Affinage

PELP1

Proline-, glutamic acid- and leucine-rich protein 1 · UniProt Q8IZL8

Length
1130 aa
Mass
119.7 kDa
Annotated
2026-06-10
95 papers in source corpus 37 papers cited in narrative 37 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PELP1 is a large multidomain scaffold protein that functions both as a nuclear receptor coregulator and as the structural core of a ribosome biogenesis complex, integrating hormone signaling, chromatin modification, and cell cycle control to drive proliferation (PMID:11481323, PMID:20448663, PMID:36351913). It was first identified as an estrogen receptor alpha (ERα) coactivator that binds ERα through its nine LXXLL motifs and recruits the general coactivators p300/CBP to enhance estradiol-dependent transcription (PMID:11481323). PELP1 reads histone methylation marks and remodels chromatin at ERα target promoters: it interacts with histones H1 and H3, displaces H1 in cyclic phase with promoter occupancy, and reprograms the demethylase KDM1/LSD1 to switch its substrate specificity from H3K4 to H3K9 while engaging the arginine methyltransferases CARM1 and PRMT6 (PMID:15374949, PMID:20448663, PMID:23486015, PMID:24447537). Its transcriptional output is context-dependent — acting as a corepressor in the absence of ER by recruiting HDAC2 to bind hypoacetylated histones, and switching to coactivation upon ER binding (PMID:15456770). Beyond the nucleus, PELP1 serves as a scaffold for rapid non-genomic signaling, bridging ERα via LXXLL motifs and cSrc via an N-terminal PXXP motif to activate Src/MAPK, and after cSrc phosphorylates it at Tyr920 it recruits the p85 subunit of PI3K to drive Akt activation (PMID:14963108, PMID:17194752). Cytoplasmic restriction of PELP1 confers estrogen hypersensitivity, tamoxifen resistance, and tumorigenicity through constitutive Src/MAPK, PI3K/Akt, mTOR, and metabolic (PFKFB3/4) signaling and cancer stem cell expansion (PMID:16140940, PMID:24688046, PMID:34103681). PELP1 is a CDK substrate (Ser477/Ser991) that couples ER signaling to the pRb/E2F cell cycle machinery and to rDNA transcription in the nucleolus (PMID:12682072, PMID:20807815, PMID:21695158). Structurally, PELP1 is the central scaffold of the human Rix1/rixosome complex with WDR18, TEX10, and SENP3, where its proline- and glutamate-rich intrinsically disordered region chaperones histones and allosterically activates SENP3 SUMO protease activity (PMID:36351913, PMID:40712028). PELP1's coregulator and scaffolding functions extend to other nuclear receptors (AR, RXRα, GR) and transcription factors (β-catenin, TFAP2C), and it is a validated therapeutic target whose small-molecule inhibitor SMIP34 induces its proteasomal degradation (PMID:15831520, PMID:16574651, PMID:33269540, PMID:35950923, PMID:32309805).

Mechanistic history

Synthesis pass · year-by-year structured walk · 24 steps
  1. 2001 High

    Established PELP1's founding identity by showing it physically binds ERα and the p300/CBP coactivators to amplify estrogen-responsive transcription, defining it as a nuclear receptor coregulator.

    Evidence Co-IP, ERE-luciferase reporter assays, and domain mapping identifying nine LXXLL motifs

    PMID:11481323

    Open questions at the time
    • Did not resolve which LXXLL motifs mediate binding
    • No structural basis for coactivation
  2. 2003 High

    Resolved how PELP1 scaffolds non-genomic ER signaling, showing it bridges cSrc (via PXXP) and ERα (via LXXLL) to activate Src/MAPK, extending its role beyond transcription into membrane-proximal kinase activation.

    Evidence Motif mutagenesis, co-IP, and kinase/reporter assays in mammalian cells

    PMID:14963108

    Open questions at the time
    • Did not define downstream PI3K branch
    • Phosphorylation events not yet mapped
  3. 2003 High

    Connected PELP1 to cell cycle control by showing it binds pRb and promotes its hyperphosphorylation and S-phase entry, linking ER coactivation to proliferative machinery.

    Evidence Co-IP, phospho-pRb antibodies, flow cytometry in MCF-7 cells

    PMID:12682072

    Open questions at the time
    • Kinase responsible for pRb phosphorylation not defined here
    • Direct vs indirect effect unresolved
  4. 2004 High

    Defined PELP1's chromatin-remodeling mechanism, showing it binds histones H1/H3, displaces H1 cyclically at promoters, and can act as either coactivator or corepressor via distinct domains binding HDAC2 or hypoacetylated histones.

    Evidence Subnuclear fractionation, ChIP, far Western, HAT assays, MNase sensitivity, dominant-negative and tethering assays

    PMID:15374949 PMID:15456770

    Open questions at the time
    • Histone-mark readers not yet identified
    • Switch mechanism between repression and activation incompletely defined
  5. 2005 High

    Demonstrated that cytoplasmic PELP1 localization is a driver of therapy resistance and tumorigenicity through constitutive Src, MAPK, AKT, and PI3K activation, mechanistically linking subcellular distribution to oncogenic phenotype.

    Evidence Engineered cytoplasm-restricted mutant, xenografts, co-IP, kinase assays

    PMID:16140940

    Open questions at the time
    • Endogenous determinants of PELP1 localization unknown
    • Did not define molecular trigger for cytoplasmic accumulation
  6. 2005 Medium

    Broadened PELP1's coregulator scope to other steroid receptors and identified cytoplasmic regulators, showing AR/Gβ engagement governs meiotic arrest and HRS sequesters PELP1 in the cytoplasm to restrain ER coactivation.

    Evidence Yeast two-hybrid, RNAi in Xenopus oocytes, co-IP, fractionation, reporter assays

    PMID:15831520 PMID:16352611

    Open questions at the time
    • Single-lab findings
    • Physiological relevance of HRS sequestration in human cancer not established
  7. 2006 High

    Pinpointed the molecular switch for the PI3K/Akt arm, showing cSrc phosphorylation of PELP1 at Tyr920 is required for p85 recruitment and E2-induced Akt-mediated survival, separating this branch from Src/MAPK and proliferation.

    Evidence Site-directed Y920A mutagenesis, co-IP, in vitro kinase, apoptosis assays

    PMID:17194752

    Open questions at the time
    • Other phosphosites not yet characterized
    • Single-lab reconstitution
  8. 2006 Medium

    Extended PELP1 coactivation to RXRα signaling, showing it stabilizes RXRα homodimers and RXRα-PPARγ heterodimers and enhances retinoid-induced transcription and apoptosis.

