| 2019 |
DDX5 resolves R-loops (RNA:DNA hybrids) in an ATP-dependent manner in vitro; its RGG/RG motif is methylated by PRMT5, and this methylation is required for DDX5 interaction with XRN2 and repression of cellular R-loops (but not for helicase enzymatic activity itself). DDX5 associates with XRN2 at transcriptional termination regions to facilitate RNA polymerase II release. |
In vitro R-loop resolution assay with recombinant DDX5, co-immunoprecipitation of DDX5-XRN2, DRIP-qPCR in DDX5-deficient cells, RGG/RG motif mutagenesis, identification of PRMT5 as the writer by binding/methylation assays |
The EMBO journal |
High |
31267554
|
| 2021 |
BRCA2 physically interacts with DDX5 and stimulates its DNA-RNA hybrid-unwinding helicase activity at DNA double-strand breaks (DSBs). The BRCA2-T207A breast cancer variant shows impaired interaction with DDX5, reducing DDX5 association with DNA-RNA hybrids near DSBs and altering RPA and RAD51 recruitment kinetics. |
Co-immunoprecipitation identifying DDX5 as BRCA2-interacting protein, in vitro helicase stimulation assay, DRIP at DSBs, analysis of BRCA2-T207A variant cells, RPA/RAD51 foci quantification |
The EMBO journal |
High |
33634895
|
| 2015 |
DDX5 functions as a transcriptional co-activator of the nuclear receptor RORγt in TH17 cells; this co-activation requires DDX5's intrinsic RNA helicase activity and binding of the lncRNA Rmrp. A Rmrp mutation corresponding to cartilage-hair hypoplasia reduced DDX5-RORγt interaction and RORγt target gene transcription. |
Co-immunoprecipitation of DDX5-RORγt complex, RNA helicase activity mutants, targeted Rmrp gene mutation in mice, chromatin occupancy studies, TH17 differentiation and inflammatory disease models |
Nature |
High |
26675721
|
| 2019 |
DDX5 is a highly active G-quadruplex (G4) resolvase that unfolds MycG4-DNA without requiring a single-stranded overhang; ATP hydrolysis is not directly coupled to G4-unfolding. DDX5 is enriched at G-rich chromatin sites including the MYC promoter and activates MYC transcription; G4-interactive small molecules inhibit DDX5's interaction with the MYC promoter. |
In vitro G4-unfolding assays, ATP hydrolysis decoupling experiments, ChIP-seq for DDX5 chromatin binding, MYC transcription assays, G4-stabilizing small molecule experiments |
Proceedings of the National Academy of Sciences of the United States of America |
High |
31548374
|
| 2020 |
DDX5 clears R-loops at or near DSBs to enable proper DNA repair. DDX5 binds RNA transcripts near DSBs (shown by CLIP), requires its helicase domain, is excluded from DSBs in a transcription- and ATM activation-dependent manner, and its deficiency leads to asymmetric chromosomal deletions and impaired homologous recombination (delayed EXO1 and RPA recruitment). |
CLIP (crosslinking immunoprecipitation), ChIP, DRIP-seq in DDX5-deficient cells, NHEJ reporter (EJ5-GFP), laser irradiation-induced damage foci, EXO1/RPA recruitment assays |
NAR cancer |
High |
33015627
|
| 2022 |
TOP3B resolves R-loops in coordination with DDX5 independently of TDRD3. IP-mass spectrometry and IP-western show TOP3B physically interacts with DDX5. DDX5 and TOP3B are epistatic in resolving R-loops in a pathway parallel with senataxin; TOP3B cleaves the single-stranded DNA displaced by R-loop RNA-DNA duplexes. |
IP-mass spectrometry, IP-western blotting, biochemical assays with recombinant TOP3B and oligonucleotide R-loop mimics, RNA/DNA hybrid IP-western, genetic epistasis |
Cell reports |
High |
35830799
|
| 2021 |
DDX5 interacts with the m6A writer METTL3 to regulate methylation of mRNAs including DHX58, p65, and IKKγ by affecting the METTL3-METTL14 heterodimer complex; DDX5 promotes m6A modification and nuclear export of these transcripts, leading to YTHDF2-dependent mRNA decay of antiviral transcripts and suppression of IFN-β signaling. |
