| 1997 |
DAXX was identified as a novel protein that binds specifically to the Fas death domain via its C-terminal portion, and a different region activates both JNK and apoptosis. Overexpression of DAXX enhances Fas-mediated apoptosis and activates the JNK pathway, defining a signaling pathway distinct from FADD. |
Protein-protein interaction (binding assay), overexpression, dominant-negative inhibition |
Cell |
High |
9215629
|
| 1998 |
DAXX activates the JNK kinase kinase ASK1 upon Fas stimulation; Fas activation induces DAXX to interact with ASK1, which relieves an inhibitory intramolecular interaction between the amino- and carboxyl-termini of ASK1, activating its kinase activity. |
Co-immunoprecipitation, kinase assay, dominant-negative ASK1 overexpression |
Science |
High |
9743501
|
| 1999 |
PML is essential for DAXX recruitment to nuclear domain 10 (ND10/PML nuclear bodies); in the absence of PML, DAXX localizes to condensed chromatin. SUMO-1 modification of PML is required for recruitment of DAXX from condensed chromatin to ND10, mediated by interaction between the C-terminal domain of DAXX and PML. |
Immunofluorescence, co-immunoprecipitation, PML-null cell lines, transient PML expression rescue |
The Journal of cell biology |
High |
10525530
|
| 1999 |
Daxx-deficient mice die early in embryogenesis with extensive apoptosis, demonstrating that Daxx functions in an anti-apoptotic capacity in vivo rather than solely as a pro-apoptotic factor. |
Gene knockout (mouse), TUNEL staining, embryonic lethality phenotype |
Genes & development |
High |
10444590
|
| 2000 |
DAXX functions as a transcriptional repressor that recruits histone deacetylases; PML sequesters DAXX to PML oncogenic domains (PODs) via SUMO-1-modified PML, inhibiting DAXX-mediated transcriptional repression. PML-RARalpha fusion does not inhibit DAXX repression. |
Reporter gene assay, immunofluorescence, yeast two-hybrid, biochemical fractionation |
Molecular and cellular biology |
High |
10669754
|
| 2000 |
Phosphorylated dimers of HSP27 interact with DAXX, preventing DAXX interaction with both ASK1 and Fas, and blocking Daxx-mediated apoptosis. HSP27 also blocks Fas-induced translocation of DAXX from the nucleus to the cytoplasm. |
Co-immunoprecipitation, dominant-negative and phosphorylation-mutant HSP27, apoptosis assays |
Molecular and cellular biology |
High |
11003656
|
| 2000 |
DAXX interacts with ETS1 through its C-terminal 173 amino acid region; this interaction represses transcriptional activation of ETS1 target genes MMP1 and BCL2. The ETS1 interaction domain in DAXX is conserved in several other Daxx-interacting proteins. |
Yeast two-hybrid, in vitro binding, co-localization, reporter gene assay, domain mapping |
Oncogene |
Medium |
10698492
|
| 2001 |
ASK1 controls the subcellular localization of DAXX: ASK1 sequesters DAXX in the cytoplasm, where DAXX is bound to activated Fas and mediates pro-apoptotic signaling. In the absence of ASK1, DAXX localizes to the nucleus and functions as a transcriptional repressor. |
Immunofluorescence, transcriptional reporter assay, co-immunoprecipitation |
The Journal of biological chemistry |
Medium |
11495919
|
| 2003 |
ATRX forms a chromatin-remodeling complex with DAXX; the ATRX-DAXX complex displays ATP-dependent chromatin-remodeling activities including triple-helix DNA displacement and mononucleosome disruption, distinct from SWI/SNF or NURD complexes. Both proteins co-localize in PML nuclear bodies. |
Co-immunoprecipitation, gel filtration, ATP-dependent chromatin remodeling assay, immunofluorescence |