    Evidence Co-IP, EMSA supershift, reporter and differentiation assays

    PMID:16574651

    Open questions at the time
    • Single lab
    • In vivo retinoid relevance not established
  9. 2008 Medium

    Showed PELP1 is integrated into growth factor signaling through PKA phosphorylation that controls its subnuclear localization and coactivation, and clarified that its GR regulation is c-Src-independent and domain-specific.

    Evidence In vitro PKA kinase assays, phospho-mutants, H89 inhibitor, deletion mapping, reporter assays

    PMID:18505929 PMID:18682536

    Open questions at the time
    • PKA site sequence not fully defined
    • Cell-type dependence of GR effects unexplained
  10. 2009 Medium

    Linked PELP1 to estrogen biosynthesis by showing it is recruited to the aromatase I.3/II promoter via ERRα and histone demethylases to upregulate aromatase, with HER2 enhancing recruitment.

    Evidence ChIP, aromatase activity and reporter assays, xenograft and transgenic models

    PMID:19800002

    Open questions at the time
    • Single lab
    • Direct ERRα-PELP1 contacts not mapped
  11. 2010 High

    Identified PELP1 as a histone-mark reader that reprograms KDM1/LSD1 substrate specificity from H3K4 to H3K9, providing a mechanistic basis for its bidirectional chromatin effects at ER target genes.

    Evidence Co-IP, ChIP, siRNA, in vitro demethylase assays

    PMID:20448663

    Open questions at the time
    • Structural basis of specificity switch unresolved
    • Genome-wide scope not mapped
  12. 2010 High

    Coupled PELP1 to cell cycle and nucleolar function, showing CDKs phosphorylate Ser477/Ser991 to regulate E2-driven proliferation, E2F1 transactivation, and cell-cycle-dependent nucleolar rDNA transcription.

    Evidence In vitro CDK kinase assays, phospho-mutants, ChIP, cell synchronization, rDNA reporter assays, xenografts

    PMID:20807815 PMID:21695158

    Open questions at the time
    • How CDK phosphorylation directs nucleolar targeting not fully mechanistic
    • Link to ribosome biogenesis complex not yet made
  13. 2010 Medium

    Revealed a PTM regulating PELP1 chromatin function — TTLL4-mediated polyglutamylation of its glutamate stretch — and first placed PELP1 in chromatin-remodeling complexes with LAS1L and SENP3.

    Evidence shRNA knockdown of TTLL4, immunoprecipitation, co-IP, growth assays

    PMID:20442285

    Open questions at the time
    • Functional consequence of complex membership not resolved here
    • Single lab
  14. 2013 High

    Expanded PELP1's epigenetic reader/writer activity to arginine methylation (CARM1, PRMT6) and to RNA-level regulation, showing it controls H3 arginine methylation at ER targets, localizes to nuclear speckles with SC35, and participates in alternative splicing.

    Evidence Histone peptide arrays, RNA-seq, co-IP, ChIP, RNA-binding assays, xenografts

    PMID:23486015 PMID:24447537

    Open questions at the time
    • RNA-binding specificity beyond poly-C undefined
    • Splicing program targets incompletely mapped
  15. 2013 High

    Established PELP1 as a driver of metastasis through epigenetic repression, showing it recruits HDAC2 to silence miR-200a/miR-141, derepressing ZEB1/ZEB2 to promote EMT and invasion.

    Evidence ChIP, miR array, HDAC inhibitors, miR mimetic rescue, Boyden chamber, xenografts

    PMID:23975430

    Open questions at the time
    • Direct PELP1 promoter-binding mode unresolved
    • Other miRNA targets not surveyed
  16. 2014 Medium

    Showed PELP1 scaffolds multi-receptor transcription complexes (ER/PR/IGF1R) and cross-talks with mTOR, integrating hormone and growth-factor pathways to support proliferation.

    Evidence ChIP, co-IP, microarray, patient tumor IP, mTOR inhibitor treatment, xenografts

    PMID:24469035 PMID:24688046

    Open questions at the time
    • Direct vs scaffolded mTOR contacts unclear
    • Single-lab co-IP for mTOR association
  17. 2015 Medium

    Connected PELP1 to mutant-p53 and TNBC oncogenic programs, showing it regulates MTp53 promoter recruitment and E2F1 stability in a KDM1A-dependent manner, with S1033 phosphorylation important for oncogenic function.

    Evidence Co-IP, ChIP, siRNA, reporter assays, flow cytometry

    PMID:25788226

    Open questions at the time
    • S1033 kinase not identified
    • Single lab
  18. 2016 Medium

    Defined hypoxia- and glucocorticoid-responsive and inflammatory roles, showing PELP1 assembles a phospho-GR/HIF complex to induce Brk, and cytoplasmic PELP1 drives IKKε/RelB-mediated paracrine macrophage activation and migration.

    Evidence ChIP, co-IP, hypoxia/dexamethasone treatments, conditioned-medium and migration assays, shRNA

    PMID:26825173 PMID:27881676

    Open questions at the time
    • Direct PELP1-HIF contacts not mapped
    • Secreted paracrine factors not identified
  19. 2018 Medium

    Identified the cytoplasmic PELP1-AIB1/SRC-3 axis as a driver of cancer stem cell expansion, showing PELP1 elevates AIB1 Thr24 phosphorylation and ALDH+ tumorsphere formation independently of hormone.

    Evidence Co-IP, tumorsphere/ALDH sorting, SI-2 inhibition, shRNA, syngeneic models

    PMID:29348189

    Open questions at the time
    • Mechanism of AIB1 activation by PELP1 undefined
    • Single lab
  20. 2021 Medium

    Linked the PELP1/SRC-3 cytoplasmic complex to metabolic reprogramming, showing PELP1 binds PFKFB3/PFKFB4 and increases glycolysis and respiration to sustain stem cell expansion.

    Evidence Co-IP, Seahorse assays, PFKFB inhibitors, tumorspheres, xenograft and organoid models

    PMID:34103681

    Open questions at the time
    • Whether PELP1 directly regulates PFKFB kinase activity unclear
    • Single lab
  21. 2021 Medium

    Generalized PELP1 coactivation beyond nuclear receptors to lineage transcription factors, showing it coactivates TFAP2C and β-catenin to drive RET/AKT/ERK signaling and Wnt target gene expression in breast cancer and glioblastoma.

