10 research outputs found

    Identified proteins

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    Table S1A: Proteins identified in partially purified MCF-7 (CTRL) cell nuclear extracts. Table S1B: Proteins identified in partially purified CTAP-ER_ expressing MCF-7 (Sample) cell nuclear extracts. Table S1C: Proteins specifically identified in partially purified CTAP-ER_ (Sample) vs MCF7 (CTRL) nuclear extracts

    Comparison of ER beta interactors after either RNA or AGO2 depletion

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    Diffentially expressed proteins upon RNAse treatment and AGO2 silencing. In italic are displayed those proteins that do not fit the statistical significance parameters

    Molecular Mechanisms of Selective Estrogen Receptor Modulator Activity in Human Breast Cancer Cells: Identification of Novel Nuclear Cofactors of Antiestrogenā€“ERĪ± Complexes by Interaction Proteomics

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    Estrogen receptor alpha (ERĪ±) is a ligand-activated transcription factor that controls key cellular pathways <i>via</i> proteinā€“protein interactions involving multiple components of transcriptional coregulator and signal transduction complexes. Natural and synthetic ERĪ± ligands are classified as agonists (17Ī²-estradiol/E<sub>2</sub>), selective estrogen receptor modulators (SERMs: Tamoxifen/Tam and Raloxifene/Ral), and pure antagonists (ICI 182,780-Fulvestrant/ICI), according to the response they elicit in hormone-responsive cells. Crystallographic analyses reveal ligand-dependent ERĪ± conformations, characterized by specific surface docking sites for functional proteinā€“protein interactions, whose identification is needed to understand antiestrogen effects on estrogen target tissues, in particular breast cancer (BC). Tandem affinity purification (TAP) coupled to mass spectrometry was applied here to map nuclear ERĪ± interactomes dependent upon different classes of ligands in hormone-responsive BC cells. Comparative analyses of agonist (E<sub>2</sub>)- vs antagonist (Tam, Ral or ICI)-bound ERĪ± interacting proteins reveal significant differences among ER ligands that relate with their biological activity, identifying novel functional partners of antiestrogenā€“ERĪ± complexes in human BC cell nuclei. In particular, the E<sub>2</sub>-dependent nuclear ERĪ± interactome is different and more complex than those elicited by Tam, Ral, or ICI, which, in turn, are significantly divergent from each other, a result that provides clues to explain the pharmacological specificities of these compounds

    Molecular Mechanisms of Selective Estrogen Receptor Modulator Activity in Human Breast Cancer Cells: Identification of Novel Nuclear Cofactors of Antiestrogenā€“ERĪ± Complexes by Interaction Proteomics

    No full text
    Estrogen receptor alpha (ERĪ±) is a ligand-activated transcription factor that controls key cellular pathways <i>via</i> proteinā€“protein interactions involving multiple components of transcriptional coