner, N. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914073107 · Cited by 139 · see citing works

Recent Advances in the Regulation of Brassinosteroid Signaling and Biosynthesis PathwaysF

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Essential Requirement for PP2A Inhibition by the Oncogenic Receptor c-KIT Suggests PP2A Reactivation as a Strategy to Treat c-KIT+ Cancers

Roberts, K. G., Smith, A. M., McDougall, F. K., Carpenter, H., Horan, M. P., Neviani, P., Powell, J. A., Thomas, D., Guthridge, M. A., Perrotti, D., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2544 · Cited by 134 · see citing works

Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation

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GBA deficiency promotes SNCA/α-synuclein accumulation through autophagic inhibition by inactivated PPP2A

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Mitotic phosphatases: from entry guards to exit guides

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Sodium selenate retards epileptogenesis in acquired epilepsy models reversing changes in protein phosphatase 2A and hyperphosphorylated tau.

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Physiologic functions of PP2A: Lessons from genetically modified mice

Reynhout, S., & Janssens, V. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.07.010 · Cited by 124 · see citing works

Recurrent <i>PPP2R1A</i> Mutations in Uterine Cancer Act through a Dominant-Negative Mechanism to Promote Malignant Cell Growth

Haesen, D., Abbasi Asbagh, L., Derua, R., Hubert, A., Schrauwen, S., Hoorne, Y., Amant, F., Waelkens, E., Sablina, A., & Janssens, V. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-3342 · Cited by 124 · see citing works

Gene-function studies in systemic lupus erythematosus

Crispín, J. C., Hedrich, C. M., & Tsokos, G. C. (2013) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2013.78 · Cited by 124 · see citing works

EphB3 suppresses non-small-cell lung cancer metastasis via a PP2A/RACK1/Akt signalling complex

Guo, L., Ji, X., Gao, H., Zhao, J., Xu, J., Sun, Z.-J., Deng, Y., Shi, S., Feng, Y., Zhu, Y.-Q., et al. (2012) · Nature Communications · doi:10.1038/ncomms1675 · Cited by 116 · see citing works

DARPP-32, Jack of All Trades? Master of Which?

Yger, M., & Girault, J. (2011) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2011.00056 · Cited by 115 · see citing works

Merkel Cell Polyomavirus and Merkel Cell Carcinoma

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Regulation of chromosome segregation in oocytes and the cellular basis for female meiotic errors

Greaney, J., Wei, Z., & Homer, H. A. (2017) · Human Reproduction Update · doi:10.1093/humupd/dmx035 · Cited by 111 · see citing works

Mice lacking phosphatase PP2A subunit PR61/B’δ ( <i>Ppp2r5d</i> ) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3β

Louis, J. V., Martens, E., Borghgraef, P., Lambrecht, C., Sents, W., Longin, S., Zwaenepoel, K., Pijnenborg, R., Landrieu, I., Lippens, G., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018777108 · Cited by 112 · see citing works

One-Carbon Metabolism: Pulling the Strings behind Aging and Neurodegeneration

Lionaki, E., Ploumi, C., & Tavernarakis, N. (2022) · Cells · doi:10.3390/cells11020214 · Cited by 110 · see citing works

PR55α, a Regulatory Subunit of PP2A, Specifically Regulates PP2A-mediated β-Catenin Dephosphorylation

Zhang, W., Yang, J., Liu, Y., Chen, X., Yu, T., Jia, J., & Liu, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.013698 · Cited by 110 · see citing works

Dephosphorylation of Cdc20 is required for its C‐box‐dependent activation of the APC/C

Labit, H., Fujimitsu, K., Bayin, N. S., Takaki, T., Gannon, J., & Yamano, H. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.168 · Cited by 109 · see citing works

Greatwall-phosphorylated Endosulfine is both an inhibitor and a substrate of PP2A-B55 heterotrimers

Williams, B. C., Filter, J. J., Blake-Hodek, K. A., Wadzinski, B. E., Fuda, N. J., Shalloway, D. I., & Goldberg, M. L. (2014) · eLife · doi:10.7554/elife.01695 · Cited by 107 · see citing works

PP1 and PP2A phosphatases – cooperating partners in modulating retinoblastoma protein activation

KOLUPAEVA, V. G., & Janssens, V. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08511.x · Cited by 107 · see citing works

Protein phosphatase 2A as a therapeutic target in inflammation and neurodegeneration

Clark, A. R., & Ohlmeyer, M. H. J. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.05.016 · Cited by 106 · see citing works

Cell Cycle and DNA Repair Regulation in the Damage Response: Protein Phosphatases Take Over the Reins

Campos, A., & Clemente‐Blanco, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020446 · Cited by 106 · see citing works