    Evidence Co-IP, RNA-seq, ChIP, reporter assays, orthotopic and xenograft models

    PMID:32309805 PMID:33269540

    Open questions at the time
    • Direct binding interfaces not mapped
    • Tissue-specificity of partner selection unexplained
  22. 2022 High

    Resolved PELP1's structural role as the central scaffold of the human Rix1 complex with WDR18/TEX10/SENP3, with a cryo-EM structure showing its LxxLL motifs are not configured for steroid receptor binding in this context — implying WDR18 association partitions PELP1 away from coactivation.

    Evidence Cryo-EM at 2.7 Å of the PELP1 Rix1 domain–WDR18 subcomplex, in vitro reconstitution

    PMID:36351913

    Open questions at the time
    • How PELP1 partitions between Rix1 and coactivator pools in cells unresolved
    • Functional output of the rixosome in cancer not directly tested here
  23. 2022 High

    Identified SETDB1 as a PELP1 partner required for Akt methylation and tamoxifen resistance, and validated PELP1 as a druggable target via SMIP34, which binds PELP1 and triggers its proteasomal degradation, suppressing both extranuclear and ribosome-biogenesis functions.

    Evidence Yeast two-hybrid, GST pull-down, co-IP, in vitro methylation; SMIP34 binding assays, RNA-seq, xenograft/PDX models

    PMID:35395812 PMID:35950923

    Open questions at the time
    • SMIP34 binding site on PELP1 not crystallographically defined
    • Clinical translation not addressed
  24. 2025 High

    Provided the structural mechanism for PELP1's rixosome scaffolding, showing its C-terminal IDR engages MDN1, histones, and SENP3, that its glutamate-rich region chaperones the histone octamer, and that a SLiM-SENP3 crystal structure explains allosteric activation of SUMO protease activity.

    Evidence X-ray crystallography of SLiM-SENP3, in vitro histone chaperoning, biochemical reconstitution

    PMID:40712028

    Open questions at the time
    • In vivo SUMO substrates of the PELP1-activated rixosome not defined
    • Integration with PELP1's coactivator functions unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How PELP1 partitions between its nuclear receptor coactivator, chromatin-remodeling, extranuclear signaling, and rixosome scaffolding roles — and what governs the localization and PTM states that toggle between them — remains the central open question.
  • No unified model of how subcellular localization is regulated
  • Competition between WDR18/Rix1 binding and SR coactivation not quantified in cells
  • Causative role in any Mendelian disease not established

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140110 transcription regulator activity 5 GO:0042393 histone binding 4 GO:0060090 molecular adaptor activity 4 GO:0140097 catalytic activity, acting on DNA 2 GO:0003723 RNA binding 1 GO:0098772 molecular function regulator activity 1
Localization
GO:0005829 cytosol 3 GO:0005634 nucleus 2 GO:0005654 nucleoplasm 1 GO:0005694 chromosome 1 GO:0005730 nucleolus 1
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-4839726 Chromatin organization 4 R-HSA-74160 Gene expression (Transcription) 4 R-HSA-8953854 Metabolism of RNA 3 R-HSA-1640170 Cell Cycle 2
Partners
CARM1ESR1KDM1ANCOA3RB1SENP3SRCWDR18
Complex memberships
ER/PR/PELP1/IGF1R transcription complexERα-cSrc-p85/PI3K non-genomic signaling complexRix1 complex / rixosome (PELP1-WDR18-TEX10-SENP3)

