Affinage

PTPN9

Tyrosine-protein phosphatase non-receptor type 9 · UniProt P43378

Length
593 aa
Mass
68.0 kDa
Annotated
2026-04-28
46 papers in source corpus 23 papers cited in narrative 23 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PTPN9 (PTP-MEG2) is a non-receptor protein tyrosine phosphatase that couples lipid-directed membrane targeting to the regulation of vesicle trafficking, exocytosis, and receptor tyrosine kinase signaling. Its N-terminal Sec14p homology domain binds phosphatidylserine and PtdIns(3,4,5)P3 to localize the enzyme to secretory vesicle membranes, where it promotes homotypic vesicle fusion by dephosphorylating NSF (pY83) and controls fusion pore dynamics by dephosphorylating DYNAMIN2 (pY125) and MUNC18-1 (pY145); it also dephosphorylates the Q-SNARE VTI1B to drive ATG16L1-positive vesicle fusion during autophagosome biogenesis (PMID:17387180, PMID:33764618, PMID:33112705). PTPN9 functions as a broad negative regulator of growth factor and cytokine signaling by directly dephosphorylating EGFR, ErbB2, VEGFR2, FGFR2 (pY656/657), IGF1R (pY1166), TrkA, and STAT3 (pY705), thereby suppressing proliferative, angiogenic, and inflammatory pathways (PMID:20335174, PMID:22394684, PMID:22763125, PMID:37505213, PMID:41275311, PMID:27655914). Knockout studies establish essential roles in secretory vesicle biogenesis in lymphocytes, erythroid maturation via STAT3–GATA1 axis regulation, embryonic development, and intraocular pressure homeostasis (PMID:16330817, PMID:24727614, PMID:30315478).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 2001 High

    Establishing the enzymology and localization of PTPN9 in primary cells resolved how the N-terminal domain auto-inhibits catalytic activity and how polyphosphoinositides activate the phosphatase, providing the first framework for its regulation at membranes.

    Evidence Subcellular fractionation, active-site mutagenesis (C515), and lipid activation assays in human neutrophils

    PMID:11711529

    Open questions at the time
    • Identity of endogenous substrates on secretory vesicles unknown
    • Structural basis of auto-inhibition not determined
  2. 2002 High

    Demonstrating that PTPN9 catalytic activity drives homotypic secretory vesicle fusion in immune cells established its first cellular function — regulation of the secretory pathway rather than classical receptor signaling.

    Evidence Overexpression with fluorescence microscopy in mast cells and Jurkat T cells; pervanadate reversal; IL-2 secretion assay

    PMID:11971009 PMID:12112018

    Open questions at the time
    • Vesicle fusion substrates not identified
    • Mechanism linking phosphatase activity to membrane fusion unclear
  3. 2003 High

    Identification of phosphatidylserine and PtdIns(3,4,5)P3 as ligands of the Sec14p domain explained how PTPN9 is targeted to secretory vesicle membranes, and mutagenesis showed lipid binding is required for vesicle fusion activity.

    Evidence Lipid-overlay and liposome binding assays, point mutagenesis, PI3K inhibitor treatment, PS loading experiments

    PMID:12702726 PMID:14662869

    Open questions at the time
    • Relative contributions of PS versus PIP3 binding in vivo not resolved
    • Whether lipid binding relieves auto-inhibition not tested
  4. 2003 Medium

    Elevated PTPN9 in polycythemia vera erythroid progenitors and dominant-negative suppression of erythroid colony growth first linked the phosphatase to erythropoiesis.

    Evidence Cell fractionation and dominant-negative overexpression in primary human erythroid progenitors

    PMID:12920026

    Open questions at the time
    • Substrate in erythroid progenitors unidentified
    • Mechanism connecting PTPN9 to erythroid proliferation unclear
    • Single-lab observation
  5. 2005 High

    Meg2 knockout mice revealed that PTPN9 is essential for embryonic viability, secretory vesicle biogenesis in lymphocytes, and platelet function, elevating its role from an in vitro vesicle regulator to a required developmental factor.

