Affinage

PEA15

Astrocytic phosphoprotein PEA-15 · UniProt Q15121

Length
130 aa
Mass
15.0 kDa
Annotated
2026-06-10
100 papers in source corpus 43 papers cited in narrative 43 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

PEA-15 (PED/PEA-15) is a small cytoplasmic death effector domain (DED) adapter that acts as a phosphorylation-gated hub coordinating MAP kinase signaling, apoptosis, and glucose metabolism (PMID:11702783, PMID:15916534). Through its DED and C-terminal tail it is a high-affinity bidentate ligand of ERK1/2, engaging the D-recruitment site together with the MAP kinase insert region to form a 1:1 complex; this anchors ERK in the cytoplasm via a nuclear export sequence, blocks ERK–nucleoporin interactions and nuclear entry, competes with D-site substrates such as Elk-1 and Ets-1, and protects bound ERK2 from dephosphorylation (PMID:11702783, PMID:14707138, PMID:17658892, PMID:21506533, PMID:23575685). Loss of PEA-15 raises nuclear phospho-ERK, cFos transcription and proliferation, and PEA-15 restrains tumor cell invasion and Ras-induced senescence escape through this ERK-tethering activity (PMID:11702783, PMID:15331596, PMID:17308092). PEA-15 also scaffolds ERK onto RSK2 to control CREB-dependent transcription (PMID:12796492, PMID:18077417). In parallel, the DED binds FADD and caspase-8, displacing their interaction at the death-inducing signaling complex to block extrinsic (TNFα, FasL, TRAIL) apoptosis, a function confirmed by increased death of PEA-15-null astrocytes (PMID:10442631, PMID:10493725, PMID:15545353). In metabolism, PEA-15 binds the C-terminal D4 domain of PLD1, driving constitutive PKC-α activation that inhibits insulin-responsive PKC-ζ and impairs GLUT4 recruitment and glucose uptake; transgenic overexpression causes diabetes by impairing both insulin action and glucose-stimulated insulin secretion (PMID:9670003, PMID:11375323, PMID:18541525, PMID:15143191, PMID:17327429). These outputs are switched by phosphorylation: PKC phosphorylates Ser104 to block ERK binding, while CaMKII, Akt, or AMPK phosphorylate Ser116 to promote FADD binding, anti-apoptotic function, and stabilization against ubiquitin- and chaperone-mediated degradation, and DUSP7 dephosphorylation reverses this switch (PMID:8449955, PMID:9721757, PMID:12808093, PMID:15916534, PMID:25096718, PMID:24477641, PMID:34907034).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 1993 High

    Established PEA-15 as a defined PKC phosphoprotein, providing the first regulatory handle before any function was known.

    Evidence In vitro kinase assay with purified PKC, 2D phosphopeptide mapping in astrocytes

    PMID:8449955

    Open questions at the time
    • Functional consequence of PKC phosphorylation not yet defined
    • Site not yet mapped to Ser104
  2. 1998 High

    Identified a second, CaMKII-targeted site (Ser116) distinct from the PKC site, revealing dual-site control of PEA-15.

    Evidence Phosphopeptide microsequencing from endothelin-treated astrocytes plus in vitro CaMKII assay

    PMID:9721757

    Open questions at the time
    • Downstream effect of each site on partner binding not yet established
  3. 1998 High

    Connected PEA-15 to glucose metabolism, showing it inhibits insulin-stimulated glucose transport upstream of PKC.

    Evidence Stable overexpression in L6 muscle cells, glucose transport/GLUT4 assays with PKC inhibitor rescue

    PMID:9670003

    Open questions at the time
    • Direct PEA-15 binding partner mediating PKC activation not yet identified
    • In vivo relevance not yet tested
  4. 1999 High

    Defined the anti-apoptotic mechanism: PEA-15 DED binds FADD and caspase-8 to disrupt DISC assembly, and genetic loss sensitizes cells to death.

    Evidence Reciprocal co-IP in MCF-7/HeLa, PARP cleavage assays, and PEA-15-null astrocyte survival assays

    PMID:10442631 PMID:10493725

    Open questions at the time
    • Phosphorylation dependence of FADD binding not yet resolved
  5. 2001 High

    Established the canonical ERK-sequestration function: PEA-15 anchors ERK1/2 in the cytoplasm via a nuclear export sequence to restrain transcription and proliferation.

    Evidence PEA-15 knockout cells, NES mutant, ERK localization imaging, cFos reporter and proliferation assays

    PMID:11702783

    Open questions at the time
    • Molecular basis of ERK binding interface not yet defined
    • Mechanism of nuclear-entry blockade unresolved
  6. 2002 High

    Solved the PEA-15 structure and mapped ERK-binding residues, revealing a DED docking mode shared with death domains.

    Evidence NMR structure determination, chemical-shift footprinting, ERK-binding mutagenesis

    PMID:12456656

    Open questions at the time
    • Atomic detail of the bound ERK2 complex not yet available
  7. 2003 High

    Identified Akt as a direct Ser116 kinase that stabilizes PEA-15 against proteasomal degradation, coupling survival signaling to protein abundance.

    Evidence In vitro Akt kinase assay, S116G mutant, pulse-chase stability, phospho-specific antibody

    PMID:12808093

    Open questions at the time
    • E3 ligase mediating ubiquitination not identified
  8. 2004 High

    Resolved the nuclear-entry blockade mechanism: PEA-15 and nucleoporins compete for the ERK2 MAP kinase insert region.

    Evidence Permeabilized-cell nuclear import assay with ERK2 insert mutants and nucleoporin binding assays

    PMID:14707138

    Open questions at the time
    • Whether this fully accounts for cytoplasmic retention versus NES-mediated export not delineated
  9. 2007 High

    Quantified PEA-15 as a high-affinity bidentate ERK ligand at the D-recruitment site that competes with D-site substrates, explaining transcriptional inhibition.

    Evidence Fluorescence anisotropy binding, alkylation protection, in vitro kinase competition with Elk-1/Ets-1

    PMID:17658892

    Open questions at the time
    • Structural basis of the bidentate mode not yet visualized
  10. 2007 High

    Reframed PEA-15 as a positive ERK scaffold that targets ERK to RSK2, showing it both sequesters and routes ERK.