Evidence

Reading pass · 37 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 PELP1 was identified as a coactivator of estrogen receptor alpha (ERα). It physically interacts with ERα and with general transcriptional coactivators p300 and CBP, and enhances 17β-estradiol-dependent transcriptional activation from estrogen response elements in a dose-dependent manner. PELP1 contains nine NR-interacting LXXLL motifs, a zinc finger, and glutamic acid- and proline-rich regions. Co-immunoprecipitation, reporter gene assays (ERE-luciferase), Western blotting, tissue expression analysis The Journal of biological chemistry High 11481323
2003 MNAR/PELP1 acts as a scaffold protein mediating ERα-Src interaction: MNAR interacts with the SH3 domain of cSrc via its N-terminal PXXP motif, and with ERα via two N-terminal LXXLL motifs. Mutation of the PXXP motif abolished MNAR-induced Src activation and ER transcriptional stimulation. ERα interacts with Src's SH2 domain via phosphotyrosine 537, and this complex is further stabilized by MNAR-ER interaction. Mutation of LXXLL motifs prevented ER-MNAR complex formation and eliminated Src/MAPK pathway activation. Mutational analysis of MNAR and ERα, co-immunoprecipitation, functional kinase activation assays, reporter gene assays Molecular endocrinology (Baltimore, Md.) High 14963108
2003 PELP1 physically associates with retinoblastoma protein (pRb) via pRb's C-terminal pocket domain. PELP1 overexpression leads to persistent hyperphosphorylation of pRb at Ser-807/Ser-811 in an E2-dependent manner, enhances progression to S phase, and potentiates cyclin D1 expression. PELP1/pRb interaction is required for maximal PELP1 coactivation function and is modulated by antiestrogen agents. Co-immunoprecipitation, stable overexpression in MCF-7 cells, phospho-specific pRb antibodies, flow cytometry, reporter gene assays with mutant pRb cells The Journal of biological chemistry High 12682072
2004 PELP1 localizes to the nucleus, associates with chromatin and nuclear matrix fractions, and is recruited to 17β-estradiol-responsive promoters upon ligand stimulation. PELP1 interacts with histones H1 and H3 (with preference for H1) via its C-terminal region. PELP1 overexpression increases histone acetyltransferase activity and micrococcal nuclease sensitivity of ERE-containing nucleosomes. A PELP1 mutant lacking the H1-binding domain acts as a dominant negative, blocking ERα-mediated transcription. PELP1 displays cyclic association and dissociation from promoters in opposite phase to histone H1, suggesting a role in chromatin remodeling via H1 displacement. Subnuclear fractionation, confocal microscopy, ChIP, far Western analysis, deletion analysis, histone acetyltransferase enzymatic assay, micrococcal nuclease sensitivity assay, dominant-negative mutant studies Cancer research High 15374949
2004 PELP1 functions as a corepressor of multiple nuclear receptors and non-NR transcription factors (GR, Nur77, AP1, NF-κB, TCF/SRF) in the absence of ER. The N-terminal leucine-abundant region of PELP1 interacts with HDAC2 and exhibits repressive activity when tethered to chromatin. The C-terminal glutamic acid-abundant region binds hypoacetylated histones H3 and H4, preventing their acetylation. ER binding reverses PELP1's role to promote histone hyperacetylation. Reporter gene assays, co-immunoprecipitation, domain mapping, chromatin tethering assays, cell proliferation assays The Journal of biological chemistry High 15456770
2005 Cytoplasmic localization of PELP1 (PELP1-cyto mutant) confers hypersensitivity to estrogen, resistance to tamoxifen, and tumorigenicity in nude mice. Cytoplasmic PELP1 shows increased association with Src, enhanced MAPK activation, constitutive AKT activation, and interaction with the p85 subunit of PI3K leading to PI3K activation. Cytoplasmic PELP1 also interacts with EGFR and participates in growth factor-mediated ER transactivation. Engineered cytoplasm-restricted PELP1 mutant, stable MCF-7 cell lines, xenograft tumor assays, co-immunoprecipitation, kinase activation assays, Western blotting Cancer research High 16140940
2005 HRS (hepatocyte growth factor-regulated tyrosine kinase substrate) is a novel PELP1-binding protein identified by yeast two-hybrid screen. HRS sequesters PELP1 in the cytoplasm and inhibits PELP1 coactivation of ER transcription. HRS-PELP1 interaction activates MAPK in an EGFR-dependent but ER/Src/Shc-independent manner. Yeast two-hybrid screen, co-immunoprecipitation, subcellular fractionation, reporter gene assays, MAPK activation assays The Journal of biological chemistry Medium 16352611
2005 MNAR/PELP1 regulates androgen receptor (AR)-mediated nongenomic signaling. MNAR and AR co-immunoprecipitate via the LXXLL-rich segment of MNAR and the ligand binding domain of AR. MNAR also interacts with Gβ via the same region. Reduction of MNAR expression by RNAi in Xenopus oocytes enhances testosterone-triggered meiosis and MAPK activation, and decreases Gβγ-mediated signaling, implicating MNAR in maintaining meiotic arrest. RNA interference in Xenopus oocytes, co-immunoprecipitation, transient transfection reporter assays Molecular endocrinology (Baltimore, Md.) Medium 15831520
2006 MNAR/PELP1 phosphorylation at Tyr-920 by cSrc is required for interaction with p85 (PI3K regulatory subunit) and E2-induced activation of the PI3K/Akt pathway. Mutation Y920A abolishes MNAR-p85 interaction and PI3K/Akt activation (abrogating E2-induced protection from apoptosis) but does not impair Src/MAPK pathway activation or cell proliferation. Endogenous MNAR, ERα, cSrc, and p85 form a complex in E2-treated MCF-7 cells. Site-directed mutagenesis, co-immunoprecipitation, in vitro kinase assays, reporter gene assays, cell viability/apoptosis assays Molecular and cellular biology High 17194752
2006 PELP1 functions as a coactivator of RXRα, physically interacting with RXRα both in vitro and in vivo. PELP1 promotes formation and stability of RXRα homodimers on consensus oligonucleotides and enhances RXRα-mediated transcription and apoptosis in response to 9-cis-retinoic acid. PELP1 also coactivates RXRα-PPARγ heterodimers. Co-immunoprecipitation, EMSA supershift assays, reporter gene assays, stable MCF-7 overexpression, siRNA knockdown, differentiation assays The Journal of biological chemistry Medium 16574651
2007 PELP1 localizes to autophagosomes in cancer cells treated with resveratrol. The intermediary molecule for PELP1 accumulation in autophagosomes is HRS. Both PELP1 and HRS relocalize to autophagosomes (marked by GFP-LC3) upon resveratrol treatment. Confocal microscopy, GFP-LC3 autophagic marker, pharmacological autophagy inhibitors (3-methyladenine) Cancer research Medium 17804729
2007 PELP1 is recruited to the BCAS3 chromatin locus and activates BCAS3 expression; BCAS3 in turn functions as an ERα coactivator that requires PELP1 to enhance ER transactivation activity. BCAS3 physically associates with histone H3 and P/CAF and possesses histone acetyltransferase activity. ChIP assays, reporter gene assays, co-immunoprecipitation, siRNA knockdown, stable overexpression Molecular endocrinology (Baltimore, Md.) Medium 17505058
2008 MNAR/PELP1 interacts with GR in the nucleus (but not cytoplasm) and modulates GR transactivation in a cell-type and concentration-dependent manner: MNAR inhibits GR AF1 (ligand-independent) but potentiates AF2 (ligand-dependent). The region MNAR 884-1130 and the N-terminal 1-400 domain (containing LXXLL motifs) both independently inhibit GR transactivation. This GR regulatory function is independent of c-Src activity. Co-immunoprecipitation, reporter gene assays, deletion analysis, c-Src inhibitors and knockdown, immunofluorescence American journal of physiology. Endocrinology and metabolism Medium 18682536
2008 Growth factor signaling promotes phosphorylation of PELP1 via protein kinase A (PKA). PKA directly phosphorylates PELP1 in vitro; mutation of the putative PKA site in PELP1 compromises growth factor-induced ER transactivation, subnuclear localization of PELP1, and PELP1-mediated coactivation function. In vivo phosphorylation labeling, phospho-substrate specific antibodies, PKA inhibitor (H89), in vitro kinase assays with purified PKA, deletion and site-directed mutagenesis, reporter gene assays Molecular cancer research : MCR High 18505929
2009 PELP1 deregulation contributes to increased aromatase expression via activation of aromatase promoter I.3/II. PELP1 is recruited to the aromatase I.3/II promoter as shown by ChIP. PELP1-mediated aromatase induction requires functional Src and PI3K pathways and involves interaction with orphan receptor ERRα and histone demethylases. HER2 signaling enhances PELP1 recruitment to the aromatase promoter. ChIP assays, reporter gene assays, aromatase activity assays, Western blotting, xenograft and transgenic mouse models The Journal of steroid biochemistry and molecular biology Medium 19800002
2010 PELP1 is a reader of histone H3 methylation marks. PELP1 interacts with the histone lysine demethylase KDM1 (LSD1). Both are co-recruited to ERα target genes. PELP1 depletion affects dimethyl histone modifications (H3K4me2 and H3K9me2) at ERα target genes. PELP1 alters KDM1 substrate specificity from H3K4 to H3K9 dimethylation. Effective demethylation of H3K9me2 requires a KDM1-ERα-PELP1 functional complex. Co-immunoprecipitation, ChIP assays, siRNA knockdown, in vitro demethylase activity assays, reporter gene assays EMBO reports High 20448663
2010 TTLL4 polyglutamylase modifies PELP1 by adding glutamate side chains (polyglutamylation) to PELP1's glutamate stretch region. PELP1 polyglutamylation influences PELP1 interaction with histone H3 and affects histone H3 acetylation. PELP1 interacts with LAS1L and SENP3, components of the MLL1-WDR5 supercomplex involved in chromatin remodeling. Knockdown of TTLL4 by shRNA, immunoprecipitation, co-immunoprecipitation, cell growth assays, correlation of TTLL4 expression with PELP1 polyglutamylation levels Cancer research Medium 20442285
2010 PELP1 is a novel substrate of cyclin-dependent kinases (CDKs). Ser477 and Ser991 of PELP1 are CDK phosphorylation sites identified by site-directed mutagenesis and in vitro kinase assays. PELP1 is hyperphosphorylated during cell cycle progression. PELP1 CDK-site mutants exhibit defects in E2-mediated cell cycle progression and oncogenic functions in vivo. PELP1 modulates E2F1 transactivation and is recruited to pRb/E2F target gene promoters, facilitating ER-cell cycle machinery crosstalk. Site-directed mutagenesis, in vitro CDK kinase assays, phospho-specific antibody, ChIP assays, reporter gene assays, stable cell lines, xenograft models Cancer research High 20807815
2011 PELP1 localizes to the nucleolus and is associated with active ribosomal RNA transcription. PELP1 nucleolar localization is cell-cycle dependent (highest in S and G2 phases) and regulated by CDK activity. PELP1 depletion decreases pre-rRNA expression. PELP1 is recruited to the promoter regions of rDNA (ChIP) and is needed for optimal rDNA transcription. PELP1 domains required for nucleolar localization are essential for rDNA reporter activation. Pharmacological inhibitors, confocal microscopy, cell synchronization, CDK site mutants, siRNA, reporter gene assays (rDNA-luciferase), ChIP assays PloS one High 21695158
2012 PELP1 forms a protein complex with AR, ERβ, and PELP1 on AR-responsive DNA elements in prostate cancer cells in response to E2. This complex enables E2-induced transcription of AR-responsive genes and E2-stimulated cell proliferation. Knockdown of PELP1, AR, or ERβ blocks complex assembly, blocks E2-induced AR gene activation, and blocks proliferation. Co-immunoprecipitation, ChIP assays, siRNA knockdown, reporter gene assays, cell proliferation assays Molecular endocrinology (Baltimore, Md.) Medium 22403175
2013 PELP1 binds to the promoters of miR-200a and miR-141 and represses their expression by recruiting histone deacetylase 2 (HDAC2). PELP1 knockdown reduced ZEB1 and ZEB2 expression and metastatic potential. Re-introduction of miR-200a and miR-141 mimetics reversed PELP1 target gene expression and reduced PELP1-driven migration/invasion in vitro and in vivo. ChIP assays, whole genome miR array, siRNA knockdown, HDAC inhibitor assays, Boyden chamber assays, xenograft tumor models Oncogene High 23975430
2013 PELP1 is a reader of histone arginine methyl modifications. PELP1 functionally interacts with the arginine methyltransferase CARM1; their interaction is enhanced by ERα. PELP1-CARM1 interactions synergistically enhance ERα transactivation. PELP1 alters histone H3 arginine methylation status at ERα target gene promoters as shown by ChIP. PELP1 knockdown decreases CARM1-driven arginine dimethylation in vivo. Histone peptide array, co-immunoprecipitation, ChIP assays, pharmacological CARM1 inhibition, siRNA knockdown, reporter gene assays, xenograft models Carcinogenesis High 23486015
2013 PELP1 interacts with the arginine methyltransferase PRMT6 and modifies PRMT6 functions. PELP1 and PRMT6 are co-recruited to ERα target genes; PELP1 knockdown affects enrichment of histone H3R2 dimethylation. PELP1 co-localizes with splicing factor SC35 at nuclear speckles and participates in alternative splicing, binding RNA with preference for poly-C sequences. RNA-sequencing, co-immunoprecipitation, ChIP assays, RNA binding assays, immunofluorescence co-localization, siRNA knockdown, reporter gene assays Molecular oncology Medium 24447537
2014 PELP1 serves as a scaffold for ER/PR/PELP1/IGF1R-containing transcription complexes in breast cancer cells. Unliganded PR-B enhances estradiol-responsive ER transcription via scaffolding these complexes on ERE-containing promoters. The ER/PR/PELP1 complex was also detected in human breast cancer samples. ChIP assays, co-immunoprecipitation, stable cell line expression, growth assays, microarray gene expression, immunoprecipitation from patient tumor samples Oncogene Medium 24469035
