Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex Journal Article


Authors: Rachez, C.; Lemon, B. D.; Suldan, Z.; Bromleigh, V.; Gamble, M.; Näär, A. M.; Erdjument-Bromage, H.; Tempst, P.; Freedman, L. P.
Article Title: Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex
Abstract: Nuclear receptors modulate the transcription of genes in direct response to small lipophilic ligands. Binding to ligands induces conformational changes in the nuclear receptors that enable the receptors to interact with several types of cofactor that are critical for transcription activation (transactivation). We previously described a distinct set of ligand-dependent proteins called DRIPs, which interact with the vitamin D receptor (VDR); together, these proteins constitute a new cofactor complex. DRIPs bind to several nuclear receptors and mediate ligand-dependent enhancement of transcription by VDR and the thyroid-hormone receptor in cell-free transcription assays. Here we report the identities of thirteen DRIPs that constitute this complex, and show that the complex has a central function in hormone-dependent transactivation by VDR on chromatin templates. The DRIPs are almost indistinguishable from components of another new cofactor complex called ARC, which is recruited by other types of transcription activators to mediate transactivation on chromatin-assembled templates. Several DRIP/ARC subunits are also components of other potentially related cofactors, such as CRSP, NAT, SMCC and the mouse Mediator, indicating that unique classes of activators may share common sets or subsets of cofactors. The role of nuclear-receptor ligands may in part, be to recruit such a cofactor complex to the receptor and, in doing so, to enhance transcription of target genes.
Keywords: sequence analysis; animals; mice; complex formation; drosophila; genetic transcription; hela cells; transcription factors; nuclear proteins; cloning, molecular; regulatory mechanism; transcription regulation; amino acid sequence; molecular sequence data; sequence homology, amino acid; chromatin; nucleotide sequence; carrier proteins; ligand; transactivation; ligands; trans-activators; cell nucleus receptor; vitamin d receptor; ligand binding; receptor binding; complementary dna; macromolecular substances; trans-activation (genetics); receptors, calcitriol; humans; human; priority journal; article
Journal Title: Nature
Volume: 398
Issue: 6730
ISSN: 0028-0836
Publisher: Nature Publishing Group  
Date Published: 1999-04-29
Start Page: 824
End Page: 828
Language: English
DOI: 10.1038/19783
PUBMED: 10235266
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 16 August 2016 -- Source: Scopus
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  1. Matthew J Gamble
    7 Gamble
  2. Christophe Rachez
    17 Rachez
  3. Paul J Tempst
    324 Tempst