    Evidence Co-IP, in vitro binding, RSK2 kinase and CREB reporter assays, PEA-15-null lymphocyte rescue

    PMID:12796492 PMID:18077417

    Open questions at the time
    • How phosphorylation toggles between sequestration and scaffolding not fully resolved
  11. 2007 High

    Defined the metabolic mechanism in vivo and at the binding level: PED/PEA-15 binds the PLD1 D4 domain to drive PKC-α–dependent PKC-ζ inhibition, causing diabetes.

    Evidence SPR binding, peptide competition rescue, PED transgenic and null mice, islet GSIS and PKC isoform assays

    PMID:11375323 PMID:15143191 PMID:17327429 PMID:18541525

    Open questions at the time
    • Detailed signaling between PLD1 binding and PKC-α activation not fully mapped
  12. 2005 High

    Articulated the phosphorylation switch: Ser104 phosphorylation blocks ERK binding while Ser116 promotes FADD binding, partitioning PEA-15 between proliferation and apoptosis without changing its cytoplasmic distribution.

    Evidence Phosphomimetic/non-phosphorylatable mutants, in vitro binding, co-IP, fractionation, ERK reporter and integrin assays

    PMID:15916534 PMID:15917297

    Open questions at the time
    • Spatiotemporal coordination of the two kinases in vivo not resolved
  13. 2013 High

    Provided atomic-resolution insight into ERK regulation: PEA-15 occupies both the D-recruitment and DEF-binding sites, allosterically disrupting active ERK2 and shielding it from dephosphorylation.

    Evidence X-ray crystallography of PEA-15/ERK2 in three phospho-conformations; stoichiometry by light scattering/AUC

    PMID:21506533 PMID:23575685

    Open questions at the time
    • How allosteric inhibition reconciles with protection from dephosphorylation mechanistically not fully explained
  14. 2014 High

    Extended kinase control to AMPK and revealed chaperone-mediated autophagy as a second degradation route gated by phosphorylation.

    Evidence In vitro AMPK kinase assay and S116A mutant in mammospheres; TAP/HSC70 CMA substrate and KFERQ-motif mutagenesis

    PMID:24477641 PMID:25096718

    Open questions at the time
    • Relative contributions of proteasomal versus CMA turnover in vivo not quantified
  15. 2022 Medium

    Identified DUSP7 as the phosphatase reversing the PEA-15 switch, linking it to drug-resistance signaling downstream of FOSL1.

    Evidence ChIP, siRNA epistasis, phospho-PEA15 Western blot, doxorubicin resistance assays

    PMID:34907034

    Open questions at the time
    • Single lab; site specificity of DUSP7 dephosphorylation not mapped
    • Direct phosphatase–substrate contact not structurally defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the competing PEA-15 outputs (ERK sequestration vs. RSK2/PLD1 scaffolding vs. DISC inhibition) are spatially and temporally integrated within a single cell remains unresolved.
  • No unified model of how a single low-abundance adapter partitions among mutually exclusive partner pools
  • Endogenous stoichiometry of PEA-15 versus ERK, FADD and PLD1 not determined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 4 GO:0060090 molecular adaptor activity 3 GO:0140313 molecular sequestering activity 3
Localization
GO:0005829 cytosol 2
Pathway
R-HSA-1430728 Metabolism 4 R-HSA-162582 Signal Transduction 3 R-HSA-5357801 Programmed Cell Death 3
Partners
AKT1CASP8DUSP7FADDMAPK1PLD1PRKAA1RPS6KA3
Complex memberships
death-inducing signaling complex (DISC)