2014 PELP1 cross-talks with the mTOR signaling pathway. PELP1 knockdown reduces activation of mTOR downstream signaling components. PELP1 overexpression excessively activates mTOR signaling. mTOR signaling complex proteins are detected in PELP1 immunoprecipitates. Co-immunoprecipitation, Western blotting (phospho-mTOR pathway markers), siRNA knockdown, xenograft tumor models, mTOR inhibitor treatment Molecular cancer therapeutics Medium 24688046
2015 PELP1 interacts with mutant p53 (MTp53), regulates its recruitment to target gene promoters, and alters epigenetic marks at those promoters. PELP1 knockdown reduces MTp53 target gene expression and increases apoptosis upon genotoxic stress. PELP1 regulates E2F1 stability in a KDM1A-dependent manner. PELP1 phosphorylation at S1033 plays an important role in its oncogenic functions in TNBC cells. Co-immunoprecipitation, ChIP assays, siRNA knockdown, reporter gene assays, flow cytometry Breast cancer research and treatment Medium 25788226
2016 PELP1 interacts with glucocorticoid receptor (GR) and is induced in a HIF-dependent manner in response to hypoxia or dexamethasone. PELP1 is part of a phospho-GR/HIF/PELP1 complex that assembles on the BRK promoter, promoting Brk expression in triple-negative breast cancer. ChIP assays, co-immunoprecipitation, Western blotting, GR ligand treatments, hypoxia conditions, siRNA knockdown Cancer research Medium 26825173
2016 Cytoplasmic localization of PELP1 up-regulates IKKε and increases phosphorylation of the NF-κB subunit RelB. PELP1-cyto-expressing mammary epithelial cells secrete factors that activate macrophages in a paracrine manner, and those activated macrophages produce conditioned medium that drives HMEC migration. This migration is reduced by IKKε shRNA knockdown. Gene expression analysis, Western blotting, conditioned medium experiments, shRNA knockdown, Boyden chamber migration assays, PELP1-cyto mutant cell lines The Journal of biological chemistry Medium 27881676
2018 Cytoplasmic PELP1 forms a complex with AIB1/SRC-3, identified as a novel binding partner. Cytoplasmic PELP1 expression elevates basal phosphorylation (Thr24 activation) of AIB1, enhances ALDH+ tumorsphere formation, and upregulates specific target genes independently of hormone stimulation. Direct AIB1 knockdown or pharmacological inhibition (SI-2) abrogates cytoplasmic PELP1-induced tumorsphere formation. Co-immunoprecipitation, tumorsphere assays (ALDH+ sorting), shRNA knockdown, Western blotting, syngeneic in vivo tumor studies Molecular cancer research : MCR Medium 29348189
2021 Cytoplasmic complexes of PELP1 and SRC-3 modulate breast cancer stem cell expansion through upregulation of HIF-activated metabolic target genes PFKFB3 and PFKFB4. PELP1 physically interacts with PFKFB3 and PFKFB4 proteins. Inhibition of PFKFB3/4 kinase activity blocks PELP1-induced tumorsphere formation and PELP1/SRC-3 protein-protein interactions. Cytoplasmic PELP1 increases both glycolysis and mitochondrial respiration as measured by Seahorse metabolic assays. Co-immunoprecipitation, Seahorse metabolic assays, tumorsphere assays, PFKFB inhibitors, shRNA knockdown, xenograft and patient-derived organoid models Oncogene Medium 34103681
2021 PELP1 interacts with TFAP2C (transcription factor AP-2γ). PELP1 functions as a coactivator of TFAP2C and mediates TFAP2C-induced changes in histone methylation at the RET promoter, increasing RET expression and downstream AKT and ERK pathway activation. PELP1 knockdown abrogates TFAP2C-driven breast cancer progression in vivo. Co-immunoprecipitation, RNA-seq, ChIP assays, reporter gene assays, siRNA knockdown, Western blotting, xenograft models Molecular oncology Medium 33269540
2022 PELP1 is the central scaffold for the human Rix1 complex, whose members include WDR18, TEX10, and SENP3. The cryo-EM structure of the PELP1 Rix1 domain–WDR18 subcomplex was determined at 2.7 Å, revealing an interconnected tetrameric assembly and the architecture of PELP1's eleven LxxLL motifs, none of which are in a conformation that would support steroid receptor binding within this complex. Association with WDR18 may direct PELP1 activity away from SR coactivation. Cryo-EM structure determination (2.7 Å), in vitro reconstitution of mammalian Rix1 complex, identification of stable sub-complex Nature communications High 36351913
2022 SETDB1 interacts with PELP1, identified initially by yeast two-hybrid screen and confirmed by co-immunoprecipitation and GST pull-down. PELP1 is necessary for SETDB1-mediated Akt methylation and phosphorylation. SETDB1 overexpression promotes tamoxifen resistance in breast cancer cells, and PELP1 knockdown abolishes these effects. Yeast two-hybrid screen, co-immunoprecipitation, GST pull-down, in vitro methylation assays, Western blotting, xenograft models Breast cancer research : BCR High 35395812
2022 SMIP34, a small-molecule inhibitor of PELP1, directly binds to PELP1 and induces its degradation via the proteasome pathway. SMIP34 inhibits PELP1 oncogenic functions including extranuclear signaling (ERK, mTOR, S6, 4EBP1), ribosomal biogenesis functions (cMyc, LAS1L, TEX10, SENP3/Rix complex), and suppresses ER+ breast cancer progression in cell line-derived and patient-derived xenografts. Yeast two-hybrid screen for PELP1 peptide inhibitors, biochemical binding assays, computational modeling, RNA-seq, Western blotting, xenograft and PDX models Cancer research High 35950923
2025 PELP1 serves as the central scaffold of the rixosome complex upon which enzymatic subunits modularly assemble. The C-terminal proline-rich IDR of PELP1 mediates association with the AAA-ATPase MDN1, histones, and SENP3. The glutamic acid-rich region of the PELP1 IDR can chaperone the histone octamer in vitro. An X-ray crystal structure of a short linear motif (SLiM) from the PELP1 IDR bound to SENP3 reveals how PELP1 allosterically activates SUMO protease activity. X-ray crystallography (SLiM-SENP3 structure), in vitro histone octamer chaperoning assay, biochemical reconstitution of rixosome subunit assembly, structural and functional domain analysis Science advances High 40712028
2019 PELP1 promotes glioblastoma progression by interacting with and functioning as a coactivator of β-catenin, activating Wnt/β-catenin target gene expression. PELP1 knockdown significantly reduced expression of Wnt/β-catenin pathway genes and improved survival of orthotopic GBM tumor-bearing mice. Co-immunoprecipitation, RNA-seq, reporter gene assays, siRNA knockdown, orthotopic mouse models Neuro-oncology advances Medium 32309805
2025 PELP1 interacts with FHL2 to potentiate transcriptional activation of downstream target genes including CCND1, CCND2, CDK6, ANG, CCL2, and MMP3 in ectopic endometrial stromal cells. PELP1 knockdown inhibited proliferation, angiogenesis, and inflammation in endometriosis models. Co-immunoprecipitation, siRNA knockdown, animal models, qRT-PCR, Western blotting Cell biology international Low 41165240