Co-immunoprecipitation of DDX5-METTL3 complex, m6A sequencing, mRNA stability assays, nuclear export assays, viral infection models in vitro and in vivo |
PLoS pathogens |
Medium |
33909701
|
| 2022 |
DDX5 interacts with METTL3 and METTL14 to form an m6A writing complex that adds m6A to TLR2 and TLR4 transcripts, promoting their YTHDF2-mediated decay; upon bacterial infection, DDX5 is recruited to Hrd1 at the ER in a MyD88-dependent manner and degraded via the ubiquitin-proteasome pathway, disrupting the complex and allowing TLR2/4 upregulation and NF-κB activation. |
Co-immunoprecipitation of DDX5-METTL3/14 complex, m6A modification assays, YTHDF2 mRNA decay assays, bacterial infection models, MyD88-dependent recruitment assay, in vivo DDX5-KO and METTL3-KO mice |
EMBO reports |
High |
38182816
|
| 2021 |
DDX5 resolves a G-quadruplex structure (rG4) in the 5'UTR of STAT1 mRNA to enable STAT1 translation and interferon signaling. Direct and selective binding of helicase-active DDX5 to the WT STAT1-rG4 sequence was demonstrated by ribonucleoprotein and EMSA assays; CRISPR editing of the STAT1-rG4 sequence conferred resistance to rG4-stabilizing compounds. |
Luciferase reporter assays with WT vs. mutant rG4 sequence, rG4-stabilizing compounds, CRISPR/Cas9 editing of STAT1-rG4, circular dichroism, RNP/EMSA binding assays, IFN-α response assays |
Gut |
High |
34021034
|
| 2014 |
DDX5 and DDX17 cooperate with hnRNP H/F splicing factors to define epithelial- and myoblast-specific splicing subprograms during differentiation. DDX5/DDX17 downregulation during myogenesis and EMT contributes to splicing program switching; this downregulation is itself mediated by DDX5/DDX17-dependent miRNA production. |
RNA-seq of splicing events after knockdown, co-immunoprecipitation with hnRNP H/F, miRNA profiling, cell differentiation models |
Cell reports |
High |
24910439
|
| 2007 |
DDX5 (p68) and its paralog DDX17 (p72/p82) are required for 32S pre-rRNA cleavage and ribosome biogenesis; their apparently redundant role corresponds to RNA rearrangement (not unwinding) activity required for structural rearrangement within the pre-60S ribosomal subunit preceding 32S processing. Co-silencing of both genes causes nucleolar structure perturbation and cell death. |
siRNA knockdown of DDX5 and/or DDX17, RNA helicase mutant studies, nucleolar morphology analysis, pre-rRNA processing assays |
Nucleic acids research |
Medium |
17485482
|
| 2011 |
ARF limits the nucleolar localization of DDX5 by inhibiting the interaction between DDX5 and nucleophosmin (NPM), preventing DDX5 association with the rDNA promoter and nuclear pre-ribosomes. DDX5 promotes rRNA synthesis/maturation and ribosome output. |
Mass spectrometry of nucleolar proteins in Arf-deficient cells, Co-immunoprecipitation of DDX5-NPM, ChIP at rDNA promoter, DDX5 knockdown effects on ribosome biogenesis |
Cancer research |
Medium |
21937682
|
| 2012 |
DDX5 promotes DNA replication by directly regulating E2F-dependent gene promoters (recruiting RNA polymerase II to E2F-regulated gene promoters) to control DNA replication factor expression during G1-S phase progression. |
Episomal plasmid stability assay, ChIP for RNA Pol II at E2F promoters, DDX5 knockdown effects on replication factor expression, cell cycle analysis |
Cancer discovery |
Medium |
22750847
|
| 2008 |
DDX5 (p68) functions as a transcriptional co-activator of Runx2 in osteoblasts; p68 co-localizes with Runx2 in nuclear punctate foci. Helicase activity was not essential for Runx2 co-activation. Paradoxically, p68 suppression accelerated osteoblast differentiation, and Runx2 suppressed p68 expression in calvarial progenitors, revealing reciprocal regulation. |
Affinity purification/proteomics identifying p68-Runx2 interaction, co-localization by immunofluorescence, transcription reporter assays with helicase mutants, siRNA knockdown, osteoblast differentiation assays |