    Evidence Gene-targeted knockout mice, hematopoietic reconstitution, electron microscopy of lymphocyte vesicles, platelet/T-cell activation assays

    PMID:16330817

    Open questions at the time
    • Specific substrates responsible for vesicle biogenesis defect unknown
    • Cause of embryonic lethality (hemorrhage vs. neural tube defect vs. bone) not delineated
  6. 2006 High

    A genome-scale screen and in vivo validation identified PTPN9 as a negative regulator of hepatic insulin receptor signaling, showing that liver-targeted depletion normalizes hyperglycemia in diabetic mice — extending PTPN9 function to metabolic regulation.

    Evidence Functional genomic screen, adenoviral hepatic depletion in db/db mice, FOXO1 localization, blood glucose measurement

    PMID:16679294

    Open questions at the time
    • Whether PTPN9 directly dephosphorylates the insulin receptor (versus an intermediate) not biochemically confirmed
    • Tissue specificity of metabolic role beyond liver not explored
  7. 2007 High

    Discovery of TIP47 and Arfaptin2 as direct binding partners of the Sec14p domain provided a protein-based targeting mechanism complementing lipid-mediated vesicle recruitment.

    Evidence Yeast two-hybrid, deletion-mutant localization, TIP47 knockdown functional assay

    PMID:17387180

    Open questions at the time
    • How TIP47/Arfaptin2 coordinate with lipid binding is unknown
    • Whether these interactions are regulated remains untested
  8. 2010 High

    Substrate-trapping and knockdown experiments identified ErbB2 and EGFR as direct PTPN9 substrates, establishing the enzyme as a negative regulator of receptor tyrosine kinase signaling with tumor-suppressive properties in breast cancer.

    Evidence DA-mutant co-immunoprecipitation, GST pulldown, siRNA knockdown, soft-agar and invasion assays

    PMID:20335174

    Open questions at the time
    • Specific phosphosites on ErbB2/EGFR targeted by PTPN9 not mapped
    • Whether vesicle-localized or cytoplasmic pool mediates RTK dephosphorylation unclear
  9. 2012 High

    Concurrent identification of STAT3 and VEGFR2 as direct substrates, together with crystal structures of the catalytic domain with selective inhibitors, broadened the substrate repertoire and provided a structural framework for drug design.

    Evidence Co-IP and in vitro dephosphorylation for STAT3/VEGFR2; X-ray crystallography of inhibitor-bound PTP-MEG2; xenograft and diet-induced obesity mouse models

    PMID:22394684 PMID:22763125 PMID:23075115

    Open questions at the time
    • How PTPN9 selects among multiple RTK and non-RTK substrates in a single cell is unknown
    • Full-length structure including Sec14p domain not solved
  10. 2014 High

    Zebrafish and human cell studies demonstrated that PTPN9-mediated STAT3 dephosphorylation is required for erythroid maturation by preventing an inhibitory STAT3–GATA1–ZBP-89 complex, providing the molecular mechanism underlying its erythropoietic role.

    Evidence Morpholino knockdown in zebrafish, dominant-negative C515S and siRNA in K562 cells, co-IP of STAT3–GATA1–ZBP-89 complex

    PMID:24727614

    Open questions at the time
    • Whether this mechanism operates in mammalian definitive erythropoiesis in vivo not confirmed
    • Regulation of PTPN9 expression during erythroid differentiation not characterized
  11. 2016 High

    Identification of TrkA as both a vesicle cargo requiring PTPN9 for surface transport and a dephosphorylation substrate linked the vesicle-trafficking and signaling functions of PTPN9 in neuronal differentiation.

    Evidence Substrate trapping, in vitro dephosphorylation, surface trafficking assay, neurite outgrowth in PC12 and cortical neurons

    PMID:27655914

    Open questions at the time
    • Whether PTPN9 controls trafficking of other RTK cargoes is untested
    • In vivo neuronal phenotype of Ptpn9 loss not characterized
  12. 2018 Medium

    Heterozygous Meg2 loss in mice caused progressive glaucoma with IOP-dependent retinal ganglion cell degeneration, revealing an unexpected in vivo role in intraocular pressure homeostasis.

