Androgen receptor coregulator ARA267-alpha interacts with death receptor-6 revealed by the yeast two-hybrid.

Institute of Urology, First Hospital of Peking University, Beijing 100034, China.
Science in China Series C Life Sciences (Impact Factor: 1.61). 11/2004; 47(5):442-8.
Source: PubMed

ABSTRACT ARA267-alpha is a newly identified androgen receptor coactivator. In order to further elucidate its precise role in cells, using the ARA267-alpha fragment containing four PHD and one SET conserved domains as bait we revealed an ARA267-alpha-PHD-SET-interacting protein, death receptor-6 (DR6), in the yeast two-hybrid screening. DR6 is the member of TNF receptor family and has a death domain in its intracellular cytoplasmic portion (DR6cp) to mediate the cell apoptosis. The interaction between ARA267-alpha-PHD-SET and DR6cp was confirmed in vitro and in vivo. Our finding implied that androgen signaling pathway might cross talk with apoptosis signaling pathway through the interaction between ARA267-alpha and DR6.

  • [Show abstract] [Hide abstract]
    ABSTRACT: The recurrent translocation t(5;11)(q35;p15.5) associated with a 5q deletion, del(5q), has been reported in childhood acute myeloid leukemia (AML). We report the cloning of the translocation breakpoints in de novo childhood AML harboring a cryptic t(5;11)(q35;p15.5). Fluorescence in situ hybridization (FISH) analysis demonstrated that the nucleoporin gene (NUP98) at 11p15.5 was disrupted by this translocation. By using 3'--rapid amplification of complementary DNA ends (3'-RACE) polymerase chain reaction, we identified a chimeric messenger RNA that results in the in-frame fusion of NUP98 to a novel gene, NSD1. The NSD1 gene has 2596 amino acid residues and a 85% homology to the murine Nsd1 with the domain structure being conserved. The NSD1 gene was localized to 5q35 by FISH and is widely expressed. The reciprocal transcript, NSD1-NUP98, was also detected by reverse transcriptase--polymerase chain reaction. This is the first report in which the novel gene NSD1 has been implicated in human malignancy. (Blood. 2001;98:1264-1267)
    Blood 09/2001; 98(4):1264-7. DOI:10.1182/blood.V98.4.1264 · 10.43 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Enzymes that covalently modify histones control many cellular processes by affecting gene expression. A new class of these enzymes is the histone lysine methyltransferase family, whose catalytic activity lies within a conserved domain, the SET domain. This article surveys the evidence for a connection between SET-domain-containing proteins and cancer. It proposes that deregulation of SET-domain function has an important role in carcinogenesis.
    Trends in Biochemical Sciences 09/2002; 27(8):396-402. DOI:10.1016/S0968-0004(02)02141-2 · 13.52 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Complementary DNAs (cDNAs) encoding androgen receptors were obtained from human testis and rat ventral prostate cDNA libraries. The amino acid sequence deduced from the nucleotide sequences of the cDNAs indicated the presence of a cysteine-rich DNA-binding domain that is highly conserved in all steroid receptors. The human cDNA was transcribed and the RNA product was translated in cell-free systems to yield a 76-kilodalton protein. The protein was immunoprecipitable by human autoimmune antibodies to the androgen receptor. The protein bound androgens specifically and with high affinity.
    Science 05/1988; 240(4850):324-6. DOI:10.1126/science.3353726 · 31.48 Impact Factor
Show more