PNAS |
High |
12953102
|
| 2003 |
RNAi-mediated depletion of endogenous DAXX in cell lines results in increased apoptosis (rescued by Bcl-2) and transcriptional derepression of NF-κB and E2F1 target genes, confirming DAXX has anti-apoptotic and transcriptional repressor functions. |
RNAi knockdown, apoptosis assay, Bcl-2 rescue, transcriptional reporter assay |
Journal of cell science |
High |
12482920
|
| 2003 |
Phosphorylation of DAXX at Ser667 by the ASK1-SEK1-JNK1-HIPK1 pathway mediates DAXX relocalization from nucleus to cytoplasm during glucose deprivation. Cytoplasmic DAXX then binds to ASK1, promoting ASK1 oligomerization and JNK1 activation. |
In vivo phosphorylation labeling, immune complex kinase assay, immunofluorescence, site-directed mutagenesis |
The Journal of biological chemistry |
Medium |
12968034
|
| 2004 |
DAXX binds to the C-terminal domain of p53 via its acidic domain; acetylation and phosphorylation of p53 regulate its interaction with DAXX. MDM2 expression restores DAXX-p53 interaction and correlates with p53 deacetylation. DAXX functions as a novel negative regulator of p53, suppressing p53-dependent apoptosis. |
Co-immunoprecipitation, GST pulldown, Lys-to-Ala mutagenesis, reporter assay, apoptosis rescue |
The Journal of biological chemistry |
Medium |
15364927
|
| 2004 |
DAXX functions as a negative coregulator of androgen receptor (AR) through direct protein-protein interaction with both the AR amino-terminal domain and DNA-binding domain; DAXX interferes with AR DNA-binding activity. Sumoylation of AR is involved in DAXX interaction and trans-repression. |
Co-immunoprecipitation, in vitro binding, ChIP, reporter assay, RNAi knockdown, EMSA |
Molecular and cellular biology |
High |
15572661
|
| 2005 |
DAXX is required for stress-induced cell death and JNK activation in primary fibroblasts. RNAi depletion of DAXX in primary fibroblasts renders cells resistant to UV- and oxidative stress-induced cell death and impairs MKK/JNK activation. |
RNAi knockdown, UV and oxidative stress apoptosis assays, JNK kinase assays in primary cells |
Cell death and differentiation |
Medium |
15861194
|
| 2006 |
DAXX is required for MDM2 stability: DAXX simultaneously binds MDM2 and the deubiquitinase HAUSP/USP7, mediating the stabilizing effect of HAUSP on MDM2. DAXX enhances the intrinsic E3 ligase activity of MDM2 toward p53. Upon DNA damage, DAXX dissociates from MDM2, correlating with MDM2 self-degradation and p53 activation. |
Co-immunoprecipitation, RNAi knockdown, overexpression, ubiquitination assay, DNA damage treatment |
Nature cell biology |
High |
16845383
|
| 2006 |
DAXX acts as a SUMO reader: SUMO modification of transcription factors (AR, GR, Smad4, CBP) recruits DAXX via its SUMO-interacting motif, causing transcriptional repression. SUMO-1-modified PML competes with SUMOylated transcription factors for DAXX binding, relieving DAXX-mediated repression. |
Reporter assay, co-immunoprecipitation, domain mapping, SUMO-interaction studies |
Biochemical Society transactions |
Medium |
18031230
|
| 2006 |
DNA damage triggers DAXX ubiquitination and proteasomal degradation; this releases RASSF1C from PML nuclear bodies. The released RASSF1C translocates to cytoplasmic microtubules and activates SAPK/JNK, linking nuclear DNA damage to cytoplasmic kinase signaling. |
Co-immunoprecipitation, immunofluorescence, siRNA knockdown, ubiquitination assay, JNK activation assay |
The EMBO journal |
Medium |
16810318
|
| 2006 |
