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We propose that mutations in alpha thalassemia-mental retardation syndrome X-linked (ATRX (show ATRX Proteins))/death-domain associated protein (DAXX) prime alternative lengthening of telomeres activation by disrupting telomeric heterochromatin.
Structural and biochemical characterization of DAXX-ATRX (show ATRX Proteins) interaction.
Structural basis for DAXX interaction with ATRX (show ATRX Proteins).
Given the high frequency of ATRX (show ATRX Proteins) and DAXX mutations in cancer, these chromatin regulators likely play a key role in pathogenesis [review]
H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3.3-H4 binding and deposition requirements.
DAXX gene plays a role in the pathogenesis of neuroendocrine pancreatic neoplasms.
The widespread dynamic nature of DAXX methylation in association with trophoblast differentiation and placenta-associated pathologies is consistent with an important role for this gene in proper placental development and function.
findings reveal a previously unappreciated cross-talk between two crucial tumor suppressor genes, MEN1 and DAXX, thought to work by independent pathways
The interaction of Daxx C-terminal domain and androgen receptor (show AR Proteins) suppresses cholesterol synthesis.Daxx C-terminal domain binds directly to androgen receptor (show AR Proteins).
HDAC1 (show HDAC1 Proteins) and DAXX are co-repressors associated with epigenetic regulation that help to control promoter histone acetylation reactions involved in regulating GAD67 (show GAD1 Proteins).
data support a model in which activation of myogenic differentiation results in PML (show PML Proteins) NB loss, chromatin reorganization and DAXX relocalization, and provides a paradigm for understanding the consequence of PML (show PML Proteins) loss in other cellular contexts, such as during cancer development and progression
This study provides important details regarding the expression and post-translational modifications of DAXX in aging in the entire organism and provides reference data for the deregulation observed in age-associated diseases.
This is a promising novel therapeutic approach because it appears to be effective in a model producing severe injury by interfering with an array of proximal signals and effectors of the ischemic cascade, upstream of JNK (show MAPK8 Proteins), caspases, and BIM (show BCL2L11 Proteins) and BAX (show BAX Proteins) activation.
Daxx and Atrx (show ATRX Proteins) safeguard the genome by silencing repetitive elements when DNA methylation (show HELLS Proteins) levels are low.
The protein levels of Daxx is reduced in Stella (show DPPA3 Proteins)-null oocytes and embryos.
Daxx selectively represses IL-6 (show IL6 Proteins) transcription through HDAC1 (show HDAC1 Proteins)-mediated histone deacetylation
Overall, these data imply a regulatory role for Daxx in reovirus-induced apoptosis, depending on its location in the nucleus or cytoplasm.
phosphorylation of Daxx by RIP3 comprises an important part of ischemic necrosis in rat retinal ganglion cells
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.
Daxx, a HIPK kinase substrate in the apoptosis pathway, was phosphorylated by HIPK3 (show HIPK3 Proteins) at Ser (show SIGLEC1 Proteins)-669 in response to cAMP stimulation.
Daxx mRNA was detected in embryonic development from 6 h to 120 h and in all 11 selected zebrafish tissues, and Daxx expression first increased and then decreased during megalocytivirus infectious spleen and kidney necrosis virus infection.
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.
CENP-C binding protein
, ETS1-associated protein 1
, Fas-binding protein
, death domain-associated protein 6
, death-associated protein 6
, fas death domain-associated protein
, death-domain associated protein
, 28S ribosomal protein S29, mitochondrial
, death associated protein 3
, 28S ribosomal protein S29, mitochondrial-like
, Fas death domain-associated protein
, LOW QUALITY PROTEIN: death domain-associated protein 6
, death-associated protein 6 L homeolog