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Showing PPME1 — PME-1 is a alias.

PPME1

Protein phosphatase methylesterase 1 · UniProt Q9Y570

Length
386 aa
Mass
42.3 kDa
Annotated
2026-06-10
33 papers in source corpus 19 papers cited in narrative 19 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PPME1/PME-1 is a serine-hydrolase methylesterase that controls the methylation status, composition, and activity of PP2A-family phosphatases, thereby tuning kinase signaling, mitosis, neuronal differentiation, and cell-death decisions (PMID:10318862, PMID:18596935). It was identified through stable association with catalytically inactive PP2A C subunit and demethylates PP2Ac via a lipase-like catalytic triad whose nucleophilic serine is required for activity, a reaction blocked by okadaic acid (PMID:10318862). Genetic ablation in mice eliminates demethylated PP2A and paradoxically lowers PP2A catalytic activity, because PME-1 methylesterase activity protects PP2Ac from poly-ubiquitination and proteasomal degradation, stabilizing the catalytic subunit while also acting as a direct PP2A inhibitory binding partner (PMID:18596935, PMID:26678046). Demethylation by PME-1 selectively drives dissociation of B55- and PR72-containing holoenzymes but not B56 complexes (PMID:30186749), and a cryo-EM structure of the PP2A-B56–PME-1 complex shows that PME-1 disordered regions, including a substrate-mimicking motif, tether to the B56 regulatory subunit and occupy the holoenzyme substrate groove to activate the methylesterase (PMID:35924897). CHK1-mediated phosphorylation of PP2Ac at Thr219 promotes PME-1 association independent of methylation, and PME-1 binding reciprocally shields CHK1 from PP2A-mediated dephosphorylation (PMID:38588804). Through these activities PME-1 supports basal ERK and Akt signaling, controls mitotic spindle length via the LCMT1–PME-1 methylation equilibrium, and modulates apoptosis and stress responses in tumor cells (PMID:19293187, PMID:25839665, PMID:37500619). Separation-of-function knock-in mice establish that the methylesterase activity and the PP2A-inhibitory binding activity are independently essential for development and tissue homeostasis, with distinct phenotypes in apoptosis/ROS control versus olfactory epithelium integrity (PMID:40326231).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 1999 High

    Established the molecular identity and catalytic mechanism of PME-1, answering what enzyme removes the methyl group from PP2A and how it acts.

    Evidence Co-purification with inactive PP2A mutants, cDNA cloning, and in vitro demethylation by bacterially expressed protein with active-site characterization

    PMID:10318862

    Open questions at the time
    • Did not resolve the in vivo consequences of demethylation
    • Structural basis of substrate engagement not determined
  2. 2008 High

    Defined the organismal requirement for PME-1 and revealed the counterintuitive coupling between demethylation and PP2A activity.

    Evidence Targeted gene knockout in mice with PP2A activity assay and phosphoproteome analysis

    PMID:18596935

    Open questions at the time
    • Mechanism behind reduced PP2A activity in KO tissues not yet explained
    • Did not separate methylesterase from binding functions
  3. 2009 Medium

    Placed PME-1-mediated PP2A inhibition within growth-factor/ERK signaling, linking it to malignant phenotypes.

    Evidence siRNA knockdown and epistasis analysis in malignant glioma cells

    PMID:19293187

    Open questions at the time
    • Direct PP2A substrate in the ERK pathway not identified
    • Single cell-type context
  4. 2010 Medium

    Connected PP2A demethylation to a specific developmental output, neuronal process outgrowth.

    Evidence Overexpression, knockdown, and methylation-site mutant (L309Δ) in N2a neurite outgrowth assays

    PMID:21044074

    Open questions at the time
    • Downstream phospho-substrates governing outgrowth not defined
    • Cell-line model only
  5. 2012 Medium

    Identified upstream regulation of the methylation equilibrium, showing GSK-3β tunes PP2A demethylation via PME-1 and PPMT1.

    Evidence siRNA knockdown and double-knockdown epistasis with methylation Western blots

    PMID:22732552

    Open questions at the time
    • Direct vs indirect regulation of PME-1 by GSK-3β unresolved
    • Single lab
  6. 2014 Medium

    Defined substrate selectivity among type 2A phosphatases, showing PME-1 acts on PP4 but not PP6.

