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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 26 Aug 2015.

Death-domain associated protein

Daxx, hDaxx
This gene encodes a multifunctional protein that resides in multiple locations in the nucleus and in the cytoplasm. It interacts with a wide variety of proteins, such as apoptosis antigen Fas, centromere protein C, and transcription factor erythroblastosis virus E26 oncogene homolog 1. In the nucleus, the encoded protein functions as a potent transcription repressor that binds to sumoylated transcription factors. Its repression can be relieved by the sequestration of this protein into promyelocytic leukemia nuclear bodies or nucleoli. This protein also associates with centromeres in G2 phase. In the cytoplasm, the encoded protein may function to regulate apoptosis. The subcellular localization and function of this protein are modulated by post-translational modifications, including sumoylation, phosphorylation and polyubiquitination. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2008] (from NCBI)
Top mentioned proteins: PML, CAN, RAD54, p53, Histone
Papers on Daxx
Computational genomic analysis of PARK7 interactome reveals high BBS1 gene expression as a prognostic factor favoring survival in malignant pleural mesothelioma.
New
Zarogiannis et al., In Am J Physiol Lung Cell Mol Physiol, 07 Sep 2015
In the Gordon Mesothelioma study, 34 of them were assessed out of which SUMO1, UBC3, KIAA0101, HDAC2, DAXX, RBBP4, BBS1, NONO, RBBP7, HTRA2, STUB1 were significantly over- whereas TRAF6 and MTA2 were significantly under-expressed in MPM patients (Network 2).
Daxx and TCF4 interaction links to oral squamous cell carcinoma growth by promoting cell cycle progression via induction of cyclin D1 expression.
New
Chen et al., Taipei, Taiwan. In Clin Oral Investig, 24 Aug 2015
OBJECTIVES: Death domain-associated protein (Daxx) has been recently implicated as a positive factor in ovarian cancer and prostate cancer, but the role of Daxx in oral squamous cell carcinoma (OSCC) has never been addressed.
Histone H3.3 is required for endogenous retroviral element silencing in embryonic stem cells.
New
Impact
Banaszynski et al., Cambridge, United Kingdom. In Nature, 11 Jul 2015
Deposition at a subset of these elements is dependent upon the H3.3 chaperone complex containing α-thalassaemia/mental retardation syndrome X-linked (ATRX) and death-domain-associated protein (DAXX).
Alternative lengthening of telomeres phenotype in malignant vascular tumors is highly associated with loss of ATRX expression and is frequently observed in hepatic angiosarcomas.
New
Jeng et al., Taipei, Taiwan. In Hum Pathol, 05 Jul 2015
Recently, ALT has been found to be associated with inactivation of either α-thalassemia/mental retardation syndrome X-linked (ATRX) or death domain-associated (DAXX) protein.
Biomarker-driven diagnosis of diffuse gliomas.
Review
New
Brat et al., Atlanta, United States. In Mol Aspects Med, Jun 2015
Pediatric gliomas differ in their spectrum of disease from those in adults; high grade gliomas occurring in children frequently have mutations in H3F3A, ATRX and DAXX, but not IDH.
Molecular pathways in gliomagenesis and their relevance to neuropathologic diagnosis.
Review
New
Brat et al., Atlanta, United States. In Adv Anat Pathol, Jan 2015
Pediatric GBMs differ from those in adults and frequently have mutations in H3F3A, ATRX, and DAXX, but not IDH.
Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex.
New
Marmorstein et al., Philadelphia, United States. In Nat Commun, Dec 2014
Comparison of the structure with the unrelated H3.3-specific chaperone DAXX reveals nearly identical points of contact between the chaperone and histone in the proximity of H3.3 G90, although the mechanism for H3.3 G90 recognition appears to be distinct.
Update on the neuroprotective effect of estrogen receptor alpha against Alzheimer's disease.
Review
New
Li et al., Dalian, China. In J Alzheimers Dis, Dec 2014
The ERα-mediated inhibition of Death domain-associated protein (Daxx) translocation and the combination of membrane ERα and caveolin in caveolae may protect against AD.