    Evidence Meg2 heterozygous KO mice, IOP measurement, latanoprost pharmacological rescue, optic nerve histology

    PMID:30315478

    Open questions at the time
    • Molecular substrate mediating IOP regulation not identified
    • Relevance to human glaucoma genetics not established
    • Single-lab observation
  13. 2020 High

    Identification of VTI1B as a PTPN9 substrate that regulates SNARE complex assembly on ATG16L1-positive vesicles extended the phosphatase's membrane fusion role to autophagosome biogenesis, with cross-species validation in Drosophila.

    Evidence siRNA/RNAi depletion, VTI1B phospho-mutant analysis, SNARE complex co-IP, autophagy flux assays, Drosophila Ptpmeg2 RNAi

    PMID:33112705

    Open questions at the time
    • Whether PTPN9-VTI1B axis operates in selective autophagy pathways is unknown
    • Upstream kinase phosphorylating VTI1B not identified
  14. 2021 High

    Crystallographic and electrochemical studies revealed that PTPN9 controls catecholamine secretion through structurally separable substrate interfaces: NSF-pY83 dephosphorylation drives vesicle fusion, while DYNAMIN2-pY125 and MUNC18-1-pY145 dephosphorylation controls fusion pore dynamics.

    Evidence X-ray crystallography of PTPN9–substrate complexes, mutagenesis, electrochemical single-vesicle catecholamine release measurement

    PMID:33764618

    Open questions at the time
    • Whether these substrate interfaces can be independently targeted pharmacologically is untested
    • Physiological kinases counteracting PTPN9 at NSF/DYNAMIN2/MUNC18-1 not identified
  15. 2023 High

    ACAP1 was identified as a bridging adaptor mediating PTPN9–FGFR2 interaction via the Sec14p domain, with dephosphorylation at FGFR2 pY656/657; the cancer-associated FGFR2 I654V mutation disrupts this interaction, providing a disease-relevant substrate selectivity mechanism.

    Evidence Co-IP, mutagenesis, phosphatase assays, structural modeling, patient-derived xenograft validation

    PMID:37505213

    Open questions at the time
    • Whether ACAP1-mediated recruitment generalizes to other RTK substrates is unknown
    • Full structural model of PTPN9–ACAP1–FGFR2 ternary complex awaits experimental determination
  16. 2025 High

    Crystal structure-guided identification of IGF1R pY1166 as a direct substrate, with Tyr333 and Asp335 as key PTPN9 contact residues, provided structural precision for substrate recognition and confirmed tumor-suppressive activity through IGF1R axis inhibition.

    Evidence IP-mass spectrometry, X-ray crystallography of PTPN9–IGF1R interface, active-site mutagenesis, orthotopic mouse models, clinical tissue correlation

    PMID:41275311

    Open questions at the time
    • How PTPN9 prioritizes IGF1R versus other RTK substrates in cells co-expressing multiple receptors is unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • A full-length structure of PTPN9 revealing how the Sec14p domain auto-inhibits the catalytic domain and how lipid/protein cofactors relieve inhibition remains unresolved, as does a unified model for how a single phosphatase coordinates its diverse vesicle-fusion and RTK-regulatory functions within the same cell.
  • Full-length PTPN9 structure not solved
  • Upstream regulation of PTPN9 activity (post-translational modifications, transcriptional control beyond miR-24) poorly defined
  • Kinases counteracting PTPN9 at most substrate sites not identified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 11
Localization
GO:0031410 cytoplasmic vesicle 5 GO:0005829 cytosol 2
Pathway
R-HSA-162582 Signal Transduction 8 R-HSA-392499 Metabolism of proteins 4 R-HSA-5653656 Vesicle-mediated transport 4 R-HSA-168256 Immune System 1 R-HSA-9612973 Autophagy 1
Partners
DNM2EGFRERBB2NSFSTAT3STXBP1TIP47VTI1B

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2010 PTPN9 directly dephosphorylates ErbB2 and EGFR (but not ErbB3 or Shc) as demonstrated by substrate-trapping mutant (DA) co-immunoprecipitation and GST pulldown showing preferential association of phospho-ErbB2/EGFR with PTPN9-DA vs. WT, and by siRNA knockdown increasing ErbB2/EGFR phosphorylation. PTPN9 WT expression also specifically impairs EGF-induced STAT3 and STAT5 activation and inhibits soft-agar growth and invasion of breast cancer cells. Substrate-trapping mutant overexpression, co-immunoprecipitation, GST pulldown, siRNA knockdown, in vitro phosphorylation assays The Journal of biological chemistry High 20335174
2012 PTPN9 (PTP-MEG2) directly interacts with STAT3 and mediates its dephosphorylation in the cytoplasm. Overexpression of PTP-MEG2 decreased tyrosine phosphorylation of STAT3, suppressed STAT3 transcriptional activity, and reduced tumor growth in vitro and in vivo; depletion increased STAT3 phosphorylation. Immunoprecipitation, overexpression and siRNA knockdown, in vitro dephosphorylation assay, xenograft models Breast cancer research : BCR High 22394684
2012 PTPN9 (PTP-MEG2) dephosphorylates VEGFR2 at Tyr1175 in endothelial cells, as shown by substrate-trapping DA mutant preferentially co-immunoprecipitating with VEGFR2 after VEGF stimulation. PTP-MEG2 DA also associates with JAK1 (but not JAK2 or Tyk2) and regulates JAK1 phosphorylation. Overexpression of WT PTP-MEG2 inhibits VEGF-induced VEGFR2 phosphorylation and IL-6 production. Substrate-trapping mutant co-immunoprecipitation, overexpression and siRNA knockdown American journal of physiology. Cell physiology High 22763125
2002 PTPN9 (PTP-MEG2) expression on secretory vesicles causes striking homotypic enlargement/fusion of secretory vesicles in mast cells and Jurkat T cells. This requires the catalytic activity of PTP-MEG2 (effect reversed by pervanadate), reduces IL-2 secretion from stimulated Jurkat cells, and fused vesicles retain secretory vesicle markers (carboxypeptidase E, chromogranin C, IL-2). Overexpression with fluorescence microscopy/immunofluorescence, secretion assay, pharmacological inhibition of phosphatase activity Journal of immunology High 11971009
2003 The N-terminal Sec14p homology domain of PTP-MEG2 binds phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) in vitro and colocalizes with this lipid on secretory vesicle membranes. Point mutations preventing PtdIns(3,4,5)P3 binding abolish the ability of PTP-MEG2 to induce homotypic secretory vesicle fusion. Inhibition of cellular PtdIns(3,4,5)P3 synthesis rapidly reverses PTP-MEG2 effects on secretory vesicles. Lipid binding assay, site-directed mutagenesis, fluorescence colocalization, pharmacological PI3K inhibition Journal of immunology High 14662869
2003 PTP-MEG2 specifically binds phosphatidylserine (among >20 lipid compounds tested) through its N-terminal Sec14 domain, as shown by lipid-membrane overlay and liposome binding assays. In intact cells, the Sec14 domain is responsible for perinuclear localization of PTP-MEG2, and loading of phosphatidylserine into cell membranes causes translocation of PTP-MEG2 to the plasma membrane. Lipid-membrane overlay assay, liposome binding assay, immunofluorescence/subcellular fractionation, phosphatidylserine loading experiment The Journal of biological chemistry High 12702726
2005 MEG2 knockout mice exhibit late embryonic lethality, hemorrhages, neural tube defects, and abnormal bone development. T lymphocytes and platelets from Meg2-/- hematopoietic reconstituted mice show profound activation defects attributable to impaired IL-2 secretion; ultrastructural analysis reveals near-complete absence of mature secretory vesicles in lymphocytes, confirming MEG2 role in secretory vesicle genesis and function. Knockout mouse generation, hematopoietic reconstitution, functional lymphocyte/platelet activation assays, electron microscopy, secretion assays The Journal of experimental medicine High 16330817