Source papers

Stage 0 corpus · 95 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2019 Metformin induces human esophageal carcinoma cell pyroptosis by targeting the miR-497/PELP1 axis. Cancer letters 191 30771436
2001 Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha. The Journal of biological chemistry 160 11481323
2004 Characterization of the interactions of estrogen receptor and MNAR in the activation of cSrc. Molecular endocrinology (Baltimore, Md.) 140 14963108
2014 Progesterone receptor-B enhances estrogen responsiveness of breast cancer cells via scaffolding PELP1- and estrogen receptor-containing transcription complexes. Oncogene 113 24469035
2013 Significance of PELP1/HDAC2/miR-200 regulatory network in EMT and metastasis of breast cancer. Oncogene 96 23975430
2010 PELP1 is a reader of histone H3 methylation that facilitates oestrogen receptor-alpha target gene activation by regulating lysine demethylase 1 specificity. EMBO reports 94 20448663
2005 Functional implications of altered subcellular localization of PELP1 in breast cancer cells. Cancer research 94 16140940
2004 Potential role of a novel transcriptional coactivator PELP1 in histone H1 displacement in cancer cells. Cancer research 84 15374949
2008 MNAR plays an important role in ERa activation of Src/MAPK and PI3K/Akt signaling pathways. Steroids 83 18261753
2003 Functional interactions between the estrogen receptor coactivator PELP1/MNAR and retinoblastoma protein. The Journal of biological chemistry 76 12682072
2012 Targeting the PELP1-KDM1 axis as a potential therapeutic strategy for breast cancer. Breast cancer research : BCR 72 22812534
2007 Functional and biological properties of the nuclear receptor coregulator PELP1/MNAR. Nuclear receptor signaling 60 17525794
2004 The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains. The Journal of biological chemistry 58 15456770
2013 PELP1 oncogenic functions involve CARM1 regulation. Carcinogenesis 52 23486015
2010 Involvement of the tubulin tyrosine ligase-like family member 4 polyglutamylase in PELP1 polyglutamylation and chromatin remodeling in pancreatic cancer cells. Cancer research 51 20442285
2016 Breast Tumor Kinase (Brk/PTK6) Is Induced by HIF, Glucocorticoid Receptor, and PELP1-Mediated Stress Signaling in Triple-Negative Breast Cancer. Cancer research 49 26825173
2013 PELP1: a review of PELP1 interactions, signaling, and biology. Molecular and cellular endocrinology 48 23933151
2005 The modulator of nongenomic actions of the estrogen receptor (MNAR) regulates transcription-independent androgen receptor-mediated signaling: evidence that MNAR participates in G protein-regulated meiosis in Xenopus laevis oocytes. Molecular endocrinology (Baltimore, Md.) 48 15831520
2011 Therapeutic targeting of PELP1 prevents ovarian cancer growth and metastasis. Clinical cancer research : an official journal of the American Association for Cancer Research 46 21421858
2006 Phosphorylation of MNAR promotes estrogen activation of phosphatidylinositol 3-kinase. Molecular and cellular biology 46 17194752
2005 Novel estrogen receptor coactivator PELP1/MNAR gene and ERbeta expression in salivary duct adenocarcinoma: potential therapeutic targets. Human pathology 45 16021574
2012 Central role for PELP1 in nonandrogenic activation of the androgen receptor in prostate cancer. Molecular endocrinology (Baltimore, Md.) 42 22403175
2016 PELP1: Structure, biological function and clinical significance. Gene 41 26997260
2008 Role of PELP1/MNAR signaling in ovarian tumorigenesis. Cancer research 40 18559538
2005 Hepatocyte growth factor-regulated tyrosine kinase substrate (HRS) interacts with PELP1 and activates MAPK. The Journal of biological chemistry 39 16352611
2011 Significance of PELP1 in ER-negative breast cancer metastasis. Molecular cancer research : MCR 38 22086908
2010 Cyclin-dependent kinase-mediated phosphorylation plays a critical role in the oncogenic functions of PELP1. Cancer research 38 20807815
2021 PELP1/SRC-3-dependent regulation of metabolic PFKFB kinases drives therapy resistant ER+ breast cancer. Oncogene 37 34103681
2008 PELP1--a novel estrogen receptor-interacting protein. Molecular and cellular endocrinology 34 18571832
2007 Identifying the estrogen receptor coactivator PELP1 in autophagosomes. Cancer research 34 17804729
2004 Cloning and functional characterization of PELP1/MNAR promoter. Gene 33 15087130
2005 Cloning, expression, and localization of MNAR/PELP1 in rodent brain: colocalization in estrogen receptor-alpha- but not in gonadotropin-releasing hormone-positive neurons. Endocrinology 32 16141397
2013 PELP1 oncogenic functions involve alternative splicing via PRMT6. Molecular oncology 31 24447537
2013 Vitamin C induces periodontal ligament progenitor cell differentiation via activation of ERK pathway mediated by PELP1. Protein & cell 30 23836152
2010 PELP1: A novel therapeutic target for hormonal cancers. IUBMB life 30 20014005
2012 Integration of ERα-PELP1-HER2 signaling by LSD1 (KDM1A/AOF2) offers combinatorial therapeutic opportunities to circumventing hormone resistance in breast cancer. Breast cancer research : BCR 28 22992372
2008 Growth factor regulation of estrogen receptor coregulator PELP1 functions via Protein Kinase A pathway. Molecular cancer research : MCR 27 18505929
2005 Characterization of MNAR expression. Steroids 26 16297421
2015 Novel role of PELP1 in regulating chemotherapy response in mutant p53-expressing triple negative breast cancer cells. Breast cancer research and treatment 25 25788226
2022 SETDB1 interactions with PELP1 contributes to breast cancer endocrine therapy resistance. Breast cancer research : BCR 24 35395812
2020 Gallic Acid Impedes Non-Small Cell Lung Cancer Progression via Suppression of EGFR-Dependent CARM1-PELP1 Complex. Drug design, development and therapy 24 32425504
2011 Regulation of rDNA transcription by proto-oncogene PELP1. PloS one 24 21695158
2018 Cancer Stem Cell Phenotypes in ER+ Breast Cancer Models Are Promoted by PELP1/AIB1 Complexes. Molecular cancer research : MCR 23 29348189
2007 Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1). Molecular endocrinology (Baltimore, Md.) 23 17505058
2003 Rapid extranuclear signaling by the estrogen receptor (ER): MNAR couples ER and Src to the MAP kinase signaling pathway. Molecular interventions 23 14993433
2014 The social network of PELP1 and its implications in breast and prostate cancers. Endocrine-related cancer 22 24859989
2007 Emerging significance of ER-coregulator PELP1/MNAR in cancer. Histology and histopathology 22 17128415
2014 PELP1 overexpression in the mouse mammary gland results in the development of hyperplasia and carcinoma. Cancer research 21 25377474
2008 MNAR functionally interacts with both NH2- and COOH-terminal GR domains to modulate transactivation. American journal of physiology. Endocrinology and metabolism 21 18682536
