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ATRX, DAXX or MEN1 mutant pancreatic neuroendocrine tumors are a distinct alpha-cell signature subgroup
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Data show that phosphatase and tensin homolog (PTEN) interacts with death domain associated protein (DAXX) and, in turn PTEN directly regulates oncogene expression by modulating DAXX-histone H3.3 (H3.3) association on the chromatin.
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Daxx directly binds to the DNA-binding domain of Slug, impeding histone deacetylase 1 (HDAC1) recruitment and antagonizing Slug E-box binding. This, in turn, stimulates E-cadherin and occludin expression and suppresses Slug-mediated epithelial-mesenchymal transition (EMT) and cell invasiveness.
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Results show that the X-linked nuclear protein (ATRX)-Fas death domain-associated protein (DAXX) complex is involved in gene repression and telomere chromatin structure.
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disruption of CENP-B/Daxx-dependent H3.3 pathway deregulates heterochromatin marks H3K9me3, ATRX and HP1alpha at centromeres and elevates chromosome instability
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Disrupting the ATRX/DAXX complex and inhibiting telomerase activity in telomerase-positive cancer cells lead to the alternative lengthening of telomeres switch.
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Study found that enhanced nuclear accumulation of Daxx correlated with the malignant phenotype in gastric mucosa.
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ATRX or DAXX loss was proved to be an independent predictor for OS of PanNETs in a multivariate Cox regression analysis including well-established risk factors; tumor stage and tumor grade.
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Both primary Alternative lengthening of telomeres(ALT) -positive and ATRX/DAXX-negative PanNETs are independently associated with aggressive clinicopathologic behavior and displayed reduced recurrence-free survival. In contrast, ALT activation and loss of ATRX/DAXX are both associated with better overall survival in patients with metastases
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Whole-exome sequencing has identified recurrent mutations in the genes DAXX and ATRX, which correlate with loss of protein expression and alternative lengthening of telomeres (ALT).ALT and DAXX/ATRX loss in PanNETs was associated with shorter disease-free survival (DFS) and disease-specific survival (DSS) and likely plays a significant role in driving metastatic disease
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We propose that mutations in alpha thalassemia-mental retardation syndrome X-linked (ATRX)/death-domain associated protein (DAXX) prime alternative lengthening of telomeres activation by disrupting telomeric heterochromatin.
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Structural and biochemical characterization of DAXX-ATRX interaction.
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Structural basis for DAXX interaction with ATRX.
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Given the high frequency of ATRX and DAXX mutations in cancer, these chromatin regulators likely play a key role in pathogenesis [review]
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H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3.3-H4 binding and deposition requirements.
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DAXX gene plays a role in the pathogenesis of neuroendocrine pancreatic neoplasms.
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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.
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findings reveal a previously unappreciated cross-talk between two crucial tumor suppressor genes, MEN1 and DAXX, thought to work by independent pathways
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The interaction of Daxx C-terminal domain and androgen receptor suppresses cholesterol synthesis.Daxx C-terminal domain binds directly to androgen receptor.
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HDAC1 and DAXX are co-repressors associated with epigenetic regulation that help to control promoter histone acetylation reactions involved in regulating GAD67.