Journal of cellular biochemistry |
Medium |
17960593
|
| 2013 |
DDX5 (p68) functions as a co-activator in the Notch signaling pathway by directly interacting with RBP-J. DDX5 localizes to RBP-J binding sites at Notch target gene promoters (preTCRα, Hes1, CD25) in a Notch-dependent manner. The RNA co-activator SRA acts as a DDX5 cofactor in this context; DDX5/SRA co-activation is accompanied by p300 occupancy and histone acetylation. |
Biotinylation-tagging followed by mass spectrometry identifying DDX5 in RBP-J/NICD complex, biochemical interaction assays, ChIP at Notch target gene loci, siRNA knockdown, SRA knockdown/overexpression |
Biochimica et biophysica acta |
Medium |
23396200
|
| 2013 |
DDX5 (p68) unwinds the stem-loop IDX-rasISS1 structure in H-Ras pre-mRNA and prevents binding of hnRNP H to this structure, thereby regulating alternative splicing of H-Ras to modulate the ratio of p21/p19 H-Ras isoforms. p68 also alters dynamic localization of SC35 splicing factor. |
In vitro RNA unwinding assays, RNA-protein binding competition assays, SC35 localization by immunofluorescence, RNAi knockdown |
PloS one |
Medium |
18698352
|
| 2012 |
DDX5 binds the lncRNA mrhl RNA in mouse spermatogonial cells (identified by Northwestern blot and RNA pulldown); mrhl RNA downregulation causes cytoplasmic translocation of tyrosine-phosphorylated DDX5 (p68). Concomitant knockdown of both mrhl RNA and p68 prevented nuclear β-catenin translocation, placing DDX5 downstream of mrhl RNA in negative regulation of Wnt signaling. |
Northwestern blot, RNA pulldown identifying DDX5 as mrhl RNA binding protein, co-knockdown epistasis, β-catenin localization assays, TOP/FOP luciferase assay |
Molecular and cellular biology |
Medium |
22665494
|
| 2015 |
DDX5 directly interacts with β-catenin, promotes its nuclear translocation, and co-activates expression of cyclin D1 and c-Myc in NSCLC cells. β-catenin silencing abrogates DDX5-induced expression of these targets. |
Co-immunoprecipitation of DDX5-β-catenin, β-catenin nuclear localization assay, siRNA epistasis for cyclin D1/c-Myc expression, luciferase reporter assays |
Cancer science |
Medium |
26212035
|
| 2013 |
DDX5 (Ddx5) and DDX17 (ddx17) act as dual transcriptional coactivators of NFAT5 and simultaneously promote inclusion of NFAT5 exon 5, which introduces a premature termination codon triggering NMD of NFAT5 mRNA, thereby reducing NFAT5 protein level while enhancing NFAT5 transcriptional activity. |
Transcription reporter assays, alternative splicing analysis (RT-PCR), NMD pathway validation, siRNA knockdown, cell migration assays |
Oncogene |
Medium |
22266867
|
| 2013 |
DDX5 interacts with DDX3 (identified by yeast two-hybrid and confirmed by Co-IP); the interaction is enhanced in the G2/M phase when DDX5 accumulates in the cytoplasm. Dephosphorylation of serine/threonine residues in both DDX3 and DDX5 enhances their interaction (demonstrated by PP2A treatment). DDX3 knockdown blocks nuclear shuttling of DDX5, and both proteins are involved in mRNP export (UV cross-linking). |
Yeast two-hybrid, Co-immunoprecipitation, cell-cycle phase fractionation, PP2A/PTP1B phosphatase treatment, GST pulldown, UV cross-linking, siRNA knockdown with nuclear localization readout |
Journal of cellular biochemistry |
Medium |
22034099
|
| 2013 |
DDX5 binds hUpf3 (a component of the exon junction complex/NMD machinery) and activates NMD of Ddx17/p72 and Smg5 mRNAs. ATP-binding activity of DDX5 and the 3'UTR of target mRNAs are required for NMD triggering. DDX5 binding to Upf3 interferes with EJC binding. |
Co-immunoprecipitation of DDX5-Upf3, NMD reporter assays, ATP-binding mutant analysis, 3'UTR requirement assays |
Nucleic acids research |
Medium |
23788676
|
| 2014 |