2014 Inhibition of mTOR signaling reduces PELP1-mediated tumor growth and therapy resistance. Molecular cancer therapeutics 20 24688046
2006 9-cis-retinoic acid up-regulates expression of transcriptional coregulator PELP1, a novel coactivator of the retinoid X receptor alpha pathway. The Journal of biological chemistry 20 16574651
2022 A First-in-Class Inhibitor of ER Coregulator PELP1 Targets ER+ Breast Cancer. Cancer research 19 35950923
2021 Altered Expression of ESR1, ESR2, PELP1 and c-SRC Genes Is Associated with Ovarian Cancer Manifestation. International journal of molecular sciences 18 34207568
2018 PELP1: a key mediator of oestrogen signalling and actions in the brain. Journal of neuroendocrinology 18 28485080
2009 Regulation of aromatase induction by nuclear receptor coregulator PELP1. The Journal of steroid biochemistry and molecular biology 18 19800002
2005 Developmental expression of MNAR mRNA in the mouse brain. Cell and tissue research 18 15846512
2015 Increased expression of proline-, glutamic acid- and leucine-rich protein PELP1 in non-small cell lung cancer. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 17 26211588
2006 Comprehensive analysis of recent biochemical and biologic findings regarding a newly discovered protein-PELP1/MNAR. Clinical & experimental metastasis 17 16826428
2022 Cryo-EM reveals the architecture of the PELP1-WDR18 molecular scaffold. Nature communications 16 36351913
2021 Interaction of transcription factor AP-2 gamma with proto-oncogene PELP1 promotes tumorigenesis by enhancing RET signaling. Molecular oncology 16 33269540
2020 PELP1 Suppression Inhibits Gastric Cancer Through Downregulation of c-Src-PI3K-ERK Pathway. Frontiers in oncology 16 32117782
2015 Cytoplasmic PELP1 and ERRgamma protect human mammary epithelial cells from Tam-induced cell death. PloS one 16 25789479
2006 Cloning, distribution, and colocalization of MNAR/PELP1 with glucocorticoid receptors in primate and nonprimate brain. Neuroendocrinology 16 17142998
2019 PELP1 promotes glioblastoma progression by enhancing Wnt/β-catenin signaling. Neuro-oncology advances 15 32309805
2014 PELP1 suppression inhibits colorectal cancer through c-Src downregulation. Oxidative medicine and cellular longevity 15 24967003
2019 PELP1 signaling contributes to medulloblastoma progression by regulating the NF-κB pathway. Molecular carcinogenesis 13 31872914
2016 Cytoplasmic Localization of Proline, Glutamic Acid, Leucine-rich Protein 1 (PELP1) Induces Breast Epithelial Cell Migration through Up-regulation of Inhibitor of κB Kinase ϵ and Inflammatory Cross-talk with Macrophages. The Journal of biological chemistry 13 27881676
2012 PELP1/MNAR suppression inhibits proliferation and metastasis of endometrial carcinoma cells. Oncology reports 13 22992812
2020 Estradiol-Induced MMP-9 Expression via PELP1-Mediated Membrane-Initiated Signaling in ERα-Positive Breast Cancer Cells. Hormones & cancer 12 32037484
2018 The Clinical Value of PELP1 for Breast Cancer: A Comparison with Multiple Cancers and Analysis in Breast Cancer Subtypes. Cancer research and treatment 10 30134648
2022 Targeting PELP1 Attenuates Angiogenesis and Enhances Chemotherapy Efficiency in Colorectal Cancer. Cancers 9 35053547
2022 Global Genomic and Proteomic Analysis Identified Critical Pathways Modulated by Proto-Oncogene PELP1 in TNBC. Cancers 9 35205680
2018 Increased expression of PELP1 in human sperm is correlated with decreased semen quality. Asian journal of andrology 9 29676290
2013 Temporal expression of Pelp1 during proliferation and osteogenic differentiation of rat bone marrow mesenchymal stem cells. PloS one 8 24146754
2022 Copy Number Variations Contribute to Intramuscular Fat Content Differences by Affecting the Expression of PELP1 Alternative Splices in Pigs. Animals : an open access journal from MDPI 7 35681846
2022 Expression of estrogen receptors, PELP1, and SRC in human spermatozoa and their associations with semen quality. Human cell 7 36577884
2017 Role of Scaffold Protein Proline-, Glutamic Acid-, and Leucine-Rich Protein 1 (PELP1) in the Modulation of Adrenocortical Cancer Cell Growth. Cells 7 29112114
2015 Estrogens Correlate with PELP1 Expression in ER Positive Breast Cancer. PloS one 7 26247365
2023 Targeting PELP1 oncogenic signaling in TNBC with the small molecule inhibitor SMIP34. Breast cancer research and treatment 6 37199805
2023 MiR-195-5p is involved in testicular ischemia/reperfusion injury by directly targeting PELP1 and regulating spermatogonia pyroptosis. International immunopharmacology 6 37290329
2013 Increased PELP1 expression in rat periodontal ligament tissue in response to estrogens treatment. Journal of molecular histology 6 23436000
2023 PELP1 inhibition by SMIP34 reduces endometrial cancer progression via attenuation of ribosomal biogenesis. Molecular oncology 5 37853941
2021 Overexpression of PELP1 in Lung Adenocarcinoma Promoted E2 Induced Proliferation, Migration and Invasion of the Tumor Cells and Predicted a Worse Outcome of the Patients. Pathology oncology research : POR 5 34257530
2022 PELP1 is overexpressed in lung cancer and promotes tumor cell malignancy and resistance to tyrosine kinase inhibitor drug. Pathology, research and practice 4 35969940
2021 PELP1 promotes the expression of RUNX2 via the ERK pathway during the osteogenic differentiation of human periodontal ligament stem cells. Archives of oral biology 4 33607589
2024 PELP1 Is a Novel Therapeutic Target in Hepatocellular Carcinoma. Cancer research communications 3 39258975
2021 Inflammation-induced PELP1 expression promotes tumorigenesis by activating GM-CSF paracrine secretion in the tumor microenvironment. The Journal of biological chemistry 3 34774800
2019 PELP1 is a novel oncogene in gastric tumorigenesis and negatively regulated by miR-15 family microRNAs. Cancer biomarkers : section A of Disease markers 3 31322541
2025 PELP1 coordinates the modular assembly and enzymatic activity of the rixosome complex. Science advances 2 40712028
2025 Effects of PELP1 on proliferation, metastasis and angiogenesis of epithelial ovarian cancer. Medical oncology (Northwood, London, England) 1 40715657
2025 The Interaction of PELP1 With FHL2 Contributes to Ectopic Endometrial Stromal Cell Proliferation, Angiogenesis, and Inflammation in Endometriosis. Cell biology international 1 41165240
2020 PELP-1 regulates adverse responses to endocrine therapy in Estrogen Receptor (ER) positive breast cancer. Oncotarget 1 33473257
2025 The PELP1 Pathway and Its Importance in Cancer Treatment. Biomolecules 0 41463382
2025 Proline-, Glutamic Acid-, Leucine-Rich Protein 1 (PELP1): Diversity, Structural Conservation, and Evolutionary Origins Across the Species. International journal of molecular sciences 0 41465416
2023 PELP1 and SRC kinase as important molecules in the estrogen-mediated pathway in human testis and epididymis. Acta biochimica Polonica 0 37159918

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