Evidence

Reading pass · 43 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1993 PEA-15 is a major substrate for protein kinase C (PKC) in astrocytes. In vitro phosphorylation by purified PKC occurs at a consensus site (LTRIPSAKK), and two-dimensional peptide mapping confirmed the same site is phosphorylated in intact cells. PKC mediates the transition from the less acidic (Pa) to the more acidic (Pb) isoelectric form of PEA-15. In vitro kinase assay with purified PKC, 2D gel electrophoresis, 2D phosphopeptide mapping, partial microsequencing, [32P] labeling of intact astrocytes The Journal of biological chemistry High 8449955
1998 Endothelin-1 stimulation of astrocytes induces phosphorylation of PEA-15 at two distinct sites: Ser104 (the previously identified PKC site) and a novel site Ser116, phosphorylated by calcium/calmodulin-dependent protein kinase II (CaMKII) but not by casein kinase II. CaMKII phosphorylation of Ser116 in vitro facilitates subsequent PKC phosphorylation at Ser104. Microsequencing of phosphopeptides from endothelin-treated astrocytes, in vitro kinase assay with partly purified CaMKII, 2D phosphopeptide mapping, okadaic acid treatment Journal of neurochemistry High 9721757
1998 PEA-15 overexpression in L6 skeletal muscle cells increases plasma membrane GLUT1 content and inhibits insulin-stimulated glucose transport and cell-surface GLUT4 recruitment. These effects are reversed by PKC inhibition, placing PEA-15 upstream of PKC in glucose transport regulation. Stable transfection of L6 cells, glucose transport assay, surface GLUT4 measurement, PKC inhibitor rescue The EMBO journal High 9670003
1998 The death effector domain (DED) of PEA-15 is required for its ability to block Ras-mediated suppression of integrin activation. PEA-15 acts through a pathway involving the small GTPase R-Ras (blocked by dominant-negative R-Ras) rather than by blocking ERK MAP kinase activation downstream of Ras. Expression cloning, dominant-negative R-Ras rescue, integrin activation assay, DED deletion mutant analysis The Journal of biological chemistry Medium 9852038
1999 PEA-15 binds to FADD and FLICE (caspase-8) through its death effector domain, displacing FADD-FLICE interaction and thereby blocking TNFα- and FasL-induced apoptosis. Overexpression of a FADD DED-deletion mutant blocked PEA-15–FLICE association, and TNFα reduced PEA-15 association with endogenous FADD and FLICE. Co-immunoprecipitation from MCF-7 and HeLa cell lysates, PARP cleavage assay for FLICE (caspase-8) activity, DED-deletion mutant FADD overexpression Oncogene High 10442631
1999 PEA-15 knockout in mice demonstrates that endogenous PEA-15 expression protects astrocytes from TNFα-induced apoptosis in vitro. PEA-15 null astrocytes show increased death after TNFα exposure, and in vitro assays confirm PEA-15 binding to FADD and caspase-8 as the mechanistic basis. PEA-15 null mutant mouse generation, in vitro astrocyte apoptosis assay, in vitro binding assays for FADD and caspase-8 The Journal of neuroscience High 10493725
2000 PEA-15 activates the ERK MAP kinase pathway in a Ras-dependent manner: PEA-15 expression in CHO cells increases Ras GTP loading, MEK and ERK activity, and bypasses the anchorage-dependence of ERK activation. The DED of PEA-15 is required for this ERK-activating function. ERK/MEK kinase assays, Ras-GTP pull-down, anchorage-independent ERK activation assay, DED deletion mutant analysis in CHO cells Molecular biology of the cell Medium 10982386
2000 PEA-15 interacts with phospholipase D1 (PLD1) and PLD2. The PLD1-interacting site on PEA-15 encompasses part of the DED plus C-terminal flanking sequences, overlapping the RhoA-interacting site on PLD1. PEA-15 co-expression increases PLD1 protein expression levels (faster accumulation, longer persistence) without directly affecting PLD1 enzymatic activity, suggesting PEA-15 acts as a PLD chaperone/stabilizer. Yeast two-hybrid screen, co-immunoprecipitation, in vitro PLD activity assay, co-expression stability analysis The Journal of biological chemistry Medium 10926929
2001 PEA-15 mediates cytoplasmic sequestration of ERK1/2 MAP kinases by binding ERKs and preventing their nuclear localization. PEA-15 contains a nuclear export sequence required for cytoplasmic ERK anchoring. Genetic deletion of PEA-15 results in increased ERK nuclear localization, increased cFos transcription, and increased cell proliferation. PEA-15 knockout mouse cells, nuclear export sequence mutant, ERK localization imaging, cFos reporter assay, cell proliferation assay Developmental cell High 11702783
2001 In L6 skeletal muscle cells overexpressing PED/PEA-15, PKC-α and PKC-β are constitutively activated and inhibit PKC-ζ insulin responsiveness. Blockade of PKC-α (more effectively than PKC-β) restores insulin activation of PKC-ζ and glucose uptake. Thus, PED/PEA-15 action on glucose transport is mediated through PKC-α–dependent inhibition of PKC-ζ. PKC isoform blockade (pharmacological and dominant-negative), 2-deoxyglucose uptake assay, PKC-ζ activity measurement in L6(PED) cells Diabetes Medium 11375323
2002 PEA-15 controls the activity of ERK, JNK, and p38 subfamilies of MAPKs. PED/PEA-15 simultaneously activates ERK1/2 and inhibits JNK/p38 signaling (by impairing Cdc-42, MKK4, MKK6 activation). The anti-apoptotic function of PED requires both ERK activation and JNK/p38 inhibition. 293 cell transfection, kinase phosphorylation assays, MEK inhibitor (PD98059) epistasis, JNK1 and p38 overexpression rescue, apoptosis assays The Journal of biological chemistry Medium 11790785
2002 The three-dimensional structure of PEA-15 was determined by NMR spectroscopy: PEA-15 consists of an N-terminal death effector domain (DED) and a C-terminal tail of irregular structure. NMR footprinting and mutagenesis identified residues in both the DED and C-terminal tail required for ERK binding. The DED surface used by PEA-15 to bind ERK2 is similar to the death domain (DD) surface used by Drosophila Tube, revealing an unexpected common docking mode. NMR structure determination, NMR chemical shift footprinting, site-directed mutagenesis of ERK-binding residues The EMBO journal High 12456656
2002 Only the doubly phosphorylated form of PED/PEA-15 is recruited to the TRAIL death-inducing signaling complex (DISC) in TRAIL-resistant glioma cells. CaMK inhibitor treatment rescues TRAIL sensitivity, indicating that CaMK-dependent phosphorylation of PEA-15 is required for its DISC recruitment and TRAIL resistance. DISC immunoprecipitation from TRAIL-sensitive and -resistant glioma cells, Western blot with phospho-specific antibodies, CaMK inhibitor treatment The Journal of biological chemistry Medium 11976344
2003 Protein kinase B/Akt directly binds PEA-15 (independently of Akt activity) and phosphorylates it at Ser116. Akt phosphorylation of Ser116 stabilizes PEA-15 by reducing its ubiquitin-dependent proteasomal degradation. A nonphosphorylatable S116G mutant showed 10-fold reduced Akt phosphorylation, a 3-fold higher degradation rate, and ~2-fold reduced anti-apoptotic activity. In vitro kinase assay with recombinant Akt and PEA-15, phospho-Ser116-specific antibodies, pull-down and co-immunoprecipitation, S116G point mutant, pulse-chase stability assay Molecular and cellular biology High 12808093
2003 PEA-15 binds RSK2 (but not RSK1) through its C-terminal tail, not the DED. This interaction inhibits RSK2 kinase activity by ~50%, blocks nuclear accumulation of RSK2 after EGF stimulation, and suppresses RSK2-dependent CREB transcription and histone H3 phosphorylation. PEA-15 does not alter ERK phosphorylation of RSK2 and is not itself an RSK2 substrate. Co-immunoprecipitation, in vitro binding with translated RSK2, RSK2 kinase assay, nuclear localization imaging, CREB reporter assay, histone H3 phosphorylation assay, C-terminal deletion analysis The Journal of biological chemistry High 12796492
2004 PEA-15 prevents nuclear entry of ERK2 by interfering with ERK2–nucleoporin interactions. The MAP kinase insert region of ERK2 is required for both PEA-15 binding and nucleoporin binding. In a permeabilized cell system, excess PEA-15 blocked wild-type ERK2 nuclear entry but not MAP kinase insert-deleted ERK2. Permeabilized cell nuclear import assay, ERK2/p38 chimeras and MAP kinase insert mutants, nucleoporin binding assay, ERK2 localization The Journal of biological chemistry High 14707138
2004 Pro-apoptotic Omi/HtrA2 mitochondrial serine protease directly binds the DED of PED/PEA-15 and degrades it. Upon UVC exposure, Omi/HtrA2 is released from mitochondria into the cytoplasm, binds PED/PEA-15, and proteolytically degrades it; specific Omi inhibitor ucf-101 prevents this degradation. PED/PEA-15 in turn blocks Omi/HtrA2 co-precipitation with XIAP, modulating caspase-3 activation. Yeast two-hybrid screen, in vitro binding and in vitro degradation assay, co-immunoprecipitation, ucf-101 inhibitor treatment, caspase-3 activity assay The Journal of biological chemistry High 15328349
2004 High expression of PED/PEA-15 in primitive neural stem/progenitor cells localizes to the death-inducing signaling complex (DISC) and prevents caspase-8 recruitment and activation, providing protection from death receptor–induced apoptosis. Lentiviral antisense knockdown of PED sensitizes these cells to apoptosis by inflammatory cytokines and death receptors. DISC immunoprecipitation, lentiviral antisense PED knockdown, caspase-8 activation assay, neural stem cell apoptosis assay The Journal of experimental medicine High 15545353
2004 PEA-15 promotes cytoplasmic ERK localization during oncogenic Ras-induced cellular senescence. RNAi-mediated knockdown of PEA-15 in Ras-expressing primary mouse embryo fibroblasts restores nuclear phospho-ERK localization and promotes escape from senescence, indicating PEA-15 acts as a nuclear export factor for ERK1/2 in this context. RNA interference against PEA-15, ERK localization imaging by immunofluorescence, Ras-induced senescence assay, E1A downregulation of PEA-15 (Western blot) The Journal of biological chemistry Medium 15331596
2004 PED/PEA-15 overexpression in transgenic mice causes diabetes by impairing both insulin action and glucose-stimulated insulin secretion. In muscle and fat, PED overexpression activates PKC-α and blocks insulin induction of PKC-ζ; in beta-cells, it blocks PKC-ζ induction by glucose, reducing expression of Sur1, Kir6.2 potassium channel subunits and their regulator Foxa2. PED transgenic mice, in vivo glucose/insulin tolerance tests, isolated adipocyte glucose uptake, PKC isoform activity assays, MIN6 beta-cell stable overexpression, antisense knockdown Molecular and cellular biology High 15143191
2005 Phosphorylation of PEA-15 at Ser104 blocks ERK binding in vitro and in vivo, whereas phosphorylation at Ser116 promotes FADD binding. These phosphorylation events act as a molecular switch determining whether PEA-15 engages the proliferation (ERK) or apoptosis (FADD) pathway. All phosphorylation states of PEA-15 remain predominantly cytoplasmic, so phosphorylation does not influence nuclear versus cytoplasmic distribution. In vitro binding assays with phosphomimetic and non-phosphorylatable mutants, co-immunoprecipitation from cells, phospho-epitope antibody characterization, subcellular fractionation The Biochemical journal High 15916534
2005 Phosphorylation of both Ser104 and Ser116 is required to block PEA-15 interaction with ERK1/2. Using phosphomimetic and non-phosphorylatable PEA-15 mutants, dual phosphorylation abrogates PEA-15-mediated inhibition of ERK nuclear localization and transcriptional activity, thus enabling cell proliferation. PEA-15 phosphorylation also modulates non-transcriptional ERK effects on integrin activation. Phosphomimetic (S104D/S116D) and non-phosphorylatable (S104A/S116A) mutants, in vitro binding, ERK nuclear localization assay, Elk-1/cFos reporter assay, integrin activation assay, phospho-specific antibody in situ staining Molecular biology of the cell High 15917297
2003 PEA-15 reversal of Raf-1-mediated integrin suppression depends on its capacity to bind ERK1/2. Mutations in either the DED or C-terminal tail that block ERK1/2 binding abolish integrin suppression reversal. ERK1/2 residues preceding the αG helix and within the MAP kinase insert are required for PEA-15 binding and are also required for ERK2 to suppress integrin activation. Membrane-targeted ERK1/2-CAAX suppresses integrin activation in a manner not reversible by PEA-15. ERK2/p38 chimeras, site-directed mutagenesis of ERK2, membrane-targeted ERK1/2-CAAX constructs, integrin activation assay, co-immunoprecipitation The Journal of biological chemistry Medium 14506247
2007 PEA-15 inhibits tumor cell invasion by binding ERK1/2 and preventing their nuclear localization. PEA-15 mutants that cannot bind ERK1/2 fail to inhibit invasion; overexpression of ERK1 or activated MEK reverses PEA-15-mediated invasion inhibition; a PEA-15 mutant that cannot prevent ERK nuclear localization does not inhibit invasion. shRNA-mediated PEA-15 knockdown, forced overexpression, ERK1/2-binding mutants of PEA-15, ERK1/MEK overexpression rescue, invasion assay, ERK nuclear localization imaging Cancer research Medium 17308092
2007 PEA-15 acts as a scaffold that targets ERK to RSK2 by simultaneously binding both proteins, thereby enhancing ERK-mediated RSK2 activation and CREB transcription. This scaffolding activity is regulated by PEA-15 phosphorylation. In PEA-15-null lymphocytes, phorbol ester-stimulated RSK2 activation is impaired and rescued by exogenous PEA-15. Co-immunoprecipitation, in vitro binding, RSK2 kinase assay, CREB reporter assay, PEA-15-null lymphocyte rescue experiment Proceedings of the National Academy of Sciences of the United States of America High 18077417
2007 PEA-15 is a high-affinity ligand for both ERK1 and ERK2 (Kd ~0.2–0.4 μM regardless of ERK activation state). PEA-15 binds at the D-recruitment site (DRS) of ERK1/2 (likely via its C-terminus) in a bidentate manner also involving the MAP kinase insert. PEA-15 competes with D-site-containing substrates (Elk-1, Ets-1) and potently inhibits ERK2-mediated phosphorylation of these transcription factors. Neither PEA-15 phosphorylation nor ERK1/2 activation state significantly affects binding affinity. Fluorescence anisotropy binding assay, competition assay with Elk-1 D-site peptide, single-cysteine ERK2 alkylation protection assay, in vitro ERK2 kinase assay with Elk-1 and Ets-1 Biochemistry High 17658892
2007 PED/PEA-15 overexpression in pancreatic beta-cells inhibits PKC-ζ induction by glucose, thereby reducing expression of potassium channel subunits Sur1, Kir6.2 and Foxa2 and impairing glucose-stimulated insulin secretion. Rescue of PKC-ζ activity in PED-overexpressing beta-cells restores channel gene expression and insulin secretion. PED/PEA-15-null mouse islets show increased PKC-ζ activation and enhanced insulin secretion. Beta-cell-specific PED transgenic mice, islet isolation, glucose-stimulated insulin secretion assay, PKC-ζ activity assay, mRNA quantification of Sur1/Kir6.2/Foxa2, MIN-6 and INS-1 cell overexpression/antisense knockdown Diabetes High 17327429
2007 TPA (phorbol ester) increases PED/PEA-15 cellular levels post-translationally by inducing phosphorylation at Ser116 via a PKC-ζ/CaMKII pathway that prevents ubiquitinylation and proteasomal degradation of PED/PEA-15. The S116G mutant abolishes TPA-mediated protection from ubiquitin-dependent degradation. Ubiquitin co-immunoprecipitation, proteasome inhibitor (lactacystin) treatment, PKC-ζ dominant-negative and antisense, CaMK inhibitor (KN-93), S116G and S104G mutants, pulse-chase protein stability The Journal of biological chemistry High 17227770
2008 PED/PEA-15 binds the C-terminal D4 domain of PLD1 with high affinity (Kd ~0.37 μM). A peptide spanning PED residues 1–24 competes with this interaction. Disrupting PED/PEA-15–PLD1 binding in L6 skeletal muscle cells overexpressing PED abolishes the PED-induced PKC-α activation and restores insulin-stimulated glucose uptake by ~70%. Surface plasmon resonance, ELISA-like binding assay, peptide competition in cells and transgenic mouse-derived myocytes, PKC-α activity assay, 2-deoxyglucose uptake assay The Journal of biological chemistry High 18541525
2010 PEA-15 promotes autophagy in glioma cells in a JNK-dependent manner. Overexpression of PEA-15 potently activates JNK; this activation depends on phosphorylation at both Ser104 and Ser116. JNK inhibition abrogates PEA-15-mediated autophagy induction. Non-phosphorylatable PEA-15 mutants fail to promote autophagy. PEA-15 overexpression in glioma cells, siRNA knockdown, JNK phosphorylation assay, autophagy markers (LC3), JNK inhibitor treatment, phosphorylation-site mutant analysis The Journal of biological chemistry Medium 20452983
2011 Activated ERK2 forms a 1:1 monomeric complex with PEA-15 (~57 kDa by light scattering); ERK2 itself does not dimerize under physiological conditions with or without divalent cations. This confirms the PEA-15–ERK2 interaction is a 1:1 stoichiometric complex. Static light scattering, analytical ultracentrifugation (sedimentation equilibrium and velocity), dynamic light scattering, NMR diffusion measurement Biochemistry High 21506533
2011 Hsp27 regulates PEA-15 activity through Akt: Hsp27 silencing decreases Akt-mediated phosphorylation of PEA-15, causing PEA-15 to bind and sequester ERK (inhibiting proliferation) while releasing FADD (enabling Fas-induced apoptosis). Hsp27 overexpression promotes proliferation and suppresses Fas-induced apoptosis via the same PEA-15 molecular switch. Hsp27 siRNA silencing and overexpression, Akt inhibition, co-immunoprecipitation of PEA-15 with ERK and FADD, ERK nuclear localization assay, Fas-induced apoptosis assay, cell proliferation assay Cell death and differentiation Medium 22179576
2012 Hexokinase II (HKII) directly interacts with PEA-15 and together they inhibit apoptosis after hypoxia. Under glucose deprivation (normoxia), HKII accelerates apoptosis in the absence of PEA-15, demonstrating that HKII acts as a metabolic sensor and that its pro-survival vs. pro-apoptotic output is gated by PEA-15. Co-immunoprecipitation of HKII and PEA-15, siRNA knockdown of PEA-15, hypoxia/glucose deprivation apoptosis assays, HKII overexpression Proceedings of the National Academy of Sciences of the United States of America Medium 22233811
2012 PED/PEA-15 induces autophagy and mediates TGF-β1-driven inhibition of skeletal muscle cell differentiation through a PP2A/FoxO1 mechanism. TGF-β1 transcriptionally upregulates PED/PEA-15; specific PED/PEA-15 shRNAs block both TGF-β1-induced autophagy and impaired differentiation. PED/PEA-15 overexpressing transgenic mice show atrophic muscle fibers with increased LC3II/LC3I and reduced PP2A/FoxO1 phosphorylation. TGF-β1 treatment of myoblasts, PED/PEA-15 shRNA, autophagy inhibitor (3-methyladenine), transgenic mouse muscle analysis (LC3, FoxO1 phosphorylation), myotube differentiation assay Cell death and differentiation Medium 22281705
2012 PED/PEA-15 interacts with the 67 kDa laminin receptor (67LR/37LRP). This interaction was confirmed by yeast two-hybrid, pull-down with recombinant His-tagged 37LRP, and co-immunoprecipitation. 67LR-mediated laminin signaling induces phosphorylation of PED/PEA-15 at both Ser104 and Ser116, enabling cell proliferation and apoptosis resistance. Yeast two-hybrid screen, recombinant His-tag pull-down, co-immunoprecipitation, cell adhesion/migration assay on laminin, phospho-specific Western blot Journal of cellular and molecular medicine Medium 21895963
2013 Crystal structures of PEA-15 bound to three different ERK2 phospho-conformers reveal a bipartite binding mode: PEA-15 occupies both the D-recruitment site (DRS) and the DEF-binding site (DBS) of ERK2. PEA-15 can bind the ERK2 activation loop in the Thr-X-Tyr region in different phosphorylation states. Dually phosphorylated ERK2 bound by PEA-15 undergoes allosteric disruption of active-conformation features, while PEA-15 protects ERK2 from dephosphorylation. X-ray crystallography of PEA-15/ERK2 complexes in three phospho-conformations, structural analysis of allosteric changes Nature communications High 23575685
2014 AMPK directly phosphorylates PEA-15 at Ser116. In mammary cells forming mammospheres, AMPK activity increases and phosphorylates PEA-15 at Ser116, promoting its anti-apoptotic function. AMPK or PEA-15 knockdown, or overexpression of the non-phosphorylatable S116A PEA-15 mutant, impairs mammosphere formation and anoikis resistance. In vitro AMPK kinase assay with PEA-15 substrate, immunoprecipitation of AMPK-PEA-15 complex, shRNA knockdown, S116A PEA-15 mutant overexpression, mammosphere and xenograft assays Breast cancer research : BCR High 25096718
2014 PED/PEA-15 is degraded via chaperone-mediated autophagy (CMA) through interaction with HSC70. PED has two KFERQ-like CMA targeting motifs; phosphorylation at the motif overlapping a phosphorylation site prevents HSC70 from accessing it, thus blocking CMA-mediated degradation. Unphosphorylated PED is preferentially targeted by HSC70 to lysosomes. Tandem affinity purification identifying HSC70 as PED interactor, CMA substrate assay, KFERQ motif mutagenesis, lysosomal fractionation, phospho-mimetic and non-phosphorylatable PED mutants Journal of cellular physiology Medium 24477641
2011 PEA-15 potentiates H-Ras-mediated epithelial cell transformation through activation of its binding partner PLD1. In H-Ras-transformed cells, PEA-15 co-expression enhances ERK activation, G1/S cell cycle progression, anchorage-independent growth and tumor growth in vivo. Inhibition of PLD1 or disruption of PEA-15/PLD1 binding blocks these PEA-15-mediated oncogenic effects. Soft agar colony formation, in vivo tumor xenograft, PLD1 inhibition, PEA-15/PLD1 binding interference, ERK activity assay, cell cycle analysis Oncogene Medium 22105357
2010 PED/PEA-15 interacts with Rac1 GTPase and facilitates AKT-mediated Rac1-Ser71 phosphorylation. Constitutively active Rac affects PED-Ser104 phosphorylation. PED augments migration and invasion in NSCLC cells in a Rac1-dependent manner, with effects mediated through the ERK1/2 pathway. Tandem affinity purification (TAP) identifying Rac1, co-immunoprecipitation, Rac1 siRNA and pharmacological inhibition, migration/invasion assay, phosphorylation analysis Journal of cellular physiology Medium 20648624
2012 PED/PEA-15 overexpression in fibroblasts impairs cell motility and wound closure through ERK1/2-dependent suppression of RhoA activation. TgPED fibroblasts show increased phospho-ERK1/2, decreased RhoA activation, reduced stress fibers and focal adhesions. ERK1/2 inhibition (PD98059) rescues RhoA activation and restores motility. PED-null fibroblasts show accelerated wound closure in vitro and in vivo. Transgenic and knockout mouse fibroblasts, scratch wound assay, time-lapse migration, RhoA activation assay, ERK inhibitor rescue, in vivo dorsal wound healing Journal of cellular physiology Medium 21780113
2015 PEA-15 is under integrin α5β1/AKT control. Inhibition of α5β1 integrin decreases PEA-15 levels, which in turn activates the p53 pathway to repress survivin; conversely, survivin repression decreases α5β1 integrin expression. This interconnection creates a pro-apoptotic loop in glioma cells. siRNA knockdown of PEA-15 and survivin, integrin-blocking antibodies and RGD antagonists, Western blot, caspase-8/3 activity assay, Nutlin-3a treatment Cell death and differentiation Medium 26470725
2022 DUSP7 (dual specificity phosphatase 7), transcriptionally induced by FOSL1, directly dephosphorylates PEA15. FOSL1 promotes drug resistance in breast cancer through DUSP7-mediated dephosphorylation of PEA15, shifting PEA15 from tumor-suppressor to pro-survival function. qRT-PCR, ChIP for FOSL1 binding to DUSP7 promoter, siRNA knockdown of FOSL1/DUSP7, Western blot of phospho-PEA15, doxorubicin resistance assays in vitro and in vivo Molecular cancer research : MCR Medium 34907034

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase. Developmental cell 271 11702783
2002 Tumor necrosis factor-related apoptosis-inducing ligand-induced death-inducing signaling complex and its modulation by c-FLIP and PED/PEA-15 in glioma cells. The Journal of biological chemistry 159 11976344
1998 PED/PEA-15 gene controls glucose transport and is overexpressed in type 2 diabetes mellitus. The EMBO journal 135 9670003
1999 PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis. Oncogene 134 10442631
1993 Characterization of PEA-15, a major substrate for protein kinase C in astrocytes. The Journal of biological chemistry 131 8449955
2003 Protein kinase B/Akt binds and phosphorylates PED/PEA-15, stabilizing its antiapoptotic action. Molecular and cellular biology 127 12808093
1999 Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNFalpha-induced apoptosis. The Journal of neuroscience : the official journal of the Society for Neuroscience 125 10493725
2010 miR-212 increases tumor necrosis factor-related apoptosis-inducing ligand sensitivity in non-small cell lung cancer by targeting the antiapoptotic protein PED. Cancer research 112 20388802
2014 Mitochondrial oxidative phosphorylation TRAP(1)ped in tumor cells. Trends in cell biology 111 24731398
2021 PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins. Nucleic acids research 105 33305318
2009 Precision extruding deposition (PED) fabrication of polycaprolactone (PCL) scaffolds for bone tissue engineering. Biofabrication 100 20811098
1995 Cellular expression, developmental regulation, and phylogenic conservation of PEA-15, the astrocytic major phosphoprotein and protein kinase C substrate. Journal of neurochemistry 97 7861130
1987 Analysis of Qa-2 antigen expression by preimplantation mouse embryos: possible relationship to the preimplantation-embryo-development (Ped) gene product. Biology of reproduction 95 3593833
2005 Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD. The Biochemical journal 94 15916534
2004 Absence of caspase 8 and high expression of PED protect primitive neural cells from cell death. The Journal of experimental medicine 93 15545353
2002 Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain. The EMBO journal 88 12456656
1998 The death effector domain of PEA-15 is involved in its regulation of integrin activation. The Journal of biological chemistry 81 9852038
1998 Endothelin induces a calcium-dependent phosphorylation of PEA-15 in intact astrocytes: identification of Ser104 and Ser116 phosphorylated, respectively, by protein kinase C and calcium/calmodulin kinase II in vitro. Journal of neurochemistry 78 9721757
2003 Evidence that HLA-G is the functional homolog of mouse Qa-2, the Ped gene product. Human immunology 74 14602227
2013 Structure of ERK2 bound to PEA-15 reveals a mechanism for rapid release of activated MAPK. Nature communications 73 23575685
2004 Omi/HtrA2 promotes cell death by binding and degrading the anti-apoptotic protein ped/pea-15. The Journal of biological chemistry 72 15328349
2009 Frontiers: PED/PEA-15, a multifunctional protein controlling cell survival and glucose metabolism. American journal of physiology. Endocrinology and metabolism 70 19531639
2004 The death effector domain protein PEA-15 prevents nuclear entry of ERK2 by inhibiting required interactions. The Journal of biological chemistry 70 14707138
2003 The multifunctional protein PEA-15 is involved in the control of apoptosis and cell cycle in astrocytes. Biochemical pharmacology 68 14555237
2005 Phosphorylation of phosphoprotein enriched in astrocytes (PEA-15) regulates extracellular signal-regulated kinase-dependent transcription and cell proliferation. Molecular biology of the cell 67 15917297
2012 Mitochondrial hexokinase II (HKII) and phosphoprotein enriched in astrocytes (PEA15) form a molecular switch governing cellular fate depending on the metabolic state. Proceedings of the National Academy of Sciences of the United States of America 62 22233811
2000 Death effector domain protein PEA-15 potentiates Ras activation of extracellular signal receptor-activated kinase by an adhesion-independent mechanism. Molecular biology of the cell 62 10982386
2015 Integrin α5β1 and p53 convergent pathways in the control of anti-apoptotic proteins PEA-15 and survivin in high-grade glioma. Cell death and differentiation 61 26470725
1996 The major astrocytic phosphoprotein PEA-15 is encoded by two mRNAs conserved on their full length in mouse and human. The Journal of biological chemistry 61 8662970
2001 Protein kinase C (PKC)-alpha activation inhibits PKC-zeta and mediates the action of PED/PEA-15 on glucose transport in the L6 skeletal muscle cells. Diabetes 60 11375323
2007 PEA-15 inhibits tumor cell invasion by binding to extracellular signal-regulated kinase 1/2. Cancer research 59 17308092
2004 Overexpression of the ped/pea-15 gene causes diabetes by impairing glucose-stimulated insulin secretion in addition to insulin action. Molecular and cellular biology 59 15143191
2014 Identification of a novel AMPK-PEA15 axis in the anoikis-resistant growth of mammary cells. Breast cancer research : BCR 56 25096718
2024 PED in 2024: improving the community deposition of structural ensembles for intrinsically disordered proteins. Nucleic acids research 55 37904608
1999 The phosphoprotein protein PEA-15 inhibits Fas- but increases TNF-R1-mediated caspase-8 activity and apoptosis. Developmental biology 55 10588860
2014 Phosphorylation-regulated degradation of the tumor-suppressor form of PED by chaperone-mediated autophagy in lung cancer cells. Journal of cellular physiology 54 24477641
2003 RSK2 activity is regulated by its interaction with PEA-15. The Journal of biological chemistry 54 12796492
2007 The PEA-15/PED protein protects glioblastoma cells from glucose deprivation-induced apoptosis via the ERK/MAP kinase pathway. Oncogene 53 17700518
2000 Regulation of expression of phospholipase D1 and D2 by PEA-15, a novel protein that interacts with them. The Journal of biological chemistry 53 10926929
1991 Analysis of litter size and weight in mice differing in Ped gene phenotype and the Q region of the H-2 complex. Journal of reproductive immunology 52 1865393
2003 PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation. The Journal of biological chemistry 51 14506247
2005 PED mediates AKT-dependent chemoresistance in human breast cancer cells. Cancer research 50 16061647
2004 PEA-15 is inhibited by adenovirus E1A and plays a role in ERK nuclear export and Ras-induced senescence. The Journal of biological chemistry 48 15331596
2007 ERK MAP kinase is targeted to RSK2 by the phosphoprotein PEA-15. Proceedings of the National Academy of Sciences of the United States of America 46 18077417
2002 Multiple members of the mitogen-activated protein kinase family are necessary for PED/PEA-15 anti-apoptotic function. The Journal of biological chemistry 46 11790785
1994 Identification of the Ped gene at the molecular level: the Q9 MHC class I transgene converts the Ped slow to the Ped fast phenotype. Biology of reproduction 46 7819451
2007 The anti-apoptotic protein PEA-15 is a tight binding inhibitor of ERK1 and ERK2, which blocks docking interactions at the D-recruitment site. Biochemistry 45 17658892
2004 The expression of PEA-15 (phosphoprotein enriched in astrocytes of 15 kDa) defines subpopulations of astrocytes and neurons throughout the adult mouse brain. Neuroscience 45 15207344
2019 Current Status of Porcine Epidemic Diarrhoea (PED) in European Pigs. Journal of veterinary research 41 31934654
2011 Hsp27 silencing coordinately inhibits proliferation and promotes Fas-induced apoptosis by regulating the PEA-15 molecular switch. Cell death and differentiation 40 22179576
1998 Role of the Ped gene and apoptosis genes in control of preimplantation development. Journal of assisted reproduction and genetics 40 9604770
2014 Phosphoprotein enriched in astrocytes (PEA)-15: a potential therapeutic target in multiple disease states. Pharmacology & therapeutics 39 24657708
2012 Phosphorylation is the switch that turns PEA-15 from tumor suppressor to tumor promoter. Small GTPases 37 22694972
2010 PEA-15 inhibits tumorigenesis in an MDA-MB-468 triple-negative breast cancer xenograft model through increased cytoplasmic localization of activated extracellular signal-regulated kinase. Clinical cancer research : an official journal of the American Association for Cancer Research 36 20215547
2008 PED is overexpressed and mediates TRAIL resistance in human non-small cell lung cancer. Journal of cellular and molecular medicine 36 18284607
2010 Melatonin ameliorates ischemic-like injury-evoked nitrosative stress: Involvement of HtrA2/PED pathways in endothelial cells. Journal of pineal research 35 21198825
2008 Targeting of PED/PEA-15 molecular interaction with phospholipase D1 enhances insulin sensitivity in skeletal muscle cells. The Journal of biological chemistry 35 18541525
2006 Akt down-regulates ERK1/2 nuclear localization and angiotensin II-induced cell proliferation through PEA-15. Molecular biology of the cell 35 16822839
2006 The PEA15 gene is overexpressed and related to insulin resistance in healthy first-degree relatives of patients with type 2 diabetes. Diabetologia 35 17021921
2012 PED/PEA-15 induces autophagy and mediates TGF-beta1 effect on muscle cell differentiation. Cell death and differentiation 34 22281705
2008 Epigalocatechin-3-gallate (EGCG) downregulates PEA15 and thereby augments TRAIL-mediated apoptosis in malignant glioma. Neuroscience letters 34 18948169
2003 Search for the bovine homolog of the murine ped gene and characterization of its messenger RNA expression during bovine preimplantation development. Biology of reproduction 34 14568917
2011 Activated ERK2 is a monomer in vitro with or without divalent cations and when complexed to the cytoplasmic scaffold PEA-15. Biochemistry 32 21506533
2009 Proteomic differential display analysis identified upregulated astrocytic phosphoprotein PEA-15 in human malignant pleural mesothelioma cell lines. Proteomics 32 19771552
2006 Antitumor effect of E1A in ovarian cancer by cytoplasmic sequestration of activated ERK by PEA15. Oncogene 32 16170361
2005 Raised expression of the antiapoptotic protein ped/pea-15 increases susceptibility to chemically induced skin tumor development. Oncogene 32 16044159
2007 PED/PEA-15 regulates glucose-induced insulin secretion by restraining potassium channel expression in pancreatic beta-cells. Diabetes 30 17327429
2011 Serum 25-Hydroxyvitamin D Levels, phosphoprotein enriched in diabetes gene product (PED/PEA-15) and leptin-to-adiponectin ratio in women with PCOS. Nutrition & metabolism 29 22112520
2014 Quantitative proteomics reveals that PEA15 regulates astroglial Aβ phagocytosis in an Alzheimer's disease mouse model. Journal of proteomics 28 25108202
2016 Parkinson-like phenotype in insulin-resistant PED/PEA-15 transgenic mice. Scientific reports 27 27426254
2011 PEA-15 potentiates H-Ras-mediated epithelial cell transformation through phospholipase D. Oncogene 27 22105357
2014 FADD adaptor and PEA-15/ERK1/2 partners in major depression and schizophrenia postmortem brains: basal contents and effects of psychotropic treatments. Neuroscience 26 25075716
2010 The PEA-15 protein regulates autophagy via activation of JNK. The Journal of biological chemistry 26 20452983
1999 Search for a human homologue of the mouse Ped gene. Molecular human reproduction 26 10341001
1998 The expression pattern of the Qa-2 antigen in mouse preimplantation embryos and its correlation with the Ped gene phenotype. Molecular human reproduction 26 9809678
2012 PED/PEA-15 interacts with the 67 kD laminin receptor and regulates cell adhesion, migration, proliferation and apoptosis. Journal of cellular and molecular medicine 25 21895963
2010 The time course of unconditioned morphine-induced psychomotor sensitization mirrors the phosphorylation of FADD and MEK/ERK in rat striatum: role of PEA-15 as a FADD-ERK binding partner in striatal plasticity. European neuropsychopharmacology : the journal of the European College of Neuropsychopharmacology 25 19758790
1999 Identification of two major histocompatibility complex class Ib genes, Q7 and Q9, as the Ped gene in the mouse. Biology of reproduction 25 10208972
2017 Phosphoprotein enriched in diabetes (PED/PEA15) promotes migration in hepatocellular carcinoma and confers resistance to sorafenib. Cell death & disease 24 29072691
2011 MEK1/2 inhibitor selumetinib (AZD6244) inhibits growth of ovarian clear cell carcinoma in a PEA-15-dependent manner in a mouse xenograft model. Molecular cancer therapeutics 24 22144664
2008 Molecular cloning and characterization of the human PED/PEA-15 gene promoter reveal antagonistic regulation by hepatocyte nuclear factor 4alpha and chicken ovalbumin upstream promoter transcription factor II. The Journal of biological chemistry 24 18765665
2005 Quantifying ERK2-protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains. Biochimica et biophysica acta 24 16324895
2022 Transcription Factor FOSL1 Enhances Drug Resistance of Breast Cancer through DUSP7-Mediated Dephosphorylation of PEA15. Molecular cancer research : MCR 23 34907034
2018 PEA15 promotes liver metastasis of colorectal cancer by upregulating the ERK/MAPK signaling pathway. Oncology reports 23 30365128
2012 PEA-15 unphosphorylated at both serine 104 and serine 116 inhibits ovarian cancer cell tumorigenicity and progression through blocking β-catenin. Oncogenesis 23 23552738
2007 Phorbol esters induce intracellular accumulation of the anti-apoptotic protein PED/PEA-15 by preventing ubiquitinylation and proteasomal degradation. The Journal of biological chemistry 23 17227770
1998 Differential expression of Ped gene candidates in preimplantation mouse embryos. Biology of reproduction 23 9746747
2020 ZNF703 promotes tumor progression in ovarian cancer by interacting with HE4 and epigenetically regulating PEA15. Journal of experimental & clinical cancer research : CR 22 33246486
2012 Clozapine impairs insulin action by up-regulating Akt phosphorylation and Ped/Pea-15 protein abundance. Journal of cellular physiology 22 21618539
2003 PEA-15 modulates TNFalpha intracellular signaling in astrocytes. Annals of the New York Academy of Sciences 22 15033692
2013 The PEA-15/PED protein regulates cellular survival and invasiveness in colorectal carcinomas. Cancer letters 21 23481023
2008 MicroRNA expression in preimplantation mouse embryos from Ped gene positive compared to Ped gene negative mice. Journal of assisted reproduction and genetics 21 18347971
2000 Molecular characterization of the human PEA15 gene on 1q21-q22 and association with type 2 diabetes mellitus in Pima Indians. Gene 21 10607908
2012 Ferulic acid prevents the cerebral ischemic injury-induced decreases of astrocytic phosphoprotein PEA-15 and its two phosphorylated forms. Neuroscience letters 20 22306184
2000 Expression of MAT1/PEA-15 mRNA isoforms during physiological and neoplastic changes in the mouse mammary gland. Cancer letters 20 10737714
2018 PED subunit vaccine based on COE domain replacement of flagellin domain D3 improved specific humoral and mucosal immunity in mice. Vaccine 19 29426660
2012 PED/PEA-15 controls fibroblast motility and wound closure by ERK1/2-dependent mechanisms. Journal of cellular physiology 19 21780113
2010 PED interacts with Rac1 and regulates cell migration/invasion processes in human non-small cell lung cancer cells. Journal of cellular physiology 19 20648624
2015 Biomechanical insult switches PEA-15 activity to uncouple its anti-apoptotic function and promote erk mediated tissue remodeling. Experimental cell research 18 26615958
2005 Rapid Ped-2E9 cell-based cytotoxicity analysis and genotyping of Bacillus species. Journal of clinical microbiology 18 16333068

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