Sumoylation of DAXX at K630/K631 is required for its nuclear localization and IFN-induced growth suppression of B lymphocytes; sumoylation-defective DAXX KA mutant localizes to the cytoplasm and fails to suppress growth. Nuclear localization via sumoylation is required for proper interaction with PML. |
Sumoylation-defective mutant expression, immunofluorescence, leptomycin B treatment, growth suppression assay |
Journal of immunology |
Medium |
16818774
|
| 2007 |
DAXX represses c-met transcription by binding to the c-met promoter and recruiting HDAC2; Daxx-null mouse cells show elevated c-met, which is reversed by Daxx reconstitution. Chromatin acetylation changes at the c-met promoter are dependent on DAXX. |
ChIP, Daxx-knockout mouse cells, reconstitution, chromatin acetylation assay |
Oncogene |
Medium |
17952115
|
| 2007 |
DAXX cooperates with the Axin/HIPK2/p53 complex to induce cell death: DAXX associates with Axin at endogenous levels (enhanced by UV); Axin tethers DAXX to p53 and cooperates with DAXX to stimulate HIPK2-mediated Ser46 phosphorylation and PUMA transcription. A DAXX mutant unable to interact with Axin fails to inhibit colony formation. |
Co-immunoprecipitation, UV irradiation, siRNA, HIPK2 kinase assay, colony formation |
Cancer research |
Medium |
17210684
|
| 2007 |
DAXX represses NF-κB transcriptional activity by inhibiting p65 acetylation; DAXX physically interacts with the p65 subunit of NF-κB (induced by TNFα), and this interaction prevents p300/CBP-mediated acetylation of p65, suppressing NF-κB target gene expression. |
ChIP, EMSA, co-immunoprecipitation, reporter assay, acetylation assay |
Journal of molecular biology |
Medium |
17362989
|
| 2009 |
CHIP (carboxyl terminus of Hsp70-interacting protein) interacts with DAXX in a stress-dependent manner, ubiquitinates DAXX at K630/K631 (competing with sumoylation), partitions DAXX to an insoluble compartment, and blocks HIPK2-DAXX interaction, thereby suppressing Ser46 phosphorylation of p53 and the p53-dependent apoptotic program. |
Co-immunoprecipitation, in vitro ubiquitination, microarray, dominant-negative and KO fibroblasts |
The Journal of biological chemistry |
Medium |
19465479
|
| 2009 |
HCMV pp71 protein promotes the SUMOylation of DAXX; pp71 displaces ATRX from DAXX and mediates DAXX degradation through a ubiquitin-independent, proteasome-dependent mechanism to stimulate viral immediate-early gene expression. |
Co-immunoprecipitation, proteasome inhibitor treatment, overexpression, viral infection assay |
Journal of virology |
Medium |
19369322
|
| 2009 |
DAXX directly represses C/EBPβ transcriptional activity; DAXX binds C/EBPβ via amino acids 190-400, decreases p300-mediated C/EBPβ acetylation, and suppresses basal and p300-enhanced C/EBPβ transcriptional activity. PML abrogates this repression by re-recruiting DAXX to PML-oncogenic domains. |
GST pulldown, co-immunoprecipitation, reporter assay, acetylation assay, immunofluorescence |
The Journal of biological chemistry |
Medium |
19690170
|
| 2010 |
Adenovirus E1B-55K binds DAXX and induces its proteasome-dependent degradation, independently of E4orf6, to counteract DAXX-mediated restriction of adenoviral replication. DAXX knockdown increases adenoviral mRNA synthesis and protein expression. |
Co-immunoprecipitation, RNAi, proteasome inhibitor, viral replication assay |
Journal of virology |
Medium |
20484509
|
| 2011 |
ATRX and DAXX mutations in pancreatic neuroendocrine tumors are associated with alternative lengthening of telomeres (ALT), indicating that the ATRX-DAXX complex participates in telomere chromatin remodeling and that its loss leads to a telomerase-independent telomere maintenance mechanism. |