DDX5 interacts with c-Myc and is required for c-Myc-mediated transcription and transforming activity. ARF blocks the physical interaction between DDX5 and c-Myc and displaces DDX5 from c-Myc target gene promoters. Forced c-Myc expression accelerates DDX5 protein synthesis, suggesting an oncogenic positive feedback loop. |
Tandem affinity purification identifying DDX5 as Arf-interacting protein, Co-immunoprecipitation of DDX5-c-Myc, ChIP at c-Myc target promoters, transcription assays, protein synthesis analysis |
Oncogene |
Medium |
24469041
|
| 2009 |
DDX5 acts as a repressor of fibrogenic genes in hepatic stellate cells by interacting with transcriptional complexes at fibrogenic gene promoters. The S480A SNP reduces DDX5 homodimer recruitment to fibrogenic promoters, increasing fibrogenic gene expression and Smad3/AP-1-responsive reporter activities without altering HDAC1 recruitment. |
Transient overexpression/siRNA knockdown with SNP replacement, stable expression of WT vs. SNP DDX5, promoter reporter assays, GAL4 one-hybrid system, ChIP for DDX5 homodimers at promoters |
The Journal of biological chemistry |
Medium |
20022962
|
| 2021 |
Thrap3 interacts with arginine-methylated DDX5 and co-localizes to R-loops. The Thrap3-DDX5 axis induces recruitment of XRN2 to R-loops; loss of Thrap3 increases R-loop accumulation and DNA damage. Arginine methylation of DDX5 is required for the DDX5-Thrap3 interaction. |
Co-immunoprecipitation of Thrap3-DDX5, R-loop localization assays, XRN2 recruitment assays, R-loop accumulation measurement in Thrap3-depleted cells, methylation requirement analysis |
Experimental & molecular medicine |
Medium |
34697388
|
| 2021 |
PAK5 phosphorylates DDX5 at threonine 69; this phosphorylation promotes sumoylation of DDX5 (phosphorylation-dependent sumoylation), which stabilizes DDX5. Both phosphorylation and sumoylation enhance formation of a DDX5/Drosha/DGCR8 complex, promoting microRNA-10b processing and breast cancer proliferation/metastasis. |
Kinase assay identifying DDX5-T69 as PAK5 substrate, Co-immunoprecipitation of DDX5/Drosha/DGCR8, sumoylation assays, PAK5-/-/MMTV-PyVT transgenic mice, miR-10b processing assays |
Cell reports |
Medium |
34936874
|
| 2017 |
DDX5 inhibits somatic cell reprogramming by repressing RYBP expression via processing of miR-125b. DDX5 disruption impedes miR-125b processing, leading to Rybp upregulation, H2AK119 ubiquitination by RYBP-dependent PRC1, and suppression of lineage genes. RYBP also mediates PRC1-independent OCT4 recruitment to the Kdm2b promoter. |
iPSC reprogramming efficiency assays in Ddx5 KO cells, miR-125b processing assays, RYBP overexpression/knockdown epistasis, H2AK119ub ChIP, OCT4 ChIP at Kdm2b promoter |
Cell stem cell |
Medium |
28111200
|
| 2013 |
DDX5 functions as a cellular co-factor of HIV-1 Rev, facilitating export of unspliced viral mRNAs. DDX5 binds Rev in a largely RNA-dependent manner; mutation of the DEAD-box motif abolishes DDX5-Rev interaction, indicating the DEAD-box motif is required for this interaction. |
Co-immunoprecipitation and confocal microscopy of DDX5-Rev, DEAD-box motif mutagenesis, Rev-RRE functional assays, HIV replication assays |
PloS one |
Medium |
23741449
|
| 2020 |
DDX5 potentiates HIV-1 transcription elongation as a co-factor of Tat; DDX5 binds both Tat and HEXIM1 and may facilitate dissociation of HEXIM1 from the 7SK-snRNP complex, enhancing Tat/P-TEFb availability. N-terminal RNA binding motifs, Walker B, and glycine doublet motifs of DDX5 are essential for this function. |
siRNA knockdown with DDX5 mutant rescue, Co-IP of DDX5-Tat and DDX5-HEXIM1, Tat/LTR reporter assays, HIV infectivity assays |
Retrovirology |
Medium |
32228614
|
| 2020 |
DDX5 suppresses type I IFN production by interacting with PP2A-Cβ; viral infection enhances the DDX5-PP2A-Cβ interaction. PP2A-Cβ interacts with IRF3 and deactivates it (dephosphorylation); DDX5 knockdown promotes IRF3 phosphorylation and IFN-I production and renders mice more resistant to viral infection. |