    Evidence Co-immunoprecipitation and functional assays in endometrial cancer cells

    PMID:24928782

    Open questions at the time
    • Structural basis for PP4-versus-PP6 discrimination unknown
    • Demethylation of PP4 not directly demonstrated
  7. 2014 Medium

    Linked PME-1 to metabolic signaling, showing pharmacological promotion of demethylation relieves PP2A repression of Akt and enhances glucose uptake.

    Evidence siRNA knockdown, PP2A activity, GLUT4 translocation and PKB phosphorylation assays in skeletal muscle cells

    PMID:25038454

    Open questions at the time
    • Mechanism of carnosic acid action on PME-1 not defined
    • Single lab
  8. 2015 High

    Resolved the paradox of the KO phenotype by showing methylesterase activity protects PP2Ac from ubiquitin-proteasome degradation.

    Evidence PME-1 KO MEFs, chemical inhibition, rescue with WT versus catalytic-mutant PME-1, ubiquitination and half-life measurements

    PMID:26678046

    Open questions at the time
    • E3 ligase targeting PP2Ac not identified
    • How methylation status couples to ubiquitination not mechanistically detailed
  9. 2015 Medium

    Established that the LCMT1–PME-1 methylation balance controls mitotic spindle length and faithful division.

    Evidence siRNA, overexpression, pharmacological inhibition, and spindle immunofluorescence

    PMID:25839665

    Open questions at the time
    • Relevant PP2A holoenzyme and spindle substrates not identified
    • Single lab
  10. 2016 Medium

    Showed PME-1-mediated PP2A inhibition confers drug resistance through HDAC4 and BAD, defining a synthetic-lethal vulnerability.

    Evidence Overexpression/knockdown with genetic epistasis to HDAC4 and BAD in glioma cells

    PMID:27671680

    Open questions at the time
    • Direct PP2A complex responsible not fully defined
    • Single tumor context
  11. 2018 Medium

    Revealed holoenzyme-family selectivity, showing demethylation dissociates B55/PR72 but not B56 complexes.

    Evidence In vitro demethylation with pharmacological inhibition and immunoprecipitation of PP2A subcomplexes

    PMID:30186749

    Open questions at the time
    • Mechanistic basis for B56 resistance not yet structurally explained
    • Single lab
  12. 2018 Medium

    Identified post-translational control of PME-1 abundance via USP36 deubiquitination, linking it to ERK and Akt signaling.

    Evidence Co-IP, siRNA knockdown, ubiquitination assay and stability Western blots

    PMID:29577269

    Open questions at the time
    • E3 ligase opposing USP36 unknown
    • Single lab Co-IP without reciprocal structural mapping
  13. 2020 Medium

    Mapped the global phosphotarget landscape controlled by PME-1 and showed non-redundancy with CIP2A and SET.

    Evidence siRNA depletion with mass spectrometry phosphoproteomics in HeLa cells

    PMID:32071079

    Open questions at the time
    • Direct versus indirect targets not distinguished
    • Single study
  14. 2022 High

    Provided the structural mechanism by which PME-1 engages the B56 holoenzyme using substrate-mimicking disordered motifs to access the active site.

    Evidence Cryo-EM structure plus B56 interface mutagenesis, in vitro activity, and cellular p53 signaling readouts

    PMID:35924897

    Open questions at the time
    • Structures of other holoenzyme-family complexes not solved
    • Dynamics of the activating conformational shift in cells not captured
  15. 2023 High

    Demonstrated nuclear PME-1 sensitizes glioblastoma cells to oxidative-stress death via PP2A-B55α, requiring methylesterase, binding, and nuclear localization activities.

    Evidence Pharmacological inhibition, separation-of-function mutants, fractionation, Co-IP and kinase assays in two cell lines

    PMID:37500619

    Open questions at the time
    • Determinants of PME-1 nuclear targeting not defined
    • Generality beyond glioblastoma unknown
  16. 2023 Medium

    Linked PME-1 to anoikis suppression and histone methylation in PTEN-deficient prostate cancer.

    Evidence Overexpression/knockdown, in ovo xenograft, zebrafish circulation and histone modification assays

    PMID:36461911

    Open questions at the time
    • Mechanism connecting PP2A activity to H3K9/H3K27 trimethylation not established
    • Single lab
  17. 2023 Low

    Provided transcriptome-level associations of PME-1 with inflammatory, PI3K/Akt, and EMT programs.

