| 2001 |
hnRNP E2 (PCBP2) binds the 5'UTR of CEBPA mRNA and inhibits its translation, thereby suppressing C/EBPα protein expression in BCR-ABL-expressing myeloid precursor cells. BCR-ABL induces hnRNP E2 expression to mediate this translational block. |
Ectopic expression of hnRNP E2, Western blot for C/EBPα protein vs. CEBPA mRNA levels, functional differentiation assay |
Nature genetics |
High |
11753385
|
| 2007 |
BCR/ABL-activated MAPK(ERK1/2) phosphorylates hnRNP E2 (PCBP2) at serines 173, 189, 272 and threonine 213, stabilizing the protein. Phosphorylation is required for hnRNP E2 binding to the 5'UTR of CEBPA mRNA; serine/threonine to alanine substitutions abolish phosphorylation, decrease hnRNP E2 stability, and restore C/EBPα expression and granulocytic differentiation. |
Site-directed mutagenesis (S→A substitutions), pharmacologic MAPK inhibition, in vitro/in vivo differentiation assays, binding assays to CEBPA 5'UTR |
Blood |
High |
17475908
|
| 2010 |
miR-328 acts as a decoy by binding directly to hnRNP E2 (PCBP2) in a seed-sequence-independent manner, competing with CEBPA mRNA for hnRNP E2 binding, thereby releasing CEBPA mRNA from hnRNP E2-mediated translational inhibition. |
RNA-protein interaction assays, rescue differentiation assays, miR-328 restoration in CML-BC blasts |
Cell |
High |
20211135
|
| 2011 |
PCBP1 and PCBP2 function as iron chaperones that deliver Fe(II) to the HIF prolyl hydroxylases (PHD1/2/3) and asparaginyl hydroxylase FIH1. Depletion of PCBP1 or PCBP2 reduces PHD activity, impairs prolyl hydroxylation of HIF1α, and causes HIF1α accumulation; PHD activity is restored in vitro by adding purified Fe-PCBP1. PCBP1 physically binds PHD2 and FIH1 in vivo. |
RNAi depletion, in vitro activity reconstitution with purified Fe-PCBP1, co-immunoprecipitation (PCBP1 with PHD2/FIH1), HIF1α hydroxylation and degradation assays |
Cell metabolism |
High |
22055506
|
| 2011 |
UPF1 regulates hnRNP E2 (PCBP2) targets in myeloid differentiation. miR-328, induced during monocytic differentiation, acts as an RNA decoy for hnRNP E2, antagonizing its splicing-regulatory function on target pre-mRNAs (including S100A9) in 5'UTR introns, leading to upregulation of CD11b expression and ROS production. |
RNAi knockdown of UPF1/hnRNP E2, miR-328 overexpression, differentiation assays, splicing analysis |
Scientific reports |
Medium |
27573788
|
| 2013 |
PCBP2 is involved in poliovirus IRES-mediated translation initiation; viral proteinase 3CD cleaves PCBP2 in its linker region, which inhibits cap-independent translation but the cleaved form remains active in viral RNA replication. Inhibiting PCBP2 cleavage reduces viral RNA replication efficiency, indicating cleavage mediates a switch from translation to RNA replication. |
Proteinase inhibition, viral replication assays, analysis of cleaved vs. intact PCBP2 function |
Journal of virology |
Medium |
24371074
|
| 2013 |
PCBP2 and hnRNP A1 bind to both the 5' and 3' ends of murine norovirus (MNV-1) genomic RNA, stabilize 5'-3' RNA-RNA interactions, and induce circularization of the viral RNA. siRNA knockdown of PCBP2 or hnRNP A1 reduces virus yield, establishing a role for PCBP2 in RNA circularization required for efficient viral replication. |
RNA co-precipitation with antibodies, recombinant protein binding assays, electron microscopy of RNA circularization, siRNA knockdown with viral titer readout |
Journal of virology |
Medium |
23946460
|
| 2013 |
PCBP2 promotes glioma cell growth by binding FHL3 mRNA and destabilizing it, thereby suppressing FHL3 protein expression. Knockdown of PCBP2 stabilizes FHL3 mRNA and increases FHL3 protein, inducing apoptosis; FHL3 overexpression phenocopies PCBP2 knockdown. |
RIP-ChIP protein-RNA interaction arrays, mRNA stability assay, knockdown/overexpression, in vitro and in vivo growth assays |
The Journal of clinical investigation |
Medium |
23585479
|
| 2014 |
