Literature DB >> 21141906

Nuclear receptor coactivators: structural and functional biochemistry.

Yaroslava A Bulynko1, Bert W O'Malley.   

Abstract

Transcription of eukaryotic cell is a multistep process tightly controlled by concerted action of macromolecules. Nuclear receptors are ligand-activated sequence-specific transcription factors that bind DNA and activate (or repress) transcription of specific sets of nuclear target genes. Successful activation of transcription by nuclear receptors and most other transcription factors requires "coregulators" of transcription. Coregulators make up a diverse family of proteins that physically interact with and modulate the activity of transcription factors and other components of the gene expression machinery via multiple biochemical mechanisms. The coregulators include coactivators that accomplish reactions required for activation of transcription and corepressors that suppress transcription. This review summarizes our current knowledge of nuclear receptor coactivators with an emphasis on their biochemical mechanisms of action and means of regulation.

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Year:  2010        PMID: 21141906      PMCID: PMC3647688          DOI: 10.1021/bi101762x

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  184 in total

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Journal:  Nucleic Acids Res       Date:  2003-01-01       Impact factor: 16.971

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4.  Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins.

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Journal:  Mol Cell Biol       Date:  2003-01       Impact factor: 4.272

5.  Control of Smad7 stability by competition between acetylation and ubiquitination.

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6.  A role for TGF-beta in estrogen and retinoid mediated regulation of the nuclear receptor coactivator AIB1 in MCF-7 breast cancer cells.

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Journal:  Oncogene       Date:  2002-10-17       Impact factor: 9.867

7.  Coordinate regulation of transcription and splicing by steroid receptor coregulators.

Authors:  Didier Auboeuf; Arnd Hönig; Susan M Berget; Bert W O'Malley
Journal:  Science       Date:  2002-10-11       Impact factor: 47.728

8.  Receptor-interacting protein 140 binds c-Jun and inhibits estradiol-induced activator protein-1 activity by reversing glucocorticoid receptor-interacting protein 1 effect.

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Journal:  Mol Endocrinol       Date:  2003-02

9.  Splicing and transcription-associated proteins PSF and p54nrb/nonO bind to the RNA polymerase II CTD.

Authors:  Andrew Emili; Michael Shales; Susan McCracken; Weijun Xie; Philip W Tucker; Ryuji Kobayashi; Benjamin J Blencowe; C James Ingles
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10.  The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1.

Authors:  Noora Kotaja; Ulla Karvonen; Olli A Jänne; Jorma J Palvimo
Journal:  J Biol Chem       Date:  2002-06-11       Impact factor: 5.157

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  40 in total

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2.  Inhibition of BET proteins impairs estrogen-mediated growth and transcription in breast cancers by pausing RNA polymerase advancement.

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6.  Research resource: identification of novel coregulators specific for thyroid hormone receptor-β2.

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Review 7.  The role of genetics in estrogen responses: a critical piece of an intricate puzzle.

Authors:  Emma H Wall; Sylvia C Hewitt; Laure K Case; Chin-Yo Lin; Kenneth S Korach; Cory Teuscher
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Review 8.  Metabolic choreography of gene expression: nutrient transactions with the epigenome.

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Review 9.  Phosphorylation: a fundamental regulator of steroid receptor action.

Authors:  Lindsey S Treviño; Nancy L Weigel
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10.  Endocrine disrupting chemical, bisphenol-A, induces breast cancer associated gene HOXB9 expression in vitro and in vivo.

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