    Evidence RNA-seq of PME-1 knockout MEFs

    PMID:38043157

    Open questions at the time
    • No direct mechanistic validation beyond transcriptome
    • Causality versus secondary adaptation not resolved
  18. 2024 High

    Identified CHK1 as a kinase that primes PP2Ac (Thr219) for PME-1 binding and revealed a reciprocal CHK1-protective loop.

    Evidence NanoBiT PPI assay, compound screening, in vitro kinase/phosphatase reactions, phospho-MS, and phospho-Thr219 antibody validation

    PMID:38588804

    Open questions at the time
    • Physiological contexts where CHK1-PME-1 axis operates not fully mapped
    • Effect on holoenzyme assembly downstream of Thr219 phosphorylation unresolved
  19. 2025 High

    Genetically separated the two essential PME-1 activities in vivo, showing methylesterase and PP2A-inhibitory binding functions are non-redundant for distinct developmental outcomes.

    Evidence S156A and M335D knock-in mice with histology, gene expression, and mitochondrial/ROS assays in primary fibroblasts

    PMID:40326231

    Open questions at the time
    • Molecular basis of tissue-specific phenotype divergence not defined
    • Direct downstream substrates driving apoptosis and ROS not identified

Open questions

Synthesis pass · forward-looking unresolved questions
  • How PME-1 selects among PP2A/PP4 holoenzyme families in vivo and which specific phospho-substrates mediate its distinct developmental, mitotic, and stress phenotypes remain unresolved.
  • Substrate-level wiring of PME-1-controlled PP2A to specific phenotypes incomplete
  • E3 ligase that degrades PP2Ac upon PME-1 loss unknown
  • Structural basis of B55/PR72 versus B56 selectivity not fully explained

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 5 GO:0140096 catalytic activity, acting on a protein 4 GO:0016787 hydrolase activity 2
Localization
GO:0005634 nucleus 1 GO:0005829 cytosol 1
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-1640170 Cell Cycle 2 R-HSA-5357801 Programmed Cell Death 2 R-HSA-392499 Metabolism of proteins 1
Partners
CHEK1LCMT1PPP2CAPPP2R2A (B55)PPP2R5 (B56)PPP4CUSP36
Complex memberships
PP2A holoenzyme (catalytic subunit complex)