2006 PTP-MEG2 antagonizes hepatic insulin signaling by inhibiting insulin-induced phosphorylation of the insulin receptor, thereby impairing nuclear exclusion of the gluconeogenic transcription factor FOXO1. Adenoviral-mediated depletion of PTP-MEG2 in livers of db/db diabetic mice results in insulin sensitization and normalization of hyperglycemia. Genome-scale functional screen, ectopic expression, RNAi knockdown, adenoviral liver-targeted depletion in db/db mice, quantitative image analysis of FOXO1 localization, blood glucose measurement Cell metabolism High 16679294
2001 In human neutrophils, MEG2 is predominantly cytosolic with components in secondary/tertiary granules and secretory vesicles, and associates at an early stage with nascent phagosomes. Cysteine 515 is essential for catalytic activity. The noncatalytic N-terminal domain negatively regulates the C-terminal phosphatase domain. MEG2 activity is enhanced by polyphosphoinositides (PI 4,5-bisphosphate > PI 3,4,5-trisphosphate > PI 4-phosphate) and is inhibited by opsonized zymosan or PMA stimulation. Immunofluorescence, cell fractionation, immunoprecipitation, in vitro phosphatase assay, GST-fusion protein mutagenesis (C515), lipid activation assay The Journal of biological chemistry High 11711529
2002 Full-length PTP-MEG2 exhibits lower Vmax and higher Km compared to the truncated catalytic domain alone, indicating the N-terminal lipid-binding domain has an inhibitory role on catalytic activity. Both forms show classical Michaelis-Menten kinetics with phosphotyrosine and pNPP substrates. In vitro phosphatase kinetics with purified recombinant full-length and truncated PTP-MEG2 Journal of cellular biochemistry High 12112018
2007 The N-terminal Sec14p homology domain (residues 1-261) of PTP-MEG2 is necessary and sufficient for secretory vesicle targeting. Yeast two-hybrid screening identified vesicle trafficking proteins TIP47 and Arfaptin2 as direct interactors of this domain; overexpression of TIP47 or Arfaptin2 alters PTP-MEG2 localization, and elimination of TIP47 results in loss of PTP-MEG2 function. Yeast two-hybrid, deletion mutant localization, overexpression of interactors, TIP47 knockdown functional assay The Journal of biological chemistry High 17387180
2012 Crystal structures of PTP-MEG2 complexed with selective inhibitors reveal that potent, selective inhibition is achieved by engaging both the active site and unique peripheral binding pockets. The structures provide direct evidence for the molecular basis of PTP-MEG2 substrate selectivity and inform inhibitor design. X-ray crystallography, in vitro phosphatase inhibition assay, cellular insulin signaling assay, diet-induced obese mouse model Journal of the American Chemical Society High 23075115
2013 miR-24 directly targets PTPN9 (and PTPRF), repressing their expression and thereby increasing EGFR phosphorylation; ectopic expression of PTPN9 decreased pEGFR levels, cell invasion, migration, and tumor metastasis in breast cancer models. miRNA target validation (luciferase assay), overexpression of PTPN9 with functional readouts (invasion, migration, pEGFR levels), in vivo mouse tumor models Journal of cell science High 23418360
2014 Ptpn9a (zebrafish ortholog of human PTPN9) is required for erythroid cell maturation. Mechanistically, depletion of ptpn9 increases phosphorylated STAT3, which entraps transcription factors GATA1 and ZBP-89 in an inhibitory complex, preventing them from regulating erythroid gene expression. Dominant-negative PTPN9 (C515S) and siRNA against human PTPN9 similarly inhibit erythroid differentiation in K562 cells. Morpholino knockdown in zebrafish, dominant-negative overexpression, siRNA in K562 cells, immunoprecipitation to detect STAT3-GATA1-ZBP-89 complex Journal of cell science High 24727614
2016 PTP-MEG2 identifies TrkA (neurotrophin receptor) as both a novel vesicle cargo requiring PTP-MEG2 for surface transport and a substrate: PTP-MEG2 dephosphorylates TrkA at Tyr-490 and Tyr-674/Tyr-675. Overexpression of PTP-MEG2 downregulates NGF/TrkA signaling and blocks neurite outgrowth and differentiation in PC12 cells and cortical neurons. Co-immunoprecipitation, substrate-trapping mutant, in vitro dephosphorylation, cell surface trafficking assay, neurite outgrowth assay The Journal of biological chemistry High 27655914