Co-immunoprecipitation of DDX5-PP2A-Cβ and PP2A-Cβ-IRF3, IRF3 phosphorylation assays, IFN-β production measurement, siRNA knockdown, viral infection in vivo mouse model |
Experimental cell research |
Medium |
33065113
|
| 2012 |
DDX5 is required for c-fos expression at multiple steps: transcriptional activation (recruited to c-fos gene upon estrogen), co-transcriptional RNA splicing, and mRNA export via efficient recruitment of the TAP mRNA export receptor. When splicing occurs post-transcriptionally in the absence of DDX5, c-fos mRNA is poorly exported. |
ChIP for DDX5 at c-fos gene locus, co-transcriptional splicing assays, TAP recruitment assays, mRNA export assays, DDX5 knockdown |
Nucleic acids research |
Medium |
23143267
|
| 2013 |
DDX5 and DDX17 are master regulators of estrogen and androgen receptor signaling pathways, controlling transcription and splicing of downstream target genes and of upstream regulators including GSK3β; DDX5/DDX17 control alternative splicing of GSK3β kinase, impacting ER and AR protein stability. |
RNA-seq of splicing events after DDX5/DDX17 knockdown, transcription reporter assays, ChIP, GSK3β splicing and ER/AR stability analysis |
Nucleic acids research |
Medium |
24275493
|
| 2013 |
DDX5 co-activates androgen receptor (AR)-dependent transcription in prostate cancer cells by forming a complex with nuclear β-catenin and recruiting AR and β-catenin to androgen-responsive promoters. DDX5 also co-immunoprecipitates with both processive and non-processive forms of RNA polymerase II and is found at elongating regions of the AR-mediated PSA gene. |
Co-immunoprecipitation of DDX5-β-catenin (nuclear fraction), ChIP at AR-responsive promoters, ChIP for elongating RNA Pol II, luciferase reporter assays, siRNA knockdown |
PloS one |
Medium |
23349811
|
| 2019 |
DDX5 is identified as the most enriched endogenous chromatin-bound Fra-1 interacting protein in TNBC cells, showing extensive overlap with Fra-1 cistrome; DDX5 enhances Fra-1 transcriptional activity and potentiates Fra-1-driven cell proliferation. |
Endogenous interaction profiling (IP of chromatin-bound Fra-1 + mass spectrometry), ChIP-seq overlap analysis, DDX5 overexpression reporter assays, cell proliferation assays |
Oncogene |
Medium |
31015574
|
| 2019 |
DDX5 acts as a transcriptional co-activator of PLZF (a transcription factor required for germline maintenance) in spermatogonia, regulating select target genes. DDX5 also regulates splicing of key spermatogenesis genes and controls cell cycle gene expression post-transcriptionally in undifferentiated spermatogonia. |
Inducible knockout mouse model, RNA-seq for splicing changes, Co-immunoprecipitation of DDX5-PLZF, target gene expression analysis |
Nature communications |
Medium |
31123254
|
| 2022 |
DDX5 inhibits IL-17D-induced skin inflammation by regulating pre-mRNA splicing in keratinocytes; DDX5 loss shifts IL-36R splicing toward membrane-bound intact IL-36R at the expense of soluble IL-36R (sIL-36R). IL-17D downregulates DDX5 expression via the CD93-p38 MAPK-AKT-SMAD2/3 signaling pathway. |
Keratinocyte-specific Ddx5 knockout mice, alternative splicing analysis by RT-PCR, IL-17D signaling pathway inhibitors, sIL-36R restoration experiments, skin inflammation disease models |
Nature immunology |
Medium |
36271146
|
| 2024 |
DDX5 regulates CaMKIIδ alternative splicing in cardiomyocytes to prevent production of CaMKIIδA isoform; DDX5 loss leads to CaMKIIδA accumulation, which phosphorylates L-type calcium channel (Cacna1c serine residues), impairing Ca2+ homeostasis and causing heart failure. AAV9-mediated CaMKIIδA knockdown partially rescues cardiac dysfunction in DDX5 KO mice. |