Crosstalk of the EphA2 receptor with a serine/threonine phosphatase suppresses the Akt-mTORC1 pathway in cancer cells

Yang, N.-Y., Fernandez, C., Richter, M., Xiao, Z., Valencia, F., Tice, D. A., & Pasquale, E. B. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.09.004 · Cited by 105 · see citing works

Inhibition of Protein Phosphatase 2A Radiosensitizes Pancreatic Cancers by Modulating CDC25C/CDK1 and Homologous Recombination Repair

Wei, D., Parsels, L. A., Karnak, D. M., Davis, M. A., Parsels, J. D., Marsh, A. C., Zhao, L., Maybaum, J., Lawrence, T. S., Sun, Y., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0788 · Cited by 100 · see citing works

Human cancer-associated mutations in the Aα subunit of protein phosphatase 2A increase lung cancer incidence in Aα knock-in and knockout mice

Ruediger, R., Ruiz, J., & Walter, G. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05744-11 · Cited by 98 · see citing works

FTY720 induces ferroptosis and autophagy via PP2A/AMPK pathway in multiple myeloma cells

Zhong, Y., Tian, F., Ma, H., Wang, H., Yang, W., Liu, Z., & Liao, A. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118077 · Cited by 98 · see citing works

Contemporary Issues Surrounding Folic Acid Fortification Initiatives

Choi, J., Yates, Z. R., Veysey, M. J., Heo, Y.-R., & Lucock, M. D. (2014) · Preventive Nutrition and Food Science · doi:10.3746/pnf.2014.19.4.247 · Cited by 96 · see citing works

Arabidopsis thaliana histone deacetylase 14 (HDA14) is an α‐tubulin deacetylase that associates with PP2A and enriches in the microtubule fraction with the putative histone acetyltransferase ELP3

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PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma

Puustinen, P., Junttila, M. R., Vanhatupa, S., Sablina, A. A., Hector-Greene, M., Teittinen, K. J., Raheem, O., Ketola, K., Lin, S., Kast, J., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2760 · Cited by 95 · see citing works

Pharmacologic inhibition of protein phosphatase-2A achieves durable immune-mediated antitumor activity when combined with PD-1 blockade

Ho, W. S., Wang, H., Maggio, D. M., Kovach, J. S., Zhang, Q., Song, Q., Marincola, F. M., Heiss, J. D., Gilbert, M. R., Lu, R. O., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04425-z · Cited by 92 · see citing works

A PP6-Type Phosphatase Holoenzyme Directly Regulates PIN Phosphorylation and Auxin Efflux in Arabidopsis

Dai, M., Zhang, C., Kania, U., Chen, F., Qin, X., McCray, T. N., Li, G., Qin, G., Wakeley, M. E., Terzaghi, W., et al. (2012) · The Plant Cell · doi:10.1105/tpc.112.098905 · Cited by 94 · see citing works

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

Janssens, V., & Rebollo, A. (2012) · Current Molecular Medicine · doi:10.2174/156652412799218930 · Cited by 93 · see citing works

Small molecule therapeutics for tauopathy in Alzheimer’s disease: Walking on the path of most resistance

Wang, L., Bharti, Kumar, R., Pavlov, P. F., & Winblad, B. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112915 · Cited by 92 · see citing works

Nuclear Import of Histone Deacetylase 5 by Requisite Nuclear Localization Signal Phosphorylation

Greco, T. M., Yu, F., Guise, A. J., & Cristea, I. M. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.004317 · Cited by 92 · see citing works

Protein phosphatase 2A enables expression of interleukin 17 (IL-17) through chromatin remodeling

Apostolidis, S. A., Rauen, T., Hedrich, C. M., Tsokos, G. C., & Crispín, J. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.483743 · Cited by 91 · see citing works

Sphingosine regulates the NLRP3‐inflammasome and IL‐1β release from macrophages

Luheshi, N., Giles, J. A., López‐Castejón, G., & Brough, D. (2011) · European Journal of Immunology · doi:10.1002/eji.201142079 · Cited by 91 · see citing works

Determinants for Substrate Specificity of Protein Phosphatase 2A

Slupe, A. M., Merrill, R. A., & Strack, S. (2011) · Enzyme Research · doi:10.4061/2011/398751 · Cited by 91 · see citing works

Molecular Mechanisms Underlying Cardiac Protein Phosphatase 2A Regulation in Heart

DeGrande, S. T., Little, S. C., Nixon, D. J., Wright, P., Snyder, J. S., Dun, W., Murphy, N. P., Kılıç, A., Higgins, R. S. D., Binkley, P. F., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.426957 · Cited by 92 · see citing works