2019 PTPN9 negatively regulates STAT3 activation and nuclear translocation in colorectal cancer cells. Overexpression of PTPN9 induces apoptosis (via caspase-3/9) and inhibits colony formation; knockdown has opposite effects. The effects of PTPN9 knockdown on apoptosis are attenuated by Stat3 pathway inhibition, placing PTPN9 upstream of STAT3. Overexpression and siRNA knockdown, Western blot for pSTAT3/nuclear fractionation, caspase activity assay, colony formation assay, pharmacological STAT3 inhibitor epistasis Cancer management and research Medium 30804683
2020 PTPN9 dephosphorylates the Q-SNARE VTI1B, promoting homotypic fusion of ATG16L1+ vesicles and early autophagosome formation. The nonphosphorylatable VTI1B mutant (but not the phosphomimetic) enhances SNARE complex assembly and autophagic flux. Depletion of PTPN9 and its Drosophila homolog Ptpmeg2 impairs autophagosome formation and autophagic flux. siRNA/RNAi depletion, substrate identification, phospho-mutant analysis of VTI1B, SNARE complex co-immunoprecipitation, autophagy flux assay, Drosophila genetic validation Autophagy High 33112705
2021 PTP-MEG2 controls multiple steps of catecholamine secretion: (1) dephosphorylation of NSF-pY83 promotes vesicle fusion (key residues governing NSF interaction defined by crystallography and mutagenesis); (2) PTP-MEG2 controls fusion pore opening and extension via NSF-independent dephosphorylation of DYNAMIN2-pY125 and MUNC18-1-pY145, through a structurally distinct binding interface. Biochemical assays, X-ray crystallography, site-directed mutagenesis, electrochemical catecholamine measurement, bioinformatics substrate screening EMBO reports High 33764618
2003 PTP-MEG2 is elevated in the membrane fraction of polycythemia vera (PV) erythroid progenitor cells. Expression of dominant-negative forms of PTP-MEG2 suppresses in vitro growth and expansion of both normal and PV erythroid colony-forming cells, establishing a role for PTP-MEG2 in erythroid development. Cell fractionation, immunoblotting, dominant-negative mutant overexpression, erythroid colony formation assay Blood Medium 12920026
2023 PTPN9 interacts with FGFR2 via its Sec14p domain through ACAP1 mediation and dephosphorylates FGFR2 at pY656/657. Key interaction residues include the 'YRETRRKE' motif of the Sec14p domain and Y471 of PTPN9, as well as the PH and Arf-GAP domains of ACAP1. The FGFR2 I654V substitution decreases PTPN9-FGFR2 interaction. Phosphatase activity assay, structural modeling of PTPN9-FGFR2 complex, co-immunoprecipitation, mutagenesis, patient-derived xenograft models Hepatology High 37505213
2025 PTPN9 dephosphorylates IGF1R preferentially at Y1166 (and Y1165/1166). Crystal structure analysis identified Tyr333 and Asp335 as key PTPN9 residues interacting with IGF1R; mutation of these residues restores IGF1R signaling and abolishes PTPN9's tumor-suppressive effect. PTPN9 expression is inversely correlated with IGF1R Y1165/1166 phosphorylation in clinical tissues. IP-mass spectrometry substrate identification, X-ray crystallography, active-site mutagenesis, orthotopic mouse models, biochemical dephosphorylation assay Journal of experimental & clinical cancer research High 41275311
2024 MEG2 (PTPN9) and PKCε competitively bind to STAT3, with PKCε displaying stronger binding. STAT3 Ser727 phosphorylation increases STAT3 interaction with both PKCε and MEG2. ERK1/2 activation facilitates STAT3 interaction with MEG2, leading to dephosphorylation of STAT3 at Tyr705. MEG2 overexpression inhibits IL-6 promoter activity in the presence of STAT3 and LPS, opposing the effect of PKCε. ELISA and immunoprecipitation for protein-protein interaction, Western blot, dual luciferase reporter assay, in vivo hyperalgesia model (FCA/LPS) FASEB journal Medium 38656553
2018 Heterozygous loss of Meg2 (Ptpn9) in mice causes progressive, age-dependent intraocular pressure elevation and glaucomatous neurodegeneration with retinal ganglion cell loss, optic nerve degeneration, reactive gliosis, and complement activation. IOP lowering with latanoprost prevents RGC loss, establishing the IOP-dependent mechanism. Meg2 heterozygous knockout mice, IOP measurement, ultrastructural analysis, immunohistochemistry, electroretinography, pharmacological rescue with latanoprost Molecular neurobiology Medium 30315478