Exome sequencing, immunohistochemistry for ATRX/DAXX loss, telomere FISH for ALT |
Science |
High |
21719641
|
| 2011 |
The EBV tegument protein BNRF1 disrupts the DAXX-ATRX chromatin remodeling complex at PML nuclear bodies; BNRF1 interacts with DAXX and displaces ATRX, supporting viral early gene activation. Knockdown of DAXX or ATRX reactivates EBV from latency. |
Co-immunoprecipitation, immunofluorescence, RT-PCR, RNAi knockdown, viral infection assay |
PLoS pathogens |
Medium |
22102817
|
| 2011 |
CK2 kinase phosphorylates DAXX at its SUMO-interacting motif (SIM) residues S737 and S739, promoting preferential binding to SUMO-1 over SUMO-2/3, causing DAXX preference for SUMO-1 conjugation and interaction with SUMO-1-modified factors. NMR structure shows DAXX-SIM binds SUMO-1 in a parallel orientation. Phosphorylation enhances DAXX sensitization to stress-induced apoptosis via antiapoptotic gene repression. |
NMR structure, phosphorylation assay, site-directed mutagenesis, reporter assay, apoptosis assay |
Molecular cell |
High |
21474068
|
| 2011 |
DAXX mediates activation-induced cell death (AICD) in microglia by triggering MST1 homodimerization, activation, and nuclear translocation upon IFN-γ stimulation. IFN-γ upregulates DAXX expression, and DAXX or MST1 depletion attenuates IFN-γ-induced microglial apoptosis. |
RNAi knockdown, immunofluorescence, kinase activation assay, MST1-null mice, primary microglia |
The EMBO journal |
Medium |
21572393
|
| 2011 |
NMR spectroscopy characterization of DAXX's two SUMO-interacting motifs (SIM-N and SIM-C): SIM-N binds SUMO-1 in a parallel orientation with ~4-fold higher affinity than SIM-C; SIM-N can bind intramolecularly to the adjacent N-terminal helical bundle, suggesting autoregulation. SIM-C mediates interaction with sumoylated ETS1 through SUMO-1. |
NMR spectroscopy, peptide binding assays, affinity measurements |
The Journal of biological chemistry |
High |
21383010
|
| 2012 |
DAXX promotes H3.3 loading at regulatory regions of activity-dependent genes in neurons upon membrane depolarization; calcineurin-mediated dephosphorylation of DAXX is a key molecular switch controlling its function upon neuronal activation. DAXX loss impairs both H3.3 deposition and transcriptional induction of activity-regulated genes. |
ChIP, FRAP, calcineurin inhibitor treatment, DAXX KO/knockdown, neuronal activity assay |
Neuron |
High |
22500635
|
| 2012 |
DAXX and ATRX are required to maintain a repressed chromatin environment at a CMV-promoter transgene array; ICP0 (HSV-1 E3 ubiquitin ligase) depletes DAXX and ATRX from the activated array. H3.3 is recruited but not incorporated into chromatin during activation, linking DAXX/ATRX to transcriptional repression and chromatin assembly. |
Single-cell live imaging, ChIP, RNAi, immunofluorescence with FISH, ATRX-null cell line |
Journal of cell science |
Medium |
22976303
|
| 2012 |
DAXX interacts with APC/C coactivators Cdc20 and Cdh1 (via D-box sequences near the N-terminal of DAXX), inhibits the degradation of APC/Cdc20 and APC/Cdh1 substrates, and causes a transient delay in mitotic progression. D-box deleted DAXX mutant loses this inhibitory activity. |
Co-immunoprecipitation, D-box mutant, APC/C substrate degradation assay, cell cycle analysis |
Carcinogenesis |
Medium |
23239745
|
| 2012 |
DAXX localizes to centromeres/pericentromeres during heat shock, and its presence at these regions is required for H3.3 incorporation into centromeric/pericentromeric heterochromatin under normal conditions and protection of epigenetic modifications under stress. |