The Role of Chemotherapy in Well-Differentiated Gastroenteropancreatic Neuroendocrine Tumors.
New
Pavel et al., Tampa, United States. In Front Horm Res, Dec 2014
It will also be important to evaluate whether newly discovered mutations in pancreatic NETs, such as DAXX/ATRX, are associated with response to chemotherapy.
Integrated genomic characterization of adrenocortical carcinoma.
New
Impact
Bertherat et al., Paris, France. In Nat Genet, Jun 2014
We performed exome sequencing and SNP array analysis of 45 ACCs and identified recurrent alterations in known driver genes (CTNNB1, TP53, CDKN2A, RB1 and MEN1) and in genes not previously reported in ACC (ZNRF3, DAXX, TERT and MED12), which we validated in an independent cohort of 77 ACCs.
Neuroendocrine tumors of the pancreas: current concepts and controversies.
Review
New
Adsay et al., Atlanta, United States. In Endocr Pathol, Mar 2014
Loss of expression of DAXX and ATRX proteins has been recently identified in 45 %.
Molecular genetics of gliomas.
Review
Brat et al., Atlanta, United States. In Cancer J, 2014
Pediatric GBMs have a distinctive molecular pathogenesis, as H3F3A and DAXX mutations are frequent, and their gene expression profile is different than adult GBMs.
DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition.
Impact
Patel et al., New York City, United States. In Nature, 2012
DAXX is a metazoan histone chaperone specific to the evolutionarily conserved histone variant H3.3.
Loss of ATRX or DAXX expression and concomitant acquisition of the alternative lengthening of telomeres phenotype are late events in a small subset of MEN-1 syndrome pancreatic neuroendocrine tumors.
GeneRIF
Matsukuma et al., Baltimore, United States. In Mod Pathol, 2012
These findings establish the existence of ATRX and DAXX defects and the alternative lengthening of telomeres phenotype in pancreatic neuroendocrine tumors in the context of MEN-1 syndrome
Interaction of dengue virus nonstructural protein 5 with Daxx modulates RANTES production.
GeneRIF
Limjindaporn et al., Bangkok, Thailand. In Biochem Biophys Res Commun, 2012
This work demonstrates the interaction between DENV NS5 and Daxx and the role of the interaction on the modulation of RANTES production.
Calcium-dependent dephosphorylation of the histone chaperone DAXX regulates H3.3 loading and transcription upon neuronal activation.
GeneRIF
Salomoni et al., London, United Kingdom. In Neuron, 2012
DAXX is associated with regulatory regions of selected activity-regulated genes, where it promotes H3.3 loading upon membrane depolarization. DAXX loss not only affects H3.3 deposition but also impairs transcriptional induction of these genes.
Death-associated protein 6 (Daxx) mediates cAMP-dependent stimulation of Cyp11a1 (P450scc) transcription.
GeneRIF
Chung et al., Taipei, Taiwan. In J Biol Chem, 2012
Daxx, a HIPK kinase substrate in the apoptosis pathway, was phosphorylated by HIPK3 at Ser-669 in response to cAMP stimulation.
Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma.
Impact
Jabado et al., Montréal, Canada. In Nature, 2012
Mutations in ATRX (α-thalassaemia/mental retardation syndrome X-linked) and DAXX (death-domain associated protein), encoding two subunits of a chromatin remodelling complex required for H3.3 incorporation at pericentric heterochromatin and telomeres, were identified in 31% of samples overall, and in 100% of tumours harbouring a G34R or G34V H3.3 mutation.
Daxx interacts with and modulates the activity of CREB.
GeneRIF
Shih et al., Taipei, Taiwan. In Cell Cycle, 2012
Depletion of endogenous Daxx by specific shRNA or overexpression of Daxx resulted in decreased or increased levels of the cAMP/PKA-induced reporter activity and target gene expression.
Altered telomeres in tumors with ATRX and DAXX mutations.
Impact
GeneRIF
Meeker et al., Baltimore, United States. In Science, 2011
study found 61% of pancreatic neuroendocrine tumors had abnormal telomeres; all of the tumors with abnormal telomeres had ATRX or DAXX mutations or loss of nuclear ATRX or DAXX protein
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