Elsevier

Steroids

Volume 61, Issue 4, April 1996, Pages 240-251
Steroids

Paper
Transcriptional regulation by steroid hormones

https://doi.org/10.1016/0039-128X(96)00030-XGet rights and content

Abstract

Steroid hormones influence the transcription of a large number of genes by virtue of their interaction with intracellular receptors, which are modular proteins composed of a ligand binding domain, a DNA binding domain, and several transactivation functions distributed along the molecule. The DNA binding domain is organized around two zinc ions and allows the receptors to bind as homodimers to palindromic DNA sequences, the hormone responsive elements (HRE), in such a way that each homodimer contacts one half of the palindrome. Since the two halves are separated by three base pairs, the two homodimers contact the same face of the double helix. Before hormone binding, the receptors are part of a complex with multiple chaperones which maintain the receptor in its steroid binding conformation. Following hormone binding, the complex dissociates and the receptors bind to HREs in chromatin. Regulation of gene expression by hormones involves an interaction of the DNA-bound receptors with other sequence-specific transcription factors and with the general transcription factors, which is partly mediated by co-activators and co-repressors. The specific array of cis regulatory elements in a particular promoter/enhancer region, as well as the orgainzation of the DNA sequences in nucleosomes, specifies the network of receptor interactions. Depending on the nature of these interactions, the final outcome can be induction or repression of transcription. The various levels at which these interactions are modulated are discussed using as an example the promoter of the Mouse Mammary Tumor Virus and its organization in chromatin.

References (176)

  • Z Arany et al.

    EIA-associated p300 and CREB-associated CBP belong to a conserved family of coactivators

    Cell

    (1994)
  • U Brüggemeier et al.

    Ubiquitous transcription factor OTF-1 mediates induction of the mouse mammary tumour virus promoter through synergistic interaction with hormone receptors

    Cell

    (1991)
  • G Rigaud et al.

    In vivo footprinting of rat TAT gene: Dynamic interplay between the glucocorticoid receptor and a liver-specific factor

    Cell

    (1991)
  • J.N. Miner et al.

    Regulatory Crosstalk at Composite Response Elements

    Trends Biochem Sci

    (1991)
  • H Zhang et al.

    A single upstream glucocorticoid response element juxtaposed to an AP1/ATF/CRE-like site renders the chicken glutamine synthetase gene hormonally inducible in transfected retina

    J Biol Chem

    (1991)
  • R Schüle et al.

    Functional antagonism between oncoprotein c-Jun and the glucocorticoid receptor

    Cell

    (1990)
  • C Jonat et al.

    Antitumor promotion and antiinflamation: Downregulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone

    Cell

    (1990)
  • H-F Yang-Yen et al.

    Transcriptional interference between c-Jun and the glucocorticoid receptor: Mutual inhibition of DNA binding due to direct protein-protein interaction

    Cell

    (1990)
  • N Mukaida et al.

    Novel mechanism of glucocorticoid-mediated gene repression: nuclear factor-kB is target for glucocorticoid-mediated interleukin 8 gene repression

    J Biol Chem

    (1994)
  • S Dedhar

    Novel functions for calreticulin: interaction with integrins and modulation of gene expression?

    Trends Biochem Sci

    (1994)
  • B.W. O'Malley et al.

    An alternative ligand-independent pathway for activation of steroid receptors

  • M.L. Moyer et al.

    Modulation of cell signaling pathways can enhance or impair glucocorticoid-induced gene expression without altering the state of receptor phosphorylation

    J Biol Chem

    (1993)
  • S Ruppert et al.

    Two genetically defined trans-acting loci coordinately regulate overlapping sets of liver-specific genes

    Cell

    (1990)
  • P.S. Danielian et al.

    Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors

    EMBO J

    (1992)
  • W Bourguet et al.

    Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha

    Nature

    (1995)
  • K Dahlman-Wright et al.

    Structural characterization of a minimal functional transactivation domain from the human glucocorticoid receptor

  • E Vegeto et al.

    Human progesterone receptor—A form is a cell-specific and promoter-specific repressor of human progesterone receptor-B function

    Mol Endocrinol

    (1993)
  • S.M. Hollenberg et al.

    Primary structure and expression of a functional human glucocorticoid receptor cDNA

    Nature

    (1985)
  • C.M. Bamberger et al.

    Glucocorticoid receptor β, a potential endogenous inhibitor of glucocorticoid action in humans

    J Clin Invest

    (1995)
  • P Rehberger et al.

    Heterotetrameric structure of the human progesterone receptor

  • B Segnitz et al.

    Subunit structure of the nonactivated human estrogen receptor

  • J.M. Renoir et al.

    Cyclosporin A potentiates the dexamethasone-induced mouse mammary tumor virus-chloramphenicol acetyltransferase activity in LMCAT cells: a possible role for different heat shock protein-binding immunophilins in glucocorticosteroid receptor-mediated gene expression

  • D Picard et al.

    Reduced levels of hsp90 compromise steroid receptor action in vivo

    Nature

    (1990)
  • Y Kimura et al.

    Role of protein chaperone YDJ1 in establishing hsp90-mediated signal transduction pathways

    Science

    (1995)
  • Y Sadovsky et al.

    Transcriptional activators differ in their responses to overexpression of TATA-box-binding protein

    Mol Cell Biol

    (1995)
  • C Schwerk et al.

    Identification of a transactivation function in the progesterone receptor that interacts with the TAFII10 subunit of the TFIID complex

    J Biol Chem

    (1995)
  • K Ferreri et al.

    The cAMP-regulated transcription factor CREB interacts with a component of the TFIID complex

  • I Haviv et al.

    The X protein of hepatitis B virus coactivates potent activation domains

    Mol Cell Biol

    (1995)
  • J.C. Chrivia et al.

    Phosphorylated CREB binds specifically to the nuclear protein CBP

    Nature

    (1993)
  • R.P.S. Kwok et al.

    Nuclear protein CBP is a coactivator for the transcription factor CREB

    Nature

    (1994)
  • Z Arany et al.

    A family of transcriptional adaptor proteins targeted by the E1A oncoprotein

    Nature

    (1995)
  • L Yu et al.

    Molecular cloning and characterization of a cellular protein that interacts with the human immunodeficiency virus type 1 Tat transactivator and encodes a strong transcriptional activation domain

    J Virol

    (1995)
  • S Halachmi et al.

    Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription

    Science

    (1994)
  • V Cavaillès et al.

    Interaction of proteins with transcriptionally active estrogen receptors

  • V Cavailles et al.

    Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor

    EMBO J

    (1995)
  • M Eggert et al.

    A fraction enriched in a novel glucocorticoid receptor interacting protein stimulates receptor dependent transcription in vitro

    J Biol Chem

    (1995)
  • C Baniahmad et al.

    Enhancement of human estrogen receptor activity by SPT6: A potential coactivator

    Mol Endocrinol

    (1995)
  • M Zeiner et al.

    A novel protein that interacts with members of the nuclear receptor family

  • B LeDouarin et al.

    The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18

    EMBO J

    (1995)
  • A Guiochon-Mantel et al.

    Effect of PML and PML-RAR on the transcription properties and subcellular distribution of steroid hormone receptors

    Mol Endocrinol

    (1995)
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    Present address is Departamento de Genética, Facultad de Biología, Apartado 1095, Universidad de Sevilla, Reina Mercedes, 6, E-41080 Sevilla, Spain.

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