Immunofluorescence, DAXX depletion, ChIP for H3.3 and histone modifications |
Nucleus |
Medium |
22572957
|
| 2013 |
ATM phosphorylates DAXX at Ser564 upon DNA damage; this phosphorylation disrupts the DAXX-MDM2 interaction, stabilizes p53, and facilitates p53 activation. Blockage of Ser564 phosphorylation prevents DAXX-MDM2 dissociation and inhibits DNA damage-induced p53 activation. |
Phosphorylation assay, site-directed mutagenesis (Ser564Ala), ATM inhibitor, co-immunoprecipitation, p53 activation assay |
PloS one |
Medium |
23405218
|
| 2014 |
BNRF1 forms a ternary complex BNRF1-DAXX-H3.3-H4 (replacing ATRX), demonstrated by co-immunoprecipitation and size-exclusion chromatography with purified components. BNRF1 promotes global mobilization of H3.3 and suppresses DAXX-ATRX-mediated H3.3 loading on viral chromatin, generating chromatin permissive for EBV latent gene expression. |
Co-immunoprecipitation, size-exclusion chromatography with purified proteins, FRAP, ChIP, immunofluorescence FISH |
Journal of virology |
High |
25275136
|
| 2014 |
Endogenous DAXX localizes to Cajal bodies, associates with telomerase, and regulates telomerase targeting to telomeres. DAXX knockdown reduces telomerase targeting to telomeres and leads to telomere shortening. Disease-associated DAXX mutations differentially affect interaction with binding partners and targeting to Cajal bodies. |
Co-immunoprecipitation, immunofluorescence, RNAi, telomere length analysis, disease mutant analysis |
Journal of cell science |
Medium |
25416818
|
| 2014 |
DAXX selectively represses IL-6 transcription in macrophages by binding to the IL-6 promoter and recruiting HDAC1, mediating histone deacetylation. DAXX silencing decreases HDAC1 association with the IL-6 promoter. |
ChIP, siRNA knockdown, co-immunoprecipitation, reporter assay |
The Journal of biological chemistry |
Medium |
24550390
|
| 2015 |
The DAXX/ATRX complex is co-enriched at tandem repetitive elements in mouse ESCs; global DNA hypomethylation promotes recruitment of the complex to tandem repeats including retrotransposons and telomeres. DAXX/ATRX-mediated repression involves Suv39h recruitment and H3K9 trimethylation to protect repeat elements from transcriptional de-repression. |
ChIP-seq, genome-wide binding analysis, RNA-seq, knockdown in hypomethylated cells |
Cell stem cell |
High |
26340527
|
| 2015 |
In the absence of DAXX, H3K9me3-enriched heterochromatin domains are structurally altered and become uncoupled from major satellite DNA; nucleolar structure and rDNA organization are also disrupted. DAXX loss increases global chromatin sensitivity to MNase digestion. |
Electron spectroscopic imaging (ESI), MNase digestion, immunofluorescence, Daxx-null cells |
Epigenetics & chromatin |
Medium |
26500702
|
| 2015 |
PML stabilizes cytoplasmic DAXX, and cytoplasmic DAXX inhibits reverse transcription of HIV-1 and other retroviruses; DAXX is found in the vicinity of incoming HIV-1 capsids and inhibits retroviral reverse-transcription and retrotransposition of endogenous retroviruses. |
PML/DAXX knockdown, reverse transcription quantitative assay, immunofluorescence, retrotransposition assay |
PLoS pathogens |
Medium |
26566030
|
| 2015 |
DAXX represses autophagy modulators DAPK3 and ULK1 in prostate cancer cells, thereby suppressing autophagy and promoting tumorigenicity; DAXX knockdown increases autophagic flux. |
Stable RNAi knockdown, mouse xenograft, ChIP, autophagic flux assay |
The Journal of biological chemistry |
