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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 03 Oct 2014.

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, Sp100, Ubiquitin, p53
Papers on Daxx
Sp100 isoform-specific regulation of human adenovirus 5 gene expression.
New
Schreiner et al., Hamburg, Germany. In J Virol, Jun 2014
In contrast, the PML-associated proteins Daxx and ATRX are inhibited by early viral factors.
DAXX co-folds with H3.3/H4 using high local stability conferred by the H3.3 variant recognition residues.
New
Black et al., Philadelphia, United States. In Nucleic Acids Res, Apr 2014
We now focus on the dynamic features of the DAXX histone chaperone that have been elusive from previous structural studies.
Death domain-associated protein 6 (Daxx) selectively represses IL-6 transcription through histone deacetylase 1 (HDAC1)-mediated histone deacetylation in macrophages.
New
Cao et al., Beijing, China. In J Biol Chem, Apr 2014
As a multifunctional nuclear protein, death domain-associated protein 6 (Daxx) regulates a wide range of biological processes, including cell apoptosis and gene transcription.
Mislocalization of the centromeric histone variant CenH3/CENP-A in human cells depends on the chaperone DAXX.
New
Almouzni et al., France. In Mol Cell, Mar 2014
Ectopic localization of this particle depends on the H3.3 chaperone DAXX rather than the dedicated CenH3 chaperone HJURP.
Reversible silencing of cytomegalovirus genomes by type I interferon governs virus latency.
New
Cičin-Šain et al., Braunschweig, Germany. In Plos Pathog, Feb 2014
IFN blocked the viral lytic replication cycle by upregulating the nuclear domain 10 (ND10) components, PML, Sp100 and Daxx, and their knockdown by shRNA rescued viral replication in the presence of IFNβ.
Virion factors that target Daxx to overcome intrinsic immunity.
Review
New
Wodrich et al., Hamburg, Germany. In J Virol, Oct 2013
A number of recent reports suggest that several virion proteins may also play vital roles in gene activation processes, in particular by counteracting intrinsic immune mechanisms mediated by the PML nuclear body-associated cellular factors Daxx, ATRX, and Sp100.
Neuroendocrine tumours: cracking the epigenetic code.
Review
New
Thirlwell et al., London, United Kingdom. In Endocr Relat Cancer, Jun 2013
Recent progress has been facilitated by development of high-throughput tools including second-generation sequencing and arrays for analysis of the 'epigenome' of tumour and normal tissue, permitting unbiased approaches such as exome sequencing that identified mutations of chromatin-remodelling genes ATRX/DAXX in 44% of pancreatic NETs.
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.
Molecular pathology and genetics of pancreatic endocrine tumours.
Review
Delle Fave et al., Roma, Italy. In J Mol Endocrinol, 2012
Mutations of DAXX and ATRX are common and related to altered telomeres but not to prognosis.
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.
[Death domain-associated protein (DAXX)-mediated regulation of transcription and cell death].
Review
Muromoto, Sapporo, Japan. In Yakugaku Zasshi, 2011
Death domain-associated protein (DAXX) is a multifunctional protein that modulates both cell death and transcription.
Interplay between human cytomegalovirus and intrinsic/innate host responses: a complex bidirectional relationship.
Review
Varani et al., Bologna, Italy. In Mediators Inflamm, 2011
We review the viral and cellular partners that mediate early host responses to HCMV with regard to the interaction between structural components of virions (viral glycoproteins) and cellular receptors (attachment/entry receptors, toll-like receptors, and other nucleic acid sensors) or intrinsic factors (PML, hDaxx, Sp100, viperin, interferon inducible protein 16), the reactions of innate immune cells (antigen presenting cells and natural killer cells), the numerous mechanisms of viral immunoevasion, and the potential exploitation of events that are associated with early phases of virus-host interplay as a therapeutic strategy.
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
DAXX/ATRX, MEN1, and mTOR pathway genes are frequently altered in pancreatic neuroendocrine tumors.
Impact
GeneRIF
Papadopoulos et al., Baltimore, United States. In Science, 2011
identification of mutations in pancreatic neuroendocrine tumors; 44% had somatic inactivating mutations in MEN1; 43% had mutations in genes encoding DAXX and ATRX; clinically, mutations in MEN1 and DAXX/ATRX genes were associated with better prognosis
Distinct factors control histone variant H3.3 localization at specific genomic regions.
Impact
Allis et al., New York City, United States. In Cell, 2010
Immunoaffinity purification and mass spectrometry reveal that the proteins Atrx and Daxx associate with H3.3 in a Hira-independent manner.
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