Abstract
As a highly conserved nuclear protein, death domain-associated protein(Daxx) plays an important role in transcriptional control, carcinogenesis, resistance to virus infection, and so on. Daxx can be localized in promyleocytic leukaemia protein oncogenic domains, nucleoplasm, nucleolus, cytoplasm, and heterochromatin. The subcellular localization of Daxx can be changed by modification or interacting with other proteins. Under cellular stress, Daxx can interact with many kinds of molecules, and thus affect its downstream signaling pathway. The purpose of this review was to discuss Daxx's subcellular localization in different conditions and its translocation between subcellular compartments.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adaptor Proteins, Signal Transducing / metabolism*
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Adaptor Proteins, Signal Transducing / physiology
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Animals
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Carrier Proteins / metabolism
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Carrier Proteins / physiology
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Cell Line, Tumor
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Cell Nucleolus / metabolism
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Cell Nucleus / metabolism
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Co-Repressor Proteins
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Cytoplasm / metabolism
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Heterochromatin / metabolism
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Humans
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Intracellular Signaling Peptides and Proteins / metabolism
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Intracellular Signaling Peptides and Proteins / physiology
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Molecular Chaperones
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Nuclear Proteins / metabolism*
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Nuclear Proteins / physiology
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Oxidative Stress*
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Promyelocytic Leukemia Protein
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Protein Structure, Tertiary
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Protein Transport
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Signal Transduction*
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Transcription Factors / metabolism
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Tumor Suppressor Proteins / metabolism
Substances
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Adaptor Proteins, Signal Transducing
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Carrier Proteins
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Co-Repressor Proteins
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DAXX protein, human
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Daxx protein, mouse
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Heterochromatin
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Intracellular Signaling Peptides and Proteins
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Molecular Chaperones
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Nuclear Proteins
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Promyelocytic Leukemia Protein
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Transcription Factors
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Tumor Suppressor Proteins
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PML protein, human