Source papers

Stage 0 corpus · 46 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2013 MicroRNA miR-24 enhances tumor invasion and metastasis by targeting PTPN9 and PTPRF to promote EGF signaling. Journal of cell science 129 23418360
2016 miR-96 promotes cell proliferation, migration and invasion by targeting PTPN9 in breast cancer. Scientific reports 91 27857177
2012 Protein tyrosine phosphatase Meg2 dephosphorylates signal transducer and activator of transcription 3 and suppresses tumor growth in breast cancer. Breast cancer research : BCR 67 22394684
2010 Protein-tyrosine phosphatase PTPN9 negatively regulates ErbB2 and epidermal growth factor receptor signaling in breast cancer cells. The Journal of biological chemistry 65 20335174
2006 Identification of the tyrosine phosphatase PTP-MEG2 as an antagonist of hepatic insulin signaling. Cell metabolism 53 16679294
2002 Enlargement of secretory vesicles by protein tyrosine phosphatase PTP-MEG2 in rat basophilic leukemia mast cells and Jurkat T cells. Journal of immunology (Baltimore, Md. : 1950) 49 11971009
2012 A highly selective and potent PTP-MEG2 inhibitor with therapeutic potential for type 2 diabetes. Journal of the American Chemical Society 44 23075115
2005 Tyrosine phosphatase MEG2 modulates murine development and platelet and lymphocyte activation through secretory vesicle function. The Journal of experimental medicine 42 16330817
2017 MEG2 is regulated by miR-181a-5p and functions as a tumour suppressor gene to suppress the proliferation and migration of gastric cancer cells. Molecular cancer 39 28747184
2003 PTP-MEG2 is activated in polycythemia vera erythroid progenitor cells and is required for growth and expansion of erythroid cells. Blood 39 12920026
2003 Homotypic secretory vesicle fusion induced by the protein tyrosine phosphatase MEG2 depends on polyphosphoinositides in T cells. Journal of immunology (Baltimore, Md. : 1950) 37 14662869
2001 Protein-tyrosine phosphatase MEG2 is expressed by human neutrophils. Localization to the phagosome and activation by polyphosphoinositides. The Journal of biological chemistry 35 11711529
2008 MEG-1 and MEG-2 are embryo-specific P-granule components required for germline development in Caenorhabditis elegans. Genetics 33 18202375
2003 Specific interaction of protein tyrosine phosphatase-MEG2 with phosphatidylserine. The Journal of biological chemistry 30 12702726
2007 Association of protein-tyrosine phosphatase MEG2 via its Sec14p homology domain with vesicle-trafficking proteins. The Journal of biological chemistry 28 17387180
2002 Purification and characterization of protein tyrosine phosphatase PTP-MEG2. Journal of cellular biochemistry 24 12112018
2021 BMSCs-Derived Exosomal MiR-126-3p Inhibits the Viability of NSCLC Cells by Targeting PTPN9. Journal of B.U.ON. : official journal of the Balkan Union of Oncology 22 34761590
2020 Ropivacaine inhibits cervical cancer cell growth via suppression of the miR‑96/MEG2/pSTAT3 axis. Oncology reports 19 32323811
2016 The Protein Tyrosine Phosphatase MEG2 Regulates the Transport and Signal Transduction of Tropomyosin Receptor Kinase A. The Journal of biological chemistry 19 27655914
2012 Tyrosine phosphatase PTP-MEG2 negatively regulates vascular endothelial growth factor receptor signaling and function in endothelial cells. American journal of physiology. Cell physiology 19 22763125
2018 MiR-613 promotes cell proliferation and invasion in cervical cancer via targeting PTPN9. European review for medical and pharmacological sciences 17 30024598
2019 PTPN9 induces cell apoptosis by mitigating the activation of Stat3 and acts as a tumor suppressor in colorectal cancer. Cancer management and research 16 30804683
2018 MiR-96 enhances cellular proliferation and tumorigenicity of human cervical carcinoma cells through PTPN9. Saudi journal of biological sciences 15 30108433