Cardiomyocyte-specific Ddx5 KO mice, AAV9 DDX5 overexpression, IP-mass spectrometry, RNA-seq, alternative splicing analysis, RNA immunoprecipitation sequencing, Ca2+ transient measurements, transverse aortic constriction HF model |
Circulation |
High |
39056171
|
| 2024 |
DDX5 inhibits cartilage fibrosis in osteoarthritis by regulating alternative splicing of Fn1 and Plod2 pre-mRNAs and by unfolding G-quadruplex structures in the Col2 promoter to promote COL2 expression; loss of DDX5 increases fibrosis-related (Col1, Acta2) and cartilage-degrading enzyme genes (Mmp13, Nos2). |
Chondrocyte-specific Ddx5 KO mice in OA model, alternative splicing analysis, G-quadruplex unfolding assays, gene expression analysis |
Nature aging |
Medium |
38760576
|
| 2018 |
DDX5 participates in oxLDL-induced macrophage MSR1 expression by stabilizing MSR1 mRNA; DDX5 interacts with METTL3 and inhibits METTL3-mediated m6A methylation of MSR1 mRNA, maintaining MSR1 mRNA stability and promoting lipid uptake. |
Co-immunoprecipitation of DDX5-METTL3, mass spectrometry identification, RNA-IP, dual luciferase reporter, mRNA stability assays (actinomycin D chase), siRNA knockdown |
Experimental cell research |
Medium |
29522752
|
| 2020 |
DDX5 deficiency in intestinal epithelial cells protected mice from intestinal tumorigenesis and DSS-induced colitis; DDX5 binds C3 and Fabp1 mRNA transcripts and augments their expression post-transcriptionally in a tissue-specific manner to promote oncogenesis. |
Intestinal epithelial-specific DDX5 KO mice, RNA-binding protein immunoprecipitation, DSS colitis model, tumorigenesis models |
Life science alliance |
Medium |
32817263
|
| 2023 |
DDX5 acts as a transcriptional co-repressor in RORγt+ Tregs, restricting expression of HIF1α and its downstream target IL-10; T cell-specific DDX5 knockout augments RORγt+ Treg suppressor activity and protects mice from intestinal inflammation. |
T cell-specific Ddx5 KO mice, IL-10 reporter assays, HIF1α inhibitor epistasis, intestinal inflammation model, transcriptomic analysis |
Science advances |
Medium |
36724232
|
| 2012 |
DDX5 (p68) directly interacts with VDR (vitamin D receptor) via the VDR ligand-binding domain in a manner that does not require an LXXLL motif; DDX5 co-localizes with VDR in keratinocyte nuclei and acts as a co-activator for calcitriol-dependent transcription. This interaction parallels known DDX5 interactions with ERα and AR. |
Genome-wide protein-protein interaction screen using VDR as bait, domain analysis of VDR-DDX5 interaction, VDR helix 12 mutant analysis, co-localization in HaCaT cells, transcription reporter assays, shRNA knockdown |
Molecular and cellular endocrinology |
Medium |
22476084
|
| 2018 |
DDX5 regulates microRNA biogenesis; LMTK3 binds via DDX5 to pri-miRNAs of miR-34a, miR-196-a2, and miR-182, sequestering them from processing. DDX5 is thus involved in the Microprocessor complex activity for miRNA processing. |
Co-immunoprecipitation of LMTK3-DDX5, pri-miRNA binding assay, miRNA expression profiling, functional proliferation/invasion assays |
Cancer letters |
Low |
26739063
|
| 2013 |
DDX5 (p68) binds JEV core protein, NS3, and NS5 (MTase and RdRp domains) as shown by GST pulldown and Co-IP; DDX5 is recruited to the cytoplasm and co-localizes with viral proteins and RNA. DDX5 binds specifically to the JEV 3'UTR by RNA pulldown. Helicase activity is required for DDX5's pro-viral role; DDX5 knockdown reduces JEV replication but not virus assembly/release. |
GST pulldown, Co-immunoprecipitation, confocal co-localization, RNA pulldown, JEV-replicon system, siRNA knockdown with helicase mutants |
Antiviral research |
Medium |
24035833
|
| 2024 |
MCM8 interacts with DDX5 and DHX9; loss of MCM8 reduces retention of DDX5 and DHX9 at R-loops, leading to R-loop accumulation and genome instability. MCM8 premature ovarian insufficiency-causative mutants with decreased DDX5 interaction display increased R-loop levels. |
