| 1998 |
PRMT2 (HRMT1L1) contains an N-terminal SH2 domain in addition to a methyltransferase core domain. The paralog HRMT1L2 (PRMT1) exhibited in vitro methyltransferase activity and complemented a yeast HMT1 mutant in vivo, establishing functional conservation; PRMT2 itself was identified as a putative arginine methyltransferase based on sequence homology. |
Sequence analysis, yeast complementation assay, in vitro methyltransferase assay (for HRMT1L2) |
Genomics |
Medium |
9545638
|
| 2001 |
PRMT2 (HRMT1L1) interacts with the hnRNP E1B-AP5 via its SH3 domain (not SH2), co-localizes with E1B-AP5 in the nuclear fraction, and was identified as a candidate methyltransferase responsible for in vivo RGG-box methylation of E1B-AP5. |
Yeast two-hybrid screening, in situ immunofluorescence co-localization, domain-deletion analysis |
The Biochemical journal |
Medium |
11513728
|
| 2006 |
PRMT2 directly binds RB through its AdoMet-binding domain (unlike PRMT1, PRMT3, PRMT4), forms a ternary complex with E2F1 in the presence of RB, represses E2F1 transcriptional activity in an RB-dependent manner, and PRMT2 knockout MEFs show increased E2F activity and accelerated S-phase entry. |
Co-immunoprecipitation, reporter assays, gene targeting (knockout MEFs), cell-cycle analysis, vascular injury model |
Experimental cell research |
High |
16616919
|
| 2007 |
PRMT2 acts as a coactivator of the androgen receptor (AR), interacting with the AR C-terminal region (identified by yeast two-hybrid). PRMT2 coactivation is blocked by a methyltransferase competitive inhibitor, indicating catalytic activity is required. Under androgen-free conditions PRMT2 is cytoplasmic; androgen treatment triggers co-nuclear translocation of AR and PRMT2, whereas AR antagonist hydroxyflutamide causes AR but not PRMT2 nuclear translocation. |
Yeast two-hybrid, luciferase reporter assays, immunofluorescence, methyltransferase inhibitor treatment |
The Journal of steroid biochemistry and molecular biology |
Medium |
17587566
|
| 2011 |
Three novel C-terminal splice variants of PRMT2 (PRMT2α, PRMT2β, PRMT2γ) have distinct subcellular localizations determined by their alternatively spliced C-termini. All variants bind ERα in vitro and in vivo via their N-terminal regions and enhance ERα-mediated transactivation. PRMT2 silencing enhances 17β-estradiol-induced proliferation by regulating E2F1 and E2F1-responsive genes. |
Confocal microscopy, GST pulldown, co-immunoprecipitation, luciferase reporter assays, siRNA knockdown |
The FEBS journal |
Medium |
22093364
|
| 2011 |
PRMT2 regulates LPS-induced lung inflammatory responses; Prmt2 gene dosage controls airway hyperresponsiveness, neutrophil recruitment, and IL-6/TNF-α expression. Loss of PRMT2 impairs nuclear accumulation of NF-κB in stimulated macrophages. |
Mouse knockout/monosomy model, cytokine measurement, NF-κB nuclear fractionation |
Journal of immunology |
Medium |
21957146
|
| 2015 |
PRMT2 is required for LXR-mediated ABCA1 expression and ABCA1-dependent cholesterol efflux in macrophages; Prmt2-/- bone marrow-derived macrophages show reduced ABCA1 expression and cholesterol efflux. PRMT2 expression is reduced under high-glucose conditions. |
Prmt2 knockout mouse BMDMs, cholesterol efflux assay, gene expression analysis |
PloS one |
Medium |
26288135
|
| 2017 |
PRMT2 interacts with the splicing factor SAM68 via its SH3 domain, regulates SAM68 subcellular localization, and promotes an increase in the BCL-XL/BCL-XS ratio in TNF-α or LPS stimulated cells, demonstrating a role in alternative splicing of BCL-X. |
Proteomics (SH3 domain pulldown/MS), co-immunoprecipitation in cells, RT-PCR BCL-X isoform analysis |
Journal of biochemistry |
Medium |
28057797
|
| 2018 |
PRMT2 is responsible for histone H3R8 asymmetric dimethylation (H3R8me2a). In glioblastoma, H3R8me2a enrichment at gene promoters/enhancers correlates with active histone marks and is required for oncogenic gene expression programs including cell cycle genes. Silencing or catalytic inactivation of PRMT2 inhibits GBM cell growth and glioblastoma stem cell self-renewal. |
ChIP-seq, siRNA/shRNA knockdown, catalytic mutant expression, in vitro and in vivo tumor models |
Nature communications |
High |
30382083
|
| 2018 |
PRMT2 associates with the actin nucleator Cobl through its SH3 domain and methylates Cobl's C-terminal actin-nucleating domain. This methylation is required for Cobl's actin-binding activity and its role in dendritic arborization of neurons. PRMT2 phenocopies Cobl in gain- and loss-of-function assays, and both its catalytic domain and SH3 domain are required for its effects on dendritogenesis. |
Co-immunoprecipitation, in vitro reconstitution, cellular reconstitution, in vitro methylation assay, gain/loss-of-function in neurons, actin-binding assay |
Developmental cell |
High |
29689199
|
| 2020 |
PRMT2 mediates H3R8me2a at the Bcl2 gene promoter, increasing chromatin accessibility for STAT3 and promoting Bcl2 expression. A catalytically inactive PRMT2 mutant or the type I PRMT inhibitor MS023 impairs these pro-tumorigenic functions in hepatocellular carcinoma cells. |
ChIP assay, catalytic mutant expression, PRMT inhibitor (MS023) treatment, apoptosis and proliferation assays |
Experimental cell research |
Medium |
32574605
|
| 2021 |
PRMT2 methylates TLR4 at R731 and R812 (catalyzed via residues M115), and methylates IRF3 at R285. Arginine methylation of TLR4 at R812 mediates TLR4-IRF3 interaction; methylation of IRF3 at R285 induces IRF3 dimerization and nuclear translocation, promoting IFN-β production via TLR4/IRF3 signaling. PRMT2 mutants H112Q and M115I and TLR4 R812K mutant reduce IRF3 transcriptional activity. |
Co-immunoprecipitation, in vitro methylation assay, site-directed mutagenesis, nuclear fractionation, luciferase reporter assay, IFN-β measurement |
Molecular immunology |
Medium |
34583098
|
| 2021 |
PRMT2 deposits repressive H3R8me2a at the SOCS3 promoter in colitis, inhibiting SOCS3 expression. Reduced SOCS3 prevents ubiquitination-mediated degradation of TRAF5, elevating TRAF5 and activating downstream NF-κB/MAPK signaling. PRMT2 overexpression aggravates and knockdown alleviates DSS-induced colitis. |
ChIP assay, lentiviral overexpression/knockdown in vivo, Western blot, DSS colitis mouse model |
British journal of pharmacology |
Medium |
34599829
|
| 2022 |
PRMT2 arginine-methylates BRD4 at R179, R181, and R183 (with PRMT4). This methylation promotes BRD4 recruitment to acetylated histones/chromatin, controls a transcriptional program, and is induced by DNA damage to promote BRD4 chromatin binding for DNA repair. BRD4 arginine methylation deficiency suppresses tumor growth and sensitizes cells to BET inhibitors and DNA damaging agents. |
Co-immunoprecipitation, in vitro methylation assay, ChIP assay, site-directed mutagenesis, tumor xenograft, drug sensitivity assay |
Science advances |
High |
36475791
|
| 2023 |
PRMT2 promotes HIV-1 latency by methylating HIV-1 Tat at R52, reinforcing Tat nucleolar sequestration by NPM1 and counteracting its incorporation into Super Elongation Complex (SEC) phase-separated condensates in the nucleoplasm, thereby inactivating Tat-dependent viral transcription. |
cDNA expression screening, co-immunoprecipitation, nucleolar/nuclear fractionation, phase-separation imaging, methylation assay, HIV latency cell line models, patient CD4+ T cell experiments |
Nature communications |
High |
37949879
|
| 2023 |
PRMT2-mediated H3R8me2a is enriched at the WNT5A promoter, enhancing WNT5A transcriptional expression and activating Wnt signaling to drive RCC malignant progression. |
ChIP assay, overexpression/knockdown in cell lines, in vivo xenograft |
Cell death & disease |
Medium |
37173306
|
| 2024 |
PRMT2 is activated by HIF1α under hypoxic conditions and its H3R8me2a activity is required for transcriptional activation of a subset of hypoxia-induced genes, driving glioblastoma cell migration and tumor progression. |
ChIP assay, HIF1α knockdown/overexpression, PRMT2 inactivation, mouse xenograft, clinical specimen correlation |
Cellular signalling |
Medium |
38341123
|
| 2024 |
PRMT2 promotes arginine methylation of β-catenin, inducing its proteasomal degradation, which transcriptionally inhibits GPX4 expression. This leads to ferroptosis and M1 polarization of microglia via the β-catenin-GPX4 axis in LPS-induced neuroinflammation and depression. |
Co-immunoprecipitation, Western blot (ubiquitination/degradation), siRNA knockdown, behavioral assays in mice |
Molecular neurobiology |
Medium |
38430350
|
| 2024 |
C15orf39 (PRMT2 IP) interacts with cytoplasmic PRMT2 and together they stabilize IκBα to suppress NF-κB signaling and reduce IL-6/TNF-α transcription in microglia under steady-state conditions. |
Co-immunoprecipitation, Western blot (IκBα levels), siRNA/overexpression, NF-κB reporter assay |
International journal of molecular sciences |
Low |
38892217
|
| 2025 |
Hypoxia triggers phosphorylation of PRMT2 at Serine 12 (within its N-terminal intrinsically disordered region) by CDK9, driving PRMT2 condensation into transcriptional condensates, which is required for its H3R8me2a activity and hypoxia-inducible gene expression in glioblastoma. |
Phosphorylation site mutagenesis, CDK9 inhibitor (TG02), condensate imaging, ChIP for H3R8me2a, in vivo xenograft |
Science China. Life sciences |
Medium |
40926175
|
| 2025 |
PADI4 citrullinates PRMT2 at R312, which stabilizes PRMT2 protein expression and enhances its function in promoting H3R8 histone arginine methylation-dependent transcription of ID1 and ID2. Citrullination also affects PRMT2 interaction with the deubiquitinase USP7. R312 mutation or GSK484 PADI4 inhibition reduces PRMT2 activity, stem-like properties, and cisplatin resistance in OSCC. |
Immunoprecipitation, Western blot (protein stability), ChIP, site-directed mutagenesis (R312), PADI4 inhibitor (GSK484), cancer stem cell assays |
Clinical and translational medicine |
Medium |
40078091
|
| 2025 |
In trigeminal neuropathic pain, nerve injury upregulates PRMT2 in sensory neurons, which promotes H3R8 asymmetric dimethylation at the miR-323-3p promoter, facilitating FOXA2 binding and upregulating miR-323-3p expression. Increased miR-323-3p reduces Kv2.1 potassium channel expression and currents, causing TG neuronal hyperexcitability. |
High-throughput sequencing, ChIP assay, siRNA knockdown, patch-clamp electrophysiology, in vivo pain behavioral assays |
Cell reports |
Medium |
40674210
|