A Dual Role for Receptor-interacting Protein Kinase 2 (RIP2) Kinase Activity in Nucleotide-binding Oligomerization Domain 2 (NOD2)-dependent Autophagy

Homer, C. R., Kabi, A., Marina–García, N., Sreekumar, A., Nesvizhskii, A. I., Nickerson, K. P., Chinnaiyan, A. M., Núñez, G., & McDonald, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.326835 · Cited by 89 · see citing works

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

Glucose-induced posttranslational activation of protein phosphatases PP2A and PP1 in yeast

Castermans, D., Somers, I., Kriel, J., Louwet, W., Wera, S., Versele, M., Janssens, V., & Thevelein, J. M. (2012) · Cell Research · doi:10.1038/cr.2012.20 · Cited by 86 · see citing works

Protein phosphatases PP 2A, PP 4 and PP 6: mediators and regulators in development and responses to environmental cues

Lillo, C., Kataya, A. R. A., HEIDARI, B., Creighton, M. T., Nemie-Feyissa, D., Ginbot, Z., & Jonassen, E. M. (2014) · Plant Cell & Environment · doi:10.1111/pce.12364 · Cited by 84 · see citing works

ALDH1L1 inhibits cell motility via dephosphorylation of cofilin by PP1 and PP2A

Oleinik, N. V., Krupenko, N. I., & Krupenko, S. A. (2010) · Oncogene · doi:10.1038/onc.2010.356 · Cited by 80 · see citing works

CIP2A signature reveals the MYC dependency of CIP2A-regulated phenotypes and its clinical association with breast cancer subtypes

Niemelä, M., Kauko, O., Sihto, H., Mpindi, J.-P., Nicorici, D., Pernilä, P., Kallioniemi, O.-P., Joensuu, H., Hautaniemi, S., & Westermarck, J. (2012) · Oncogene · doi:10.1038/onc.2011.599 · 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

Folate Deficiency Induces In Vitro and Mouse Brain Region-Specific Downregulation of Leucine Carboxyl Methyltransferase-1 and Protein Phosphatase 2A Bα Subunit Expression That Correlate with Enhanced Tau Phosphorylation

Sontag, J., Nunbhakdi‐Craig, V., Montgomery, L. G., Arning, E., Bottiglieri, T., & Sontag, E. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2816-08.2008 · Cited by 77 · see citing works

Antiphospholipid antibodies induce thrombosis by PP2A activation via apoER2-Dab2-SHC1 complex formation in endothelium

Sacharidou, A., Chambliss, K. L., Ulrich, V., Salmon, J. E., Shen, Y.-M. P., Herz, J., Hui, D. Y., Terada, L. S., Shaul, P. W., & Mineo, C. (2018) · Blood · doi:10.1182/blood-2017-11-814681 · Cited by 78 · 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

The <i>Arabidopsis rcn1-1</i> Mutation Impairs Dephosphorylation of Phot2, Resulting in Enhanced Blue Light Responses

Tseng, T.-S., & Briggs, W. R. (2010) · The Plant Cell · doi:10.1105/tpc.109.066423 · Cited by 75 · see citing works

The basic biology of PP2A in hematologic cells and malignancies

Haesen, D., Sents, W., Lemaire, K., Hoorne, Y., & Janssens, V. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00347 · Cited by 73 · see citing works

Regulation of Endothelial Cell Proliferation and Vascular Assembly through Distinct mTORC2 Signaling Pathways

Wang, S., Amato, K. R., Song, W., Youngblood, V., Lee, K., Boothby, M. R., Brantley‐Sieders, D. M., & Chen, J. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00306-14 · Cited by 71 · see citing works

Bod1 regulates protein phosphatase 2A at mitotic kinetochores

Porter, I. M., Schleicher, K., Porter, M., & Swedlow, J. R. (2013) · Nature Communications · doi:10.1038/ncomms3677 · Cited by 70 · see citing works

Protein Phosphatase 2A in the Regulation of Wnt Signaling, Stem Cells, and Cancer

Thompson, J. J., & Williams, C. S. (2018) · Genes · doi:10.3390/genes9030121 · Cited by 69 · see citing works

Molecular Implication of PP2A and Pin1 in the Alzheimer's Disease Specific Hyperphosphorylation of Tau

Landrieu, I., Smet‐Nocca, C., Amniai, L., Louis, J. V., Wieruszeski, J., Goris, J., Janssens, V., & Lippens, G. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021521 · Cited by 68 · see citing works

Protein Phosphatase 2A B55 and A Regulatory Subunits Interact with Nitrate Reductase and Are Essential for Nitrate Reductase Activation

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Protein Phosphatase 2A as a Therapeutic Target in Acute Myeloid Leukemia

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