Medium |
25903140
|
| 2016 |
Menin and DAXX directly interact to suppress neuroendocrine tumor cell proliferation by repressing membrane metallo-endopeptidase (MME) expression; this repression requires H3K9me3 at the MME promoter mediated partly by SUV39H1. The MEN1 T429K disease mutation reduces DAXX binding. |
Co-immunoprecipitation, ChIP, siRNA, xenograft, disease mutant analysis |
Cancer research |
Medium |
27872097
|
| 2016 |
DAXX directly binds to the DNA-binding domain of Slug, impeding HDAC1 recruitment and antagonizing Slug E-box binding to suppress EMT and cancer invasion. Under hypoxia, HIF-1α downregulates DAXX expression, promoting cancer invasion. |
Co-immunoprecipitation, in vitro binding, HDAC1 recruitment assay, ChIP, EMT assay, orthotopic mouse model |
Nature communications |
Medium |
28004751
|
| 2017 |
High-resolution X-ray crystal structure of the ATRX-DAXX interaction surface was determined. DAXX single amino acid substitutions that abrogate ATRX complex formation reveal that repression of specific endogenous retroviruses (ERVs) depends on DAXX but not ATRX. A biochemically distinct DAXX-SETDB1-KAP1-HDAC1 complex represses ERVs independently of ATRX and H3.3 incorporation. H3.3 stabilizes DAXX protein levels. |
X-ray crystallography, site-directed mutagenesis, biochemical fractionation, RNA-seq, co-immunoprecipitation |
Nature communications |
High |
29084956
|
| 2017 |
PTEN interacts with DAXX and directly regulates oncogene expression by modulating DAXX-H3.3 association on chromatin, independently of PTEN enzymatic activity. DAXX inhibition suppresses tumor growth in PTEN-deficient glioma. |
Co-immunoprecipitation, ChIP, DAXX siRNA, orthotopic xenograft, H3.3 ChIP-seq |
Nature communications |
Medium |
28497778
|
| 2017 |
CUL3-SPOP acts as an E3 ubiquitin ligase complex targeting DAXX for degradation; knockdown of SPOP and CUL3 leads to DAXX upregulation, which inversely correlates with VEGFR2, NOTCH1, DLL4, and NRP1 expression in endothelial cells. Simultaneous SPOP and DAXX knockdown reverses VEGFR2 downregulation. |
siRNA knockdown, protein expression analysis, epistasis knockdown experiment |
Scientific reports |
Medium |
28216678
|
| 2019 |
SUMO-2/3 interacts directly with DAXX and regulates its subcellular localization; alteration of SUMO-2/3 expression leads to altered DAXX nuclear/cytoplasmic distribution. Cytoplasmic DAXX inhibits proliferation and promotes apoptosis while nuclear DAXX has opposing effects in gastric cancer. |
Co-immunoprecipitation, immunofluorescence, SUMO-2/3 knockdown, cell biology assays |
Cell death & disease |
Medium |
32641734
|
| 2019 |
Acetylation of SUMO1 at K37, K39, or K46 reduces SUMO1 binding to the phosphorylated SIMs of PML and DAXX; X-ray crystal structures of acetylated SUMO1 variants bound to phosphoSIMs reveal structural plasticity providing a regulatory mechanism for SUMO-SIM interactions in PML nuclear bodies. |
X-ray crystallography, binding assays, acetylation mimetic mutants |
Structure |
High |
31879127
|
| 2019 |
DAXX-mediated repression of stem/pluripotent genes (NOTCH4, SOX2, OCT4, NANOG, ALDH1A1) in ER+ breast cancer is dependent on DNMT1; estradiol-mediated ER activation stabilizes DAXX protein, which is enriched at promoters of these genes and recruits DNMT1 for methylation. Endocrine therapy promotes DAXX degradation via increased proteasome activity. |
ChIP, DNMT1/DAXX knockdown, DNA methylation bisulfite sequencing, proteasome inhibitor |
Cancer research |
Medium |
31387918
|
| 2020 |