PCBP1 and PCBP2 deliver iron to deoxyhypusine hydroxylase (DOHH), a dinuclear iron enzyme required for hypusine modification of eIF5A. Cells depleted of PCBP1 or PCBP2 lose DOHH activity; lysates containing PCBP1/2 convert apo-DOHH to holo-DOHH in vitro with greater efficiency than depleted lysates. PCBP1 physically binds DOHH in iron-treated cells. PCBP depletion also reduced cytosolic aconitase activity without full [4Fe-4S] cluster disassembly. |
siRNA depletion, in vitro metallation reconstitution with cell lysates, co-immunoprecipitation of PCBP1 with DOHH, enzyme activity assays |
Proceedings of the National Academy of Sciences of the United States of America |
High |
24843120
|
| 2015 |
PCBP2 (but not PCBP1, PCBP3, or PCBP4) specifically binds ferroportin 1 (FPN1) in an iron-dependent manner, interacting with the C-terminal cytoplasmic region of FPN1. Iron-loaded but not iron-depleted PCBP2 interacts with FPN1. Silencing PCBP2 suppresses FPN1-dependent iron export from cells. |
Yeast and mammalian co-immunoprecipitation, domain mapping of FPN1 binding site, siRNA knockdown with iron export assay |
The Journal of biological chemistry |
High |
27302059
|
| 2015 |
PCBP2 contains nuclear-cytoplasmic shuttling activity and localizes to cytoplasmic stress granules (SGs) and a subset (~40%) of P-bodies under normal and stress conditions. Under heat or arsenic stress, PCBP2 accumulates predominantly at SGs but remains in Dcp1a-positive P-bodies. FRAP demonstrates PCBP2 dynamically moves in and out of SGs and P-bodies. |
Immunofluorescence, live-cell imaging, FRAP, subcellular fractionation |
RNA (New York, N.Y.) / Biochimica et biophysica acta |
Medium |
18174314 19230839
|
| 2015 |
IRTKS recruits the E2 SUMO ligase Ubc9 to sumoylate PCBP2 in the nucleus. Sumoylation causes PCBP2 cytoplasmic translocation during viral infection, where sumoylated PCBP2 associates with MAVS to initiate its K48-linked polyubiquitination and proteasomal degradation, attenuating antiviral signaling. |
Co-immunoprecipitation, sumoylation assays, subcellular fractionation, MAVS degradation assays with proteasome inhibitors, IRTKS knockdown |
Nature communications |
High |
26348439
|
| 2015 |
Pcbp2-null mouse embryos develop normally until midgestation (E12.5–13.5) but then undergo lethality associated with combined cardiovascular and hematopoietic abnormalities, demonstrating a non-redundant in vivo role for PCBP2 in hematopoiesis. Pcbp1 and Pcbp2 are individually essential for mouse embryonic development with distinct lethal stages. |
Targeted knockout mouse model, histological and hematopoietic analysis of embryos |
Molecular and cellular biology |
High |
26527618
|
| 2015 |
PCBP2 promotes stabilization of STAT1 and STAT2 mRNAs by binding C-rich elements in their 3'UTRs. This stabilization increases STAT1/STAT2 protein expression and phosphorylation, enhancing IFN-α antiviral activity against HCV. |
RIP-qRT-PCR, RNA half-life assays, RNA pull-down with biotinylated 3'UTR, overexpression and knockdown in HCV replicon cells |
PloS one |
Medium |
22022391
|
| 2015 |
STAT3 transcriptionally activates PCBP2 in EBV-positive B cells; high PCBP2 expression renders individual cells refractory to EBV lytic cycle activation. Suppression of PCBP2 levels is sufficient to increase the number of EBV lytic cells, placing PCBP2 downstream of STAT3 as a mediator of EBV latency maintenance. |
ChIP-seq analysis of STAT3 binding at PCBP2 locus, siRNA knockdown of PCBP2, separation of lytic vs. refractory cells, transcriptome analysis |
Journal of virology |
Medium |
25717101
|
| 2015 |
PCBP2 inhibits cardiac hypertrophy by promoting degradation of GPR56 mRNA in cardiomyocytes. PCBP2 knockdown enhances Ang II-induced hypertrophy; PCBP2 overexpression reverses it. GPR56 knockdown partially blocks PCBP2-dependent hypertrophic effects. |
Knockdown and overexpression in neonatal cardiomyocytes/H9C2 cells, mRNA stability assays, cell size and protein synthesis readouts |
Biochemical and biophysical research communications |
Medium |
26116532
|
| 2016 |
PCBP2 binds the 3'UTR of ARHGDIA mRNA and induces a local RNA structural change that favors subsequent binding of miR-151-5p and miR-16, suppressing ARHGDIA expression and promoting glioma cell migration and invasion. |
RIP, RNA structure probing, miRNA target assays, in vitro and in vivo migration/invasion assays |
Oncotarget |
Medium |
26761212
|
| 2016 |
PCBP2 binds the 3'UTR of CDK2 mRNA and stabilizes it, positively regulating CDK2 protein expression. CDK2 mediates PCBP2's pro-viability effect in gastric cancer cells. |
Ribonucleoprotein immunoprecipitation (RIP), biotin pulldown of CDK2 3'UTR, mRNA stability assay, CDK2 knockdown rescue |
FEBS open bio |
Medium |
29744291
|
| 2016 |
PCBP2 facilitates IRES-mediated c-myc translation via internal ribosome entry segment (IRES), downstream of β2-adrenergic receptor (β2-AR) signaling. β2-AR stimulation promotes PCBP2-β2-AR interaction, and knockdown of PCBP2 blocks β2-AR-induced c-myc protein increase. |
Immunoprecipitation-mass spectrometry (IP-MS), reciprocal co-IP, IRES reporter assay, siRNA knockdown |
Cancer letters |
Medium |
26803058
|
| 2016 |
SIRT6 suppresses PCBP2 expression in glioma by deacetylating H3K9ac at the PCBP2 promoter; SIRT6 levels are negatively correlated with PCBP2 and H3K9ac enrichment on the PCBP2 promoter. |
ChIP for H3K9ac at PCBP2 promoter, SIRT6 overexpression/knockdown, correlation analysis of SIRT6 and PCBP2 levels, in vitro and in vivo growth assays |
Biochemical and biophysical research communications |
Medium |
24607900
|
| 2016 |
PCBP2 regulates p73 (TAp73) expression by binding CU-rich elements in the p73 3'UTR and stabilizing p73 mRNA. PCBP2 knockout in MEFs decreases p73 expression and increases ROS production and cellular senescence in a TAp73-dependent manner. |
PCBP2 knockout and overexpression, mRNA stability assays, 3'UTR binding assays, ROS measurement, MEF senescence assay |
The Journal of biological chemistry |
Medium |
26907686
|
| 2017 |
NLRX1 recruits PCBP2 to MAVS, inducing K48-linked polyubiquitination and proteasomal degradation of MAVS during HCV infection, thereby attenuating interferon signaling. The NOD domain of NLRX1 is required for interaction with PCBP2. Mutagenesis confirmed domain requirements for PCBP2-NLRX1 interaction. |
Co-immunoprecipitation, mutagenesis of NLRX1 domains, ubiquitination assay, proteasome inhibitor treatment, NLRX1/PCBP2 depletion with IFN signaling readout |
Journal of virology |
High |
28956771
|
| 2017 |
An SRp75/hnRNPG complex interacts with hnRNP E2 (PCBP2), which activates splicing of tau exon 10. SRp75 binds the proximal downstream intron at the FTDP-17 hotspot region; hnRNPG and hnRNP E2 interact with SRp75 as shown by co-immunoprecipitation and co-transfection. |
Co-immunoprecipitation, RNAi knockdown, co-transfection splicing reporter assays |
Gene |
Medium |
21723381
|
| 2018 |
Pcbp2 enables definitive erythropoiesis by promoting inclusion of exon 6 of the Runx1 transcript. Pcbp2-null embryos show accentuated exclusion of Runx1 exon 6. Embryos homozygous for a Runx1 locus lacking exon 6 phenocopy the loss of definitive erythroid lineage in Pcbp2−/− embryos. |
Knockout mouse model, RNA-seq splicing analysis, Runx1 exon 6 conditional deletion (Runx1ΔE6) phenocopy |
Molecular and cellular biology |
High |
29866654
|
| 2019 |
PCBP2 isoform f interacts with the 5'UTR of eIF4G2 (DAP5) and Cyclin I mRNAs and inhibits their translation. eIF4G2, in turn, participates in cap-dependent translation of PCBP2 mRNA, forming a feedback loop between the translation factor and the RNA-binding protein. |
In vitro translation assay, cell-based translation reporter assay, RNA-binding assays, isoform-specific analysis |
RNA (New York, N.Y.) |
Medium |
31010886
|
| 2020 |
PCBP2 binds specifically to RNA carrying two closely spaced 8-oxoguanine (8-oxoG) residues (heavily oxidized RNA) via its conserved RNA-binding domains; mutations in these domains disrupt the interaction. In cells, PCBP2 suppresses apoptosis under oxidative conditions (opposite to PCBP1 which promotes apoptosis), as PCBP2-KO cells show increased caspase-3 activity and PARP1 cleavage under oxidative stress. |
Binding assays with 8-oxoG-containing RNA, site-directed mutagenesis of RNA-binding domains, PCBP2 knockout cell lines, caspase-3 activity and PARP cleavage assays |
The Journal of biological chemistry |
High |
32647012
|
| 2020 |
PCBP2 and DHX30 bind a CG-rich 3'UTR motif (CGPD-motif) and form a complex that represses translation of mRNAs carrying this motif in cells undergoing p53-dependent cell cycle arrest. Upon DHX30 depletion, CGPD-motif mRNA translation increases and the p53 response shifts toward apoptosis. |
Polysome profiling, UV-crosslinking/RIP to identify CGPD-motif interactors, DHX30 depletion/overexpression, translation and apoptosis assays |
Cell reports |
Medium |
32234473
|
| 2020 |
PCBP2 binds C-rich elements in the 3'UTR of sortilin mRNA and stabilizes it. Knockdown of PCBP2 decreases sortilin transcripts. Zn2+ reversibly inhibits the nucleotide-binding ability of PCBP2 in vitro, suggesting a Zn2+-sensitive mRNA stabilization mechanism. |
PCBP2 knockdown, mRNA stability assay, in vitro Zn2+ inhibition of RNA binding |
FEBS open bio |
Medium |
31961070
|
| 2020 |
PCBP2 stabilizes type I collagen α1(I) mRNA by binding its 3' end, increasing mRNA half-life. Alcohol upregulates PCBP2 in hepatic stellate cells, leading to increased collagen mRNA stability; siRNA knockdown of PCBP2 increases the decay rate of collagen α1(I) mRNA. |
PCBP2 siRNA, in vitro mRNA decay assay, Western blot for PCBP2 and collagen |
Pharmaceutical research |
Medium |
21643860
|
| 2020 |
PCBP2 directly binds the 3'UTR of RRM1 mRNA and cooperates with LINC02535 lncRNA to stabilize RRM1 mRNA. PCBP2 and LINC02535 co-localize in the cytoplasm, and together they promote DNA damage repair in cervical cancer cells. |
Co-IP, RIP, mRNA stability assay, co-localization by immunofluorescence, knockdown of PCBP2/LINC02535 |
Journal of cellular physiology |
Low |
32324262
|
| 2020 |
PCBP2 structure: cryo-EM reconstruction of full-length PCBP2 in complex with the apical region of poliovirus IRES stem-loop IV (SLIVm) resolved to 6.1 Å. PCBP2 interacts with the cruciform RNA via KH domains, featuring a prominent GNRA tetraloop. Cleavage of PCBP2 in its linker region by poliovirus 3CD proteinase makes the complex more flexible and reduces PCBP2 affinity for SLIVm, as shown by SEC-SAXS, SHAPE, hydroxyl-radical cleavage, and limited proteolysis/REMSA. |
CryoEM structure determination, SEC-SAXS, SHAPE analysis, hydroxyl-radical cleavage, REMSA, limited proteolysis |
Nucleic acids research |
High |
32556302
|
| 2022 |
PCBP2 directly interacts with cGAS and negatively regulates its enzymatic activity by antagonizing cGAS condensation (phase separation), reducing cGAMP production and thereby dampening cGAS-STING antiviral signaling. PCBP2 overexpression reduces antiviral signaling; PCBP2 loss increases cGAS activity. |
Co-immunoprecipitation, cGAMP production assay, cGAS condensation assay, PCBP2 overexpression/depletion with STING signaling readout |
Nature communications |
High |
35322803
|
| 2021 |
PCBP1 and PCBP2 are together required for erythroid differentiation; combined conditional inactivation causes midgestational repression of erythroid/hematopoietic gene expression, loss of blood formation, and fetal demise. They mediate overlapping and isoform-specific impacts on hematopoietic lineage transcriptome including mRNA representation and exon splicing. |
Conditional double knockout mouse model, RNA-seq transcriptome and splicing analysis, ex vivo primary erythroid progenitor cultures |
Molecular and cellular biology |
High |
34180713
|
| 2021 |
PCBP2 knockdown in malignant mesothelioma cells significantly decreases TfR1 and FTH expression and inhibits proliferation, indicating stagnation of intracellular iron transport. PCBP2 knockdown increases sensitivity to erastin-induced ferroptosis by increasing catalytic Fe(II) levels. |
siRNA knockdown, Western blot for TfR1/FTH, Fe(II) measurement, erastin-induced ferroptosis assay |
Pathology international |
Medium |
35089637
|
| 2021 |
PCBP2 knockdown in pancreatic stellate cells and fibroblasts reverses accumulation of type I collagen in the extracellular matrix, normalizing desmoplastic stroma and enhancing drug penetration into PDAC tumors. |
siRNA knockdown, in vitro collagen quantification, spheroid drug penetration assay, orthotopic mouse model |
Theranostics |
Medium |
33500719
|
| 2021 |
PCBP2 knockdown in extravillous trophoblasts (EVTs) impairs differentiation toward an invasive phenotype and causes transcript switching (alternative splicing) in genes controlling cellular assembly, proliferation, and cell cycle, with minimal effect on mRNA expression levels. |
siRNA knockdown, RNA-seq splicing analysis, Transwell invasion assay, placental explant culture |
Frontiers in cell and developmental biology |
Medium |
34095140
|
| 2022 |
Pcbp2 is essential for CD4+ T cell (Tconv) proliferation via regulation of co-stimulatory signaling. Pcbp2 deficiency in the CD4+ lineage does not affect Treg function but impairs Tconv proliferation and in vivo activation. Pcbp2 controls Runx1 exon 6 splicing in CD4+ T cells, connecting this splicing function to peripheral lymphocyte pool maintenance. |
Conditional Pcbp2 knockout in CD4+ T cells, proliferation assay, adoptive transfer colitis model, splicing analysis of Runx1 exon 6 |
iScience |
Medium |
36632062
|
| 2024 |
PCBP2 is required for pancreatic β cell function and adaptation to glucose. PCBP2 is induced by elevated glucose in primary mouse islets; Pcbp2-deficient β cells exhibit defects in calcium flux, insulin granule ultrastructure and exocytosis, and the amplification pathway of insulin secretion. PCBP2 impacts basal and glucose-regulated mRNAs encoding core components of the insulin secretory pathway. |
β cell-specific Pcbp2 knockout, transcriptomic analysis, calcium flux assay, electron microscopy of insulin granules, insulin secretion assay |
The Journal of clinical investigation |
High |
38950317
|
| 2024 |
PCBP1 and PCBP2 are required together for sustaining global mRNA translation in pancreatic β cells by stabilizing mRNAs encoding core translation initiation factors and ribosomal proteins through direct binding. Combined Pcbp1/2 deletion causes severe diabetes due to compromised β cell viability. |
β cell-specific Pcbp1 and combined Pcbp1/2 knockout, scRNA-seq, RIP for mRNA-protein interactions, mRNA stability assays, puromycin labeling for global translation monitoring |
Molecular metabolism |
High |
40451383
|
| 2024 |
PCBP2 stabilizes the mRNA of system Xc- components (SLC3A2/SLC7A11) and limits HIF1α/p300-HMGB1 signaling. In hepatic ischemia-reperfusion injury (HIRI), decreased PCBP2 compromises system Xc- stability, promotes ferroptosis, and enables HIF1α-driven HMGB1 secretion that worsens macrophage recruitment. |
PCBP2 knockdown in hepatocytes, mRNA stability assay for Slc3a2/Slc7a11, binding assay, HIRI mouse model with hepatocyte-specific PCBP2 knockdown |
Acta pharmaceutica Sinica. B |
Medium |
40486855
|
| 2024 |
Duck PCBP2 promotes DHAV-1 (picornavirus) replication via KH1 domain (aa 1–92) interaction with the viral RNA-dependent RNA polymerase 3Dpol, and facilitates IRES-mediated translation through interaction with stem-loop domains II and III of the DHAV-1 IRES. |
Biotinylated RNA pull-down, co-IP with 3Dpol, domain-specific interaction mapping, viral replication/translation assays |
Veterinary research |
Medium |
39300570
|
| 2025 |
PCBP2 acts as a direct interactor of an intracellular retention motif on miRNAs, binding miRNAs containing this motif (demonstrated by CLIP, RNA pull-down, and proteomics). PCBP2 requires SYNCRIP (an EV miRNA loader) for binding, as shown by SYNCRIP knockdown abolishing PCBP2-miRNA interaction. PCBP2 and SYNCRIP can co-bind miRNAs simultaneously (EMSA). PCBP2 acts as a dominant inhibitor of SYNCRIP-dependent miRNA loading into extracellular vesicles. |
CLIP coupled to RNA pull-down and proteomics, mutagenesis of retention motif, SYNCRIP knockdown, EMSA, PCBP2 knockdown with EV miRNA quantification |
eLife |
High |
40601477
|
| 2025 |
PCBP2 directly interacts with PARP1 mRNA, inhibiting m6A methylation at PARP1 mRNA and stabilizing it, leading to increased PARP1 expression and enhanced DNA repair activity that contributes to olaparib resistance in BRCA-mutated breast cancer. |
Co-IP of PCBP2 with PARP1 mRNA, m6A methylation assay, mRNA stability assay, knockdown/overexpression functional resistance assay |
Cancer research |
Medium |
40773674
|
| 2025 |
PCBP2 forms biomolecular condensates via phase separation in Alzheimer's disease brain. These condensates sequester mitochondrial and mRNA-binding proteins, impairing mitochondrial function and BACE1 mRNA stability. The small molecule CN-0928 binds INTS1, reduces PCBP2 protein level, inhibits condensate formation, and mitigates AD pathology. |
Phase separation assays, proteomics of condensate contents, PCBP2 level modulation, AD mouse models, CN-0928 target identification (INTS1 binding), cognitive readouts |
Nature communications |
Medium |
41298370
|
| 2025 |
PCBP2 is identified as an i-motif DNA-interacting protein. By destabilizing the i-motif structure, PCBP2 simultaneously reduces the mechanical stability of the facing G-quadruplex (by ~13.7 kcal/mol), enabling a replisome to bypass these DNA structural barriers during genome replication. |
Single-molecule force spectroscopy, PCBP2 identification as i-motif binding protein, quantitative mechanical stability measurements |
Angewandte Chemie (International ed. in English) |
Medium |
41327866
|
| 2025 |
A lncRNA BASP1-AS1 assembles a complex with ULK1 and LDHA, activating LDHA to increase lactate, which triggers PCBP2 K115 lactylation. This modification disrupts PCBP2-ARIH2 interaction, inhibiting ubiquitin-dependent degradation and stabilizing PCBP2 protein, which then suppresses ferroptosis and confers oxaliplatin resistance in gastric cancer. |
Multi-omics profiling, co-IP, ubiquitination assay, protein stability assay, LDHA activity assay, K115 lactylation site identification, organoid models |
Free radical biology & medicine |
Medium |
40914325
|
| 2025 |
PCBP2 promotes MAVS K48-linked polyubiquitination and proteasomal degradation during Dabie bandavirus (DBV/SFTS virus) infection, suppressing the MAVS-TBK1-IRF3 axis and type I interferon responses. PCBP2 overexpression enhances DBV replication; knockdown reduces it. |
Co-IP of PCBP2 with MAVS, ubiquitination assay, proteasome inhibitor treatment, PCBP2 overexpression/knockdown with IFN signaling and viral replication readouts |
Virus research |
Medium |
41638535
|
| 2016 |
PCBP2 was identified as the direct binding target of the immunosuppressive agent 15-deoxyspergualin (DSG) by pull-down assay. DSG treatment shifts PCBP2 intracellular localization from nucleus to cytoplasm. Overexpression of PCBP2 reduces the anti-proliferative activity of DSG. |
Biotinylated DSG probe pull-down, DSG binding confirmation, subcellular fractionation after DSG treatment, PCBP2 overexpression rescue assay |
Biochemical and biophysical research communications |
Low |
27261432
|
| 2025 |
PCBP2 promotes EGFR-driven tumor angiogenesis by binding miRNAs containing a 'GGGU' motif and promoting their loading into small extracellular vesicles (sEVs). EGFR overexpression transcriptionally upregulates PCBP2 protein, strengthening its binding to these miRNAs and their secretion via sEVs. PCBP2 depletion impairs EGFR-driven angiogenesis. |
miRNA pull-down assays, small RNA sequencing, PCBP2 depletion with sEV miRNA quantification, EGFR overexpression, co-culture and murine tumor models |
Theranostics |
Medium |
39816681
|