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 PME-1 (protein phosphatase methylesterase-1) was identified as a novel protein that stably associates with catalytically inactive mutants of PP2A C subunit. Bacterially expressed PME-1 demethylated the PP2A C subunit in vitro, and okadaic acid inhibited this reaction. PME-1 contains a lipase-like motif with a catalytic triad-activated serine as its active site nucleophile. Co-purification with inactive PP2A mutants, microsequencing, cDNA cloning, in vitro demethylation assay with bacterially expressed protein, inhibitor studies The Journal of biological chemistry High 10318862
2008 Targeted disruption of the PME-1 gene in mice causes perinatal lethality and a virtually complete loss of demethylated PP2A in the nervous system and peripheral tissues. PME-1 knockout tissues also showed dramatically reduced PP2A catalytic activity over a peptide substrate and alterations in phosphoproteome content. Genetic knockout (targeted disruption), biochemical assay of PP2A activity, phosphoproteome analysis PloS one High 18596935
2009 PME-1-mediated inhibition of PP2A promotes basal ERK pathway activity in malignant glioma cells; PME-1 supports ERK pathway signaling upstream of Raf but downstream of growth factor receptors and protein kinase C. siRNA knockdown, epistasis analysis with pathway modulators, cell-based signaling assays Cancer research Medium 19293187
2010 Expression of PME-1 or the methylation-site mutant PP2A C subunit (L309Δ), which decrease intracellular methylated PP2A-C and Bα levels, block N2a cell differentiation and LCMT1-mediated neurite formation, establishing a mechanistic link between PP2A demethylation by PME-1 and regulation of neuronal process outgrowth. Overexpression, knockdown (inducible and non-inducible), methylation-site mutant expression, neurite outgrowth assay Journal of neurochemistry Medium 21044074
2012 GSK-3β regulates demethylation of PP2A at leucine-309 by upregulating PME-1 and inhibiting PPMT1; knockdown of PME-1 or PPMT1 eliminated GSK-3β effects on PP2A-C demethylation. siRNA knockdown, Western blot for PP2A methylation status, epistasis via double knockdown FEBS letters Medium 22732552
2014 PME-1 can bind and regulate protein phosphatase 4 (PP4) catalytic subunit but not the related protein phosphatase 6 (PP6), demonstrating substrate selectivity among type 2A phosphatases. Co-immunoprecipitation, overexpression, functional assays in endometrial cancer cells Cancer research Medium 24928782
2014 Carnosic acid promotes PME-1-mediated demethylation of the PP2A catalytic subunit, leading to suppressed PP2A activity and alleviation of PP2A-mediated repression of PKB/Akt, thereby stimulating glucose uptake via GLUT4 translocation in skeletal muscle cells. siRNA knockdown of PME-1, PP2A activity assay, GLUT4 translocation assay, PKB phosphorylation measurements Cellular signalling Medium 25038454
2015 PME-1 methylesterase activity protects the PP2A catalytic subunit from ubiquitin/proteasome degradation; loss of PME-1 enhanced poly-ubiquitination of PP2Ac and shortened its half-life, leading to reduced PP2Ac levels and paradoxically lower PP2A activity. PME-1 knockout MEFs, chemical inhibition of PME-1, rescue experiments with wild-type and catalytic mutant PME-1, ubiquitination assays, protein half-life measurement PloS one High 26678046
2015 Depletion of PME-1 or pharmacological inhibition of PME-1, or overexpression of LCMT1, leads to short mitotic spindles, while depletion of LCMT1 or overexpression of PME-1 leads to long spindles; perturbation of the LCMT1-PME-1 methylation equilibrium causes mitotic arrest, spindle assembly checkpoint activation, defective cell divisions, and apoptosis. siRNA knockdown, overexpression, pharmacological inhibition, immunofluorescence microscopy of spindle size Cell cycle (Georgetown, Tex.) Medium 25839665
2016 PME-1-mediated PP2A inhibition drives resistance of glioma cells to multikinase inhibitors; this resistance is dependent on specific PP2A complexes and is mediated by a decrease in cytoplasmic HDAC4 activity, with synthetic lethality requiring coexpression of proapoptotic BAD. PME-1 overexpression/knockdown, drug sensitivity assays, genetic epistasis with HDAC4 and BAD Cancer research Medium 27671680