Co-immunoprecipitation of MCM8-DDX5/DHX9, R-loop quantification in MCM8-deficient cells, MCM8 mutant interaction analysis, primordial germ cell proliferation assays in MCM8 KO mice |
The EMBO journal |
Medium |
38858601
|
| 2018 |
DDX5 knockdown in basal breast cancer cells causes actin cytoskeleton reorganization via a DDX5→miR-182→actin cytoskeleton pathway; DDX5 regulates miR-182 (and miR-21) levels, and loss of miR-182 upregulates cofilin and profilin, key actin polymerization proteins. Treatment with miR-182 inhibitors phenocopies DDX5 knockdown. |
Quantitative proteomics, global miRNA profiling, DDX5 knockdown, miR-182 inhibitor treatment, actin cytoskeleton morphology analysis, PDCD4 (miR-21 target) upregulation assay |
Molecular & cellular proteomics |
Medium |
22086602
|
| 2021 |
AURKA forms a transcriptional coactivator complex with DDX5 to induce transcription of lncRNA TMEM147-AS1 in epithelial ovarian cancer; this occurs via direct binding of AURKA to DDX5. The feedback loop AURKA/DDX5/TMEM147-AS1/let-7 maintains cisplatin resistance via lipophagy activation. |
Co-immunoprecipitation of AURKA-DDX5, transcription assays at TMEM147-AS1 promoter, functional cisplatin resistance assays, mathematical modeling |
Cancer letters |
Low |
37217070
|
| 2018 |
DDX5 is O-GlcNAcylated by OGT; DDX5 directly interacts with OGT in SW480 cells, and O-GlcNAcylation promotes DDX5 protein stability. The OGT-DDX5 axis activates AKT/mTOR signaling to promote colorectal cancer progression. |
Co-immunoprecipitation of DDX5-OGT, O-GlcNAcylation assays, protein stability analysis (cycloheximide chase), AKT/mTOR pathway analysis, siRNA knockdown |
Journal of cellular and molecular medicine |
Low |
30484950
|
| 2021 |
HSP90 interacts directly with DDX5 and inhibits DDX5 protein degradation through the AMPK/ULK1-regulated autophagy pathway; HSP90 inhibition reduces DDX5 levels and blocks HCC tumor growth. DDX5 accumulation activates β-catenin signaling. |
Molecular docking, co-immunoprecipitation of DDX5-HSP90, autophagy pathway analysis (AMPK/ULK1), HSP90 inhibitor experiments, xenograft tumor models |
Cancer biology & medicine |
Medium |
33764710
|
| 2018 |
In oligodendrocytes, DDX5 localizes to heterogeneous cytoplasmic RNP complexes associated with Mbp mRNA in cell body and processes; DDX5 level inversely affects MBP protein level post-transcriptionally, and DDX5 knockdown increases MBP isoforms containing exon 2 (via alternative splicing regulation), indicating a dual role in translational repression and alternative splicing of Mbp. |
RNP complex immunoprecipitation with Mbp mRNA, DDX5 knockdown with MBP protein level measurement, alternative splicing analysis by RT-PCR, subcellular localization by immunofluorescence |
Journal of cell science |
Medium |
29622601
|
| 2022 |
The m6A reader YTHDC1 interacts with DDX5 in rhabdomyosarcoma cells; DDX5 and YTHDC1 co-operatively promote production of a common subset of circRNAs by mediating back-splicing. YTHDC1/DDX5 depletion reduces RMS cell proliferation. |
Co-immunoprecipitation of YTHDC1-DDX5, circRNA sequencing, back-splicing assays, siRNA knockdown of YTHDC1/DDX5 with proliferation readout |
Nature communications |
Medium |
37019933
|
| 2020 |
Genome-wide DRIP-seq mapping revealed that DDX5-, XRN2-, and PRMT5-deficient cells share many R-loop gain loci at transcription termination sites (consistent with coordinated RNA Pol II termination), but DDX5-depleted cells uniquely accumulate R-loops near transcription start sites, suggesting an independent role for DDX5 in transcription initiation. R-loop accumulation at certain loci in DDX5-deficient cells induces antisense intergenic transcription. |
DRIP-seq (genome-wide R-loop mapping) in DDX5-, XRN2-, and PRMT5-deficient cells, bioinformatic analysis of R-loop gain/loss loci |
Life science alliance |
Medium |
32747416
|