2014 Protein tyrosine phosphatase PTPN9 regulates erythroid cell development through STAT3 dephosphorylation in zebrafish. Journal of cell science 15 24727614
2023 PTPN9 dephosphorylates FGFR2 pY656/657 through interaction with ACAP1 and ameliorates pemigatinib effect in cholangiocarcinoma. Hepatology (Baltimore, Md.) 14 37505213
2015 Downregulated Expression of PTPN9 Contributes to Human Hepatocellular Carcinoma Growth and Progression. Pathology oncology research : POR 13 26715439
2020 PTPN9-mediated dephosphorylation of VTI1B promotes ATG16L1 precursor fusion and autophagosome formation. Autophagy 12 33112705
2018 Methyllucidone inhibits STAT3 activity by regulating the expression of the protein tyrosine phosphatase MEG2 in DU145 prostate carcinoma cells. Bioorganic & medicinal chemistry letters 12 29456111
2017 PTPN9 promotes cell proliferation and invasion in Eca109 cells and is negatively regulated by microRNA-126. Oncology letters 11 28789358
2011 C. elegans meg-1 and meg-2 differentially interact with nanos family members to either promote or inhibit germ cell proliferation and survival. Genesis (New York, N.Y. : 2000) 10 21305687
2020 The Critical Role of the miR-21-MEG2 Axis in Colorectal Cancer. Critical reviews in eukaryotic gene expression 9 33463918
2018 Heterozygous Meg2 Ablation Causes Intraocular Pressure Elevation and Progressive Glaucomatous Neurodegeneration. Molecular neurobiology 9 30315478
2023 Signature of miR-21 and MEG-2 and their correlation with TGF-β signaling in breast cancer. Human & experimental toxicology 8 36825546
2024 Exploring the Anti-Diabetic Potential of Quercetagitrin through Dual Inhibition of PTPN6 and PTPN9. Nutrients 7 38474775
2021 Phloridzin Acts as an Inhibitor of Protein-Tyrosine Phosphatase MEG2 Relevant to Insulin Resistance. Molecules (Basel, Switzerland) 7 33799458
2021 Effect of L3MBTL3/PTPN9 polymorphisms on risk to alcohol-induced ONFH in Chinese Han population. Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology 7 34373992
2021 PTP-MEG2 regulates quantal size and fusion pore opening through two distinct structural bases and substrates. EMBO reports 6 33764618
2019 Design, synthesis, biological evaluation and molecular dynamics simulation studies of (R)-5-methylthiazolidin-4-One derivatives as megakaryocyte protein tyrosine phosphatase 2 (PTP-MEG2) inhibitors for the treatment of type 2 diabetes. Journal of biomolecular structure & dynamics 6 31402760
2018 MEG2 inhibits the growth and metastasis of hepatocellular carcinoma by inhibiting AKT pathway. Gene 6 30399427
2024 The binding of PKCε and MEG2 to STAT3 regulates IL-6-mediated microglial hyperalgesia during inflammatory pain. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 5 38656553
2021 Tyrosine-Protein Phosphatase Non-receptor Type 9 (PTPN9) Negatively Regulates the Paracrine Vasoprotective Activity of Bone-Marrow Derived Pro-angiogenic Cells: Impact on Vascular Degeneration in Oxygen-Induced Retinopathy. Frontiers in cell and developmental biology 5 34124069
2016 Virtual screening, optimization, and identification of a novel specific PTP-MEG2 Inhibitor with potential therapy for T2DM. Oncotarget 5 27384997
2017 Synthesis, bioactivity, 3D-QSAR studies of novel dibenzofuran derivatives as PTP-MEG2 inhibitors. Oncotarget 3 28388567
2025 PTPN9 promotes melanoma progression by regulating the ferroptosis pathway. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2 39937573
2026 SARS-CoV-2 Main Protease Activates ERK1/2 Signaling to Facilitate MEG2-STAT3-Mediated Suppression of ACE2. Journal of medical virology 0 41728757
2025 PTPN9 dephosphorylates IGF1RY1165/1166 and alleviates IGF1R-mediated resistance to tyrosine kinase inhibitor in cholangiocarcinoma. Journal of experimental & clinical cancer research : CR 0 41275311