ATRX affects telomeric double-strand break repair by promoting sister telomere cohesion and through a DAXX-dependent pathway. Loss of telomeric cohesion combined with DAXX deficiency recapitulates all telomeric DSB repair phenotypes associated with ATRX loss, including ALT-associated PML bodies and T-SCEs. |
ATRX/DAXX deletion, telomere sister chromatid exchange assay, ALT-associated PML body analysis, cohesion assay |
PLoS biology |
Medium |
31895940
|
| 2020 |
Morc3 ATPase interacts with DAXX via Morc3 SUMOylation and Daxx SUMO binding; Morc3 knockout cells show reduced DAXX-mediated H3.3 incorporation at ERV regions and ERV de-repression. Morc3 mutant proteins that fail to interact with DAXX also fail to maintain ERV silencing. |
sgRNA screen, proteomics, Morc3 KO, H3.3 ChIP, SUMO-binding mutagenesis |
Nature communications |
Medium |
34650047
|
| 2020 |
Daxx loss in mouse pancreatic cells creates a permissive transcriptional state associated with dysregulation of endogenous retroviral elements (ERVs) and cooperates with inflammation and Men1 loss to alter cell state. DAXX-regulated ERV silencing is linked to its H3.3 chaperone function. |
Conditional mouse KO, RNA-seq, ERV analysis, inflammatory stress model, Men1 double KO |
Science advances |
Medium |
32821827
|
| 2021 |
DAXX prevents protein aggregation, solubilizes pre-existing aggregates, and unfolds misfolded species of model substrates and neurodegeneration-associated proteins (including p53 and MDM2) in an ATP-independent manner relying on its polyD/E region; DAXX can restore native conformation and function to aggregation-prone p53 cancer mutants. |
In vitro aggregation assay, disaggregation/unfolding assay, polyD/E domain mutagenesis, p53 functional restoration assay |
Nature |
High |
34408321
|
| 2022 |
DAXX and ATRX knockout cells show genome-wide reduction in p53 chromatin binding, loss of chromatin accessibility at p53 response elements (ChIP-seq and ATAC-seq), and depletion of H3.3 with accumulation of γH2AX at many p53 sites including subtelomeres, linking DAXX/ATRX histone chaperone function to p53 DNA damage response. |
DAXX/ATRX KO, ChIP-seq, ATAC-seq, RNA-seq, γH2AX assay |
Nature communications |
Medium |
36028493
|
| 2022 |
DAXX restricts an early, post-entry step of SARS-CoV-2 replication independently of SUMOylation but dependently on its D/E (polyD/E) domain, which is necessary for its protein-folding activity. SARS-CoV-2 PLpro (papain-like protease) promotes DAXX re-localization to cytoplasmic sites and proteasomal degradation. |
CRISPR/Cas9 screen, overexpression, domain deletion mutants, proteasome inhibitor, viral replication assay |
Nature communications |
Medium |
35508460
|
| 2023 |
DAXX provides a unique function in the histone chaperone network by recruiting histone methyltransferases to promote H3K9me3 catalysis on new H3.3-H4 prior to deposition onto DNA, providing a molecular mechanism for de novo H3K9me3 deposition and heterochromatin assembly. |
Exploratory interactomics, co-chaperone complex characterization, H3K9me3 methylation assay on H3.3-H4, ChIP |
Molecular cell |
High |
36868228
|
| 2023 |
DAXX interacts with SREBP1 and SREBP2 transcription factors via its SUMO-binding activity (SIM2); DAXX associates with lipogenic gene promoters through SREBPs to activate SREBP-mediated transcription and lipogenesis. A cell-permeable DAXX SIM2 peptide disrupts DAXX-SREBP1/2 interactions and inhibits lipogenesis and tumor growth. |
Co-immunoprecipitation, ChIP, SREBP2 knockdown, DAXX/SIM mutants, lipogenesis assay, xenograft, peptide competition |
Nature communications |
Medium |
37045819
|