2018 PME-1 demethylates PP2Ac in cell extracts even at 0°C unless prevented by a PME-1 methylesterase inhibitor, promoting dissociation of PP2A heterotrimers containing B55 or PR72 subunits but not those with B56 subunits, revealing differential sensitivity of PP2A holoenzyme families to methylation status. In vitro demethylation assay, pharmacological PME-1 inhibition, immunoprecipitation of PP2A subcomplexes FEBS open bio Medium 30186749
2018 USP36 deubiquitinase stabilizes PME-1 through its deubiquitinating enzyme activity; depletion of USP36 decreases PME-1 expression level, and USP36 promotes ERK and Akt signaling pathways through PME-1. Co-immunoprecipitation, siRNA knockdown, ubiquitination assay, Western blot for PME-1 stability FEBS letters Medium 29577269
2020 Systematic phosphoproteomics revealed that PME-1 depletion (to reactivate PP2A) modulates phosphorylation of targets in kinase signaling, cytoskeleton, RNA splicing, DNA repair, and nuclear lamina pathways, and that PME-1, CIP2A, and SET are non-redundant in phosphotarget regulation. siRNA depletion, mass spectrometry-based phosphoproteomics in HeLa cells The Journal of biological chemistry Medium 32071079
2022 Cryo-EM structure of a PP2A-B56 holoenzyme–PME-1 complex revealed that PME-1 disordered regions, including a substrate-mimicking motif, tether to the B56 regulatory subunit at remote sites, occupy the holoenzyme substrate-binding groove, and allow large structural shifts in both holoenzyme and PME-1 to activate the methylesterase. B56 interface mutations selectively block PME-1 activity toward PP2A-B56 holoenzymes and affect cellular PP2A methylation and p53 signaling. High-resolution cryo-EM structure, in vitro demethylation assay, B56 interface mutagenesis, cellular p53 signaling assay eLife High 35924897
2023 PME-1 sensitizes glioblastoma cells to oxidative stress-induced cell death via nuclear PP2A-B55α activity; oxidative stress increases nuclear localization of PP2A-B55α, binding of PP2A-B55α to PME-1, and B55α-bound PP2A-C demethylation. PME-1 overexpression increases stress-induced phosphorylation and activity of MAPKAPK2 and RIPK1, causing sensitization. The methylesterase function, PP2A binding capacity, and nuclear localization of PME-1 are all required for this effect. Pharmacological PME-1 inhibition (AMZ30), PME-1 mutants (methylesterase-dead, PP2A binding-dead, nuclear localization mutants), subcellular fractionation, co-immunoprecipitation, kinase activity assays Cell death discovery High 37500619
2023 Transcriptome analysis of PME-1 knockout mouse embryonic fibroblasts showed that PME-1 suppresses inflammatory signaling, activates PI3K/Akt signaling, and promotes epithelial-mesenchymal transition at the transcriptional level. PME-1 knockout MEFs, RNA-seq transcriptome analysis Biochemical and biophysical research communications Low 38043157
2024 CHK1 directly phosphorylates the PP2A catalytic subunit (including Thr219) to promote PME-1 association with PP2Ac; CHK1 inhibitors block PME-1/PP2Ac association without affecting PP2Ac methylation levels. Reciprocally, PME-1 binding to PP2Ac hinders PP2A-mediated dephosphorylation of CHK1. NanoBiT bioluminescence protein-protein interaction assay, compound screening, in vitro kinase/phosphatase assays, phospho-mass spectrometry, anti-phospho-Thr219 antibody generation and validation The Journal of biological chemistry High 38588804
2025 Two distinct mechanisms of PME-1 are both essential for mouse development: (1) methylesterase activity (abolished by S156A knock-in) is required to prevent systemic apoptosis, brain atrophy with cerebellar layer collapse, increased inflammation, and elevated reactive oxygen species in mitochondria; (2) PP2A inhibitory binding activity (abolished by M335D knock-in) is required for olfactory epithelium integrity and survival for ~2 days postnatally. Both phenotypes differ from the perinatal lethality of PME-1 null mice, demonstrating non-redundancy of the two mechanisms in vivo. Knock-in mouse models (S156A and M335D point mutants), histological and gene expression analysis, primary embryonic fibroblast assays (mitochondrial number, oxygen consumption rate, ROS levels) FASEB journal High 40326231
2023 PME-1 overexpression suppresses anoikis in PTEN-deficient prostate cancer cells; PME-1 inhibition increased apoptosis in in ovo PCa tumor xenografts and attenuated PCa cell survival in zebrafish circulation. PME-1-deficient PC3 cells display increased trimethylation at H3K9 and H3K27, correlating with increased apoptosis sensitivity. PME-1 overexpression, siRNA knockdown, in ovo xenograft, zebrafish circulation assay, histone modification analysis (ChIP/Western) Molecular oncology Medium 36461911

Source papers

Stage 0 corpus · 33 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1999 A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. The Journal of biological chemistry 164 10318862
2009 PME-1 protects extracellular signal-regulated kinase pathway activity from protein phosphatase 2A-mediated inactivation in human malignant glioma. Cancer research 81 19293187
2014 PME-1 modulates protein phosphatase 2A activity to promote the malignant phenotype of endometrial cancer cells. Cancer research 54 24928782
2012 A functional pectin methylesterase inhibitor protein (SolyPMEI) is expressed during tomato fruit ripening and interacts with PME-1. Plant molecular biology 53 22610346
2020 Phosphoproteome and drug-response effects mediated by the three protein phosphatase 2A inhibitor proteins CIP2A, SET, and PME-1. The Journal of biological chemistry 51 32071079
2016 Regulation of protein phosphatase 2A (PP2A) tumor suppressor function by PME-1. Biochemical Society transactions 45 27913678
2010 Regulation of protein phosphatase 2A methylation by LCMT1 and PME-1 plays a critical role in differentiation of neuroblastoma cells. Journal of neurochemistry 45 21044074
2018 Protein Phosphatase 2A and Its Methylation Modulating Enzymes LCMT-1 and PME-1 Are Dysregulated in Tauopathies of Progressive Supranuclear Palsy and Alzheimer Disease. Journal of neuropathology and experimental neurology 40 29281045
2016 PP2A Inhibitor PME-1 Drives Kinase Inhibitor Resistance in Glioma Cells. Cancer research 40 27671680
2008 Targeted disruption of the PME-1 gene causes loss of demethylated PP2A and perinatal lethality in mice. PloS one 38 18596935
2014 Carnosic acid stimulates glucose uptake in skeletal muscle cells via a PME-1/PP2A/PKB signalling axis. Cellular signalling 35 25038454
2012 Glycogen synthase kinase-3β regulates leucine-309 demethylation of protein phosphatase-2A via PPMT1 and PME-1. FEBS letters 34 22732552
2015 Protein Phosphatase Methyl-Esterase PME-1 Protects Protein Phosphatase 2A from Ubiquitin/Proteasome Degradation. PloS one 33 26678046
2020 DNAH17-AS1 promotes pancreatic carcinoma by increasing PPME1 expression via inhibition of miR-432-5p. World journal of gastroenterology 26 32351291
2013 Genetic amplification of PPME1 in gastric and lung cancer and its potential as a novel therapeutic target. Cancer biology & therapy 25 24253382
2011 PME-1, an extended-spectrum β-lactamase identified in Pseudomonas aeruginosa. Antimicrobial agents and chemotherapy 23 21402845
2018 A stable association with PME-1 may be dispensable for PP2A demethylation - implications for the detection of PP2A methylation and immunoprecipitation. FEBS open bio 22 30186749
2002 The genes pme-1 and pme-2 encode two poly(ADP-ribose) polymerases in Caenorhabditis elegans. The Biochemical journal 22 12145714
2013 IMP1 promotes choriocarcinoma cell migration and invasion through the novel effectors RSK2 and PPME1. Gynecologic oncology 17 23911878
2015 Protein phosphatase methylesterase-1 (PME-1) expression predicts a favorable clinical outcome in colorectal cancer. Cancer medicine 15 26377365
2023 PP2A methylesterase PME-1 suppresses anoikis and is associated with therapy relapse of PTEN-deficient prostate cancers. Molecular oncology 12 36461911
2022 Coupling to short linear motifs creates versatile PME-1 activities in PP2A holoenzyme demethylation and inhibition. eLife 12 35924897
2015 A LCMT1-PME-1 methylation equilibrium controls mitotic spindle size. Cell cycle (Georgetown, Tex.) 12 25839665
2021 Long non-coding RNA HOTAIR/microRNA-761 sponge regulates PPME1 and further influences cell biological functions in thyroid carcinoma. Laryngoscope investigative otolaryngology 11 34195365
2022 Hsa_circ_0050102 regulates the pancreatic cancer development via miR-218-5p/PPME1 axis. Journal of clinical laboratory analysis 9 35060203
2018 PME-1 is regulated by USP36 in ERK and Akt signaling pathways. FEBS letters 8 29577269
2023 PME-1 sensitizes glioblastoma cells to oxidative stress-induced cell death by attenuating PP2A-B55α-mediated inactivation of MAPKAPK2-RIPK1 signaling. Cell death discovery 6 37500619
2020 Reduced Expression of the PP2A Methylesterase, PME-1, or the PP2A Methyltransferase, LCMT-1, Alters Sensitivity to Beta-Amyloid-Induced Cognitive and Electrophysiological Impairments in Mice. The Journal of neuroscience : the official journal of the Society for Neuroscience 5 32341098
2025 Coexistence of tmexCD-toprJ, blaNDM-1, and blaPME-1 in multi-drug-resistant Pseudomonas juntendi isolates recovered from stool samples. Microbiology spectrum 4 39998246
2024 The luciferase-based in vivo protein-protein interaction assay revealed that CHK1 promotes PP2A and PME-1 interaction. The Journal of biological chemistry 4 38588804
2025 PP2A methylesterase, PME-1, and PP2A methyltransferase, LCMT-1, control sensitivity to impairments caused by injury-related oligomeric tau. Alzheimer's & dementia : the journal of the Alzheimer's Association 2 41388803
2023 Transcriptome analysis revealed that PME-1 suppresses inflammatory signaling, activates PI3K/Akt signaling, and promotes epithelial-mesenchymal transition. Biochemical and biophysical research communications 2 38043157
2025 Two Distinct Mechanisms of PP2A Regulation by Methylesterase PME-1 Are Both Essential for Mouse Development. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 0 40326231

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