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Large‐scale mapping of human protein–protein interactions by mass spectrometry

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From Promiscuity to Precision: Protein Phosphatases Get a Makeover

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Protein phosphatase 2A regulatory subunits and cancer

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Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases.Preprint

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Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme

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Structure of the Protein Phosphatase 2A Holoenzyme

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Biguanide metformin acts on tau phosphorylation via mTOR/protein phosphatase 2A (PP2A) signaling

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PP2A: the expected tumor suppressor

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

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The B56 Family of Protein Phosphatase 2A (PP2A) Regulatory Subunits Encodes Differentiation-induced Phosphoproteins That Target PP2A to Both Nucleus and Cytoplasm

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Emerging roles of nuclear protein phosphatases

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

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A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein

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Multiple pathways regulated by the tumor suppressor PP2A in transformation

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

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MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation

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Phosphatases: providing safe passage through mitotic exit

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Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation

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

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An integrated workflow for charting the human interaction proteome: insights into the PP2A system

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Involvement of PP2A in viral and cellular transformation

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Combined Functional Genomic and Proteomic Approaches Identify a PP2A Complex as a Negative Regulator of Hippo Signaling

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TIP41 Interacts with TAP42 and Negatively Regulates the TOR Signaling Pathway

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

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Delayed embryonic lethality in mice lacking protein phosphatase 2A catalytic subunit Cα

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B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A

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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

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Structural mechanism of demethylation and inactivation of protein phosphatase 2A

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The Tumor Suppressor PP2A Aβ Regulates the RalA GTPase

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Structure and Function of the PP2A-Shugoshin Interaction

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Identification of PP2A Complexes and Pathways Involved in Cell Transformation

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

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

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

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A Novel, Evolutionarily Conserved Protein Phosphatase Complex Involved in Cisplatin Sensitivity

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

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α4 Associates with Protein Phosphatases 2A, 4, and 6

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

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α4 Is an Essential Regulator of PP2A Phosphatase Activity

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

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Quantitative interaction proteomics using mass spectrometry

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The PP2A-Associated Protein α4 Is an Essential Inhibitor of Apoptosis

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Autoregulation of Protein Phosphatase Type 2A Expression

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

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The structural basis for tight control of PP2A methylation and function by LCMT-1

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MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, alpha 4, to microtubules: Implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders

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

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Protein phosphatase 2A methylation: a link between elevated plasma homocysteine and Alzheimer's Disease

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The metabolic advantage of tumor cells

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Rapamycin activates Tap42‐associated phosphatases by abrogating their association with Tor complex 1

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Ig Receptor Binding Protein 1 (α4) Is Associated With a Rapamycin-Sensitive Signal Transduction in Lymphocytes Through Direct Binding to the Catalytic Subunit of Protein Phosphatase 2A

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Protein Phosphatase 6 Regulatory Subunits Composed of Ankyrin Repeat Domains

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Diversity in the Regulatory B-Subunits of Protein Phosphatase 2A: Identification of a Novel Isoform Highly Expressed in Brain

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Regulation of Protein Phosphatase 2A Catalytic Activity by alpha4 Protein and Its Yeast Homolog Tap42

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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

A tumor suppressor role for PP2A-B56α through negative regulation of c-Myc and other key oncoproteins

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Academic cross-fertilization by public screening yields a remarkable class of protein phosphatase methylesterase-1 inhibitors

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Protein Phosphatase 6 Subunit with Conserved Sit4-associated Protein Domain Targets IκBϵ

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

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

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

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

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The α4 Regulatory Subunit Exerts Opposing Allosteric Effects on Protein Phosphatases PP6 and PP2A

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Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit α4

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

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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

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

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A Developmentally Regulated, Neuron-specific Splice Variant of the Variable Subunit Bβ Targets Protein Phosphatase 2A to Mitochondria and Modulates Apoptosis

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Control of mTORC1 signaling by the Opitz syndrome protein MID1

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Determinants for Substrate Specificity of Protein Phosphatase 2A

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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

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De novo telomere formation is suppressed by the Mec1-dependent inhibition of Cdc13 accumulation at DNA breaksPreprint

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

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Protein phosphatases and the regulation of mitosis

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Interaction with Tap42 Is Required for the Essential Function of Sit4 and Type 2A Phosphatases

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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

Beyond the dopamine receptor: regulation and roles of serine/threonine protein phosphatases

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Purification and Identification of a Novel Subunit of Protein Serine/Threonine Phosphatase 4

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Cloning and characterization of Bδ, a novel regulatory subunit of protein phosphatase 2A

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PP4R4/KIAA1622 Forms a Novel Stable Cytosolic Complex with Phosphoprotein Phosphatase 4

Chen, G. I., Tisayakorn, S., Jørgensen, C., D'Ambrosio, L. M., Goudreault, M., & Gingras, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803443200 · Cited by 80 · see citing works

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

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Two highly related regulatory subunits of PP2A exert opposite effects on TGF-β/Activin/Nodal signalling

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Animal models reveal role for tau phosphorylation in human disease

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Localization ofSaccharomyces cerevisiaeProtein Phosphatase 2A Subunits throughout Mitotic Cell Cycle

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Phosphatase PP2A is requisite for the function of regulatory T cells

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B56δ-related protein phosphatase 2A dysfunction identified in patients with intellectual disability

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Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56

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PP2A methylation controls sensitivity and resistance to β-amyloid-induced cognitive and electrophysiological impairments

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PP2A Inactivation Mediated by <i>PPP2R4</i> Haploinsufficiency Promotes Cancer Development

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