Physical and functional interactions between Daxx and TSG101 (Q24318359)

1

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Kenji Sugiyama

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Tetsuya Yamamoto

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Kenji Oritani

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Kazuya Shimoda

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Tadashi Matsuda

Biochemical and Biophysical Research Communications

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language of work or name

English

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publication date

9 April 2004

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published in

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volume

316

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issue

3

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page(s)

827-33

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cites work

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A putative tumor suppressor, TSG101, acts as a transcriptional suppressor through its coiled-coil domain

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Interaction of Daxx, a Fas binding protein, with sentrin and Ubc9

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Daxx enhances Fas-mediated apoptosis in a murine pro-B cell line, BAF3.

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Daxx, a Novel Fas-Binding Protein That Activates JNK and Apoptosis

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Tsg101: a novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells

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Apoptosis by death factor

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Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I.

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TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation

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DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci

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TSG101 may be the prototype of a class of dominant negative ubiquitin regulators

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EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes

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Regulation of Pax3 transcriptional activity by SUMO-1-modified PML

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Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate

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Dissecting Fas signaling with an altered-specificity death-domain mutant: requirement of FADD binding for apoptosis but not Jun N-terminal kinase activation

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A TSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control

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p53 accumulation, defective cell proliferation, and early embryonic lethality in mice lacking tsg101.

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TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes

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Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm

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The interaction of Pax5 (BSAP) with Daxx can result in transcriptional activation in B cells

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Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration

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Promyelocytic leukemia protein (PML) functions as a glucocorticoid receptor co-activator by sequestering Daxx to the PML oncogenic domains (PODs) to enhance its transactivation potential

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PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1

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The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx

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Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins

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Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs).

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Loss of Daxx, a promiscuously interacting protein, results in extensive apoptosis in early mouse development

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Sequestration and inhibition of Daxx-mediated transcriptional repression by PML

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Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity

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RNAi reveals anti-apoptotic and transcriptionally repressive activities of DAXX

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Physical and functional interactions between Daxx and DNA methyltransferase 1-associated protein, DMAP1

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