Co-activators and co-repressors in the integration of transcriptional responses

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Abstract

The nuclear hormone receptors are DNA binding transcription factors that are regulated by binding of ligands, switching them from an inactive or repressive state to gene-activating functions. Recent evidence supports the hypothesis that many nuclear receptors switch, in a ligand-dependent manner, between binding of a multicomponent co-repressor complex containing histone deacetyltransferase activity, and binding of a co-activator complex containing factors with histone acetyltransferase activity that are further regulated by diverse signal transduction pathways. The identification of these limiting co-repressor and co-activator complexes and their specific interaction motifs, in concert with solution of the structures of the receptor ligand-binding domain in apo (empty) and ligand bound forms, indicates a common molecular mechanism by which these factors activate and repress gene transcription.

References (85)

  • J Wong et al.

    Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: hormone-regulated chromatin disruption is not sufficient for transcriptional activation

    EMBO J

    (1997)
  • WL Kraus et al.

    p300 and estrogen receptors cooperatively activate transcription via differential enhancement of initiation and reinitiation

    Genes Dev

    (1998)
  • PS Danielian et al.

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

    EMBO J

    (1992)
  • D Barettino et al.

    Characterization of the ligand-dependent transactivation by steroid hormone receptors

    EMBO J

    (1994)
  • B Durand et al.

    Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity

    EMBO J

    (1994)
  • W Bourguet et al.

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

    Nature

    (1995)
  • J-P Renaud et al.

    Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid

    Nature

    (1995)
  • RL Wagner et al.

    A structural role for hormone in the thyroid hormone receptor

    Nature

    (1995)
  • AM Brzozowski et al.

    Molecular basis of agonism and antagonism in the oestrogen receptor

    Nature

    (1997)
  • CK Glass et al.

    Nuclear receptor co-activators

    Curr Opin Cell Biol

    (1997)
  • V Cavailles et al.

    Interaction of proteins with transcriptionally active astrogen receptors

    Proc Natl Acad Sci USA

    (1994)
  • R Kurokawa et al.

    Polarity-specific activities of retinoic acid receptors determined by a co-repressor

    Nature

    (1995)
  • SA Onate et al.

    Sequence and characterization of a co-activator for the steroid hormone receptor superfamily

    Science

    (1995)
  • Y Kamei et al.

    A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors

    Cell

    (1996)
  • H Hong et al.

    GRIP1, a novel mouse protein that serves as a transcriptional co-activator in yeast for the hormone binding domains of steroid receptors

    Proc Natl Acad Sci USA

    (1996)
  • J Torchia et al.

    The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function

    Nature

    (1997)
  • SL Anzick et al.

    AIB1, a steroid receptor co-activator amplified in breast and ovarian cancer

    Nature

    (1997)
  • H Chen et al.

    Nuclear receptor co-activator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with p/CAF and CBP/p300

    Cell

    (1997)
  • H Li et al.

    AC3, a steroid/nuclear receptor-associated co-activator that is related to SRC-1 and TIF2

    Proc Natl Acad Sci USA

    (1997)
  • A Takeshita et al.

    TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor co-activator-1

    J Biol Chem

    (1997)
  • E Kalkhoven et al.

    Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor

    EMBO J

    (1998)
  • R Kurokawa et al.

    Differential use of CREB binding protein-co-activator complexes

    Science

    (1998)
  • N Shikama et al.

    The p300/CBP family: integrating signals with transcription factors and chromatin

    Trends Cell Biol

    (1997)
  • DM Heery et al.

    A signature motif in co-activators mediates binding to nuclear receptors

    Nature

    (1997)
  • XF Ding et al.

    Nuclear receptor binding sites of co-activator glucocorticoid receptor interacting protein GRIP-1 and steroid receptor co-activator (SRC-1)

    Mol Endocrinol

    (1998)
  • B Le Douarin et al.

    A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors

    EMBO J

    (1996)
  • F Petrij et al.

    Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP

    Nature

    (1995)
  • H Akimaru et al.

    Drosophila CBP is a co-activator of cubitus interruptus in hedgehog signaling

    Nature

    (1997)
  • Y Tanaka et al.

    Abnormal skeletal patterning in embryos lacking a single CBP allele: a partial similarity with Rubinstein-Taybi syndrome

    Proc Natl Acad Sci USA

    (1997)
  • R Eckner et al.

    Molecular cloning and functional analysis of the adenovirus E1A-associated 300 kD protein (p300) reveals a protein with properties of a transcriptional adaptor

    Genes Dev

    (1994)
  • T Nakajima et al.

    The signal-dependent co-activator CBP is a nuclear target for pp90RSK

    Cell

    (1996)
  • T Nakajima et al.

    RNA helicase A mediates association of CBP with the RNA polymerase II

    Cell

    (1997)

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    Present Address: Departments of Oncology, Pharmacology and Toxicology, University of Western Ontario, London Regional Cancer Centre, London Ontario, Canada N6A 4L6

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