DAXX in cancer: phenomena, processes, mechanisms and regulation.
Adaptor Proteins, Signal Transducing
/ chemistry
Cell Line, Tumor
Chromatin
/ chemistry
Co-Repressor Proteins
Gene Expression Regulation, Neoplastic
Humans
Molecular Chaperones
Neoplasm Proteins
/ genetics
Neoplasms
/ genetics
Nuclear Proteins
/ chemistry
Phosphorylation
Protein Binding
Protein Interaction Mapping
Protein Processing, Post-Translational
Signal Transduction
Sumoylation
Transcription, Genetic
Ubiquitination
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
05 09 2019
05 09 2019
Historique:
accepted:
12
07
2019
revised:
05
07
2019
received:
18
03
2019
pubmed:
28
7
2019
medline:
4
12
2019
entrez:
28
7
2019
Statut:
ppublish
Résumé
DAXX displays complex biological functions. Remarkably, DAXX overexpression is a common feature in diverse cancers, which correlates with tumorigenesis, disease progression and treatment resistance. Structurally, DAXX is modular with an N-terminal helical bundle, a docking site for many DAXX interactors (e.g. p53 and ATRX). DAXX's central region folds with the H3.3/H4 dimer, providing a H3.3-specific chaperoning function. DAXX has two functionally critical SUMO-interacting motifs. These modules are connected by disordered regions. DAXX's structural features provide a framework for deciphering how DAXX mechanistically imparts its functions and how its activity is regulated. DAXX modulates transcription through binding to transcription factors, epigenetic modifiers, and chromatin remodelers. DAXX's localization in the PML nuclear bodies also plays roles in transcriptional regulation. DAXX-regulated genes are likely important effectors of its biological functions. Deposition of H3.3 and its interactions with epigenetic modifiers are likely key events for DAXX to regulate transcription, DNA repair, and viral infection. Interactions between DAXX and its partners directly impact apoptosis and cell signaling. DAXX's activity is regulated by posttranslational modifications and ubiquitin-dependent degradation. Notably, the tumor suppressor SPOP promotes DAXX degradation in phase-separated droplets. We summarize here our current understanding of DAXX's complex functions with a focus on how it promotes oncogenesis.
Identifiants
pubmed: 31350900
pii: 5539884
doi: 10.1093/nar/gkz634
pmc: PMC6735914
doi:
Substances chimiques
Adaptor Proteins, Signal Transducing
0
Chromatin
0
Co-Repressor Proteins
0
DAXX protein, human
0
Molecular Chaperones
0
Neoplasm Proteins
0
Nuclear Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
7734-7752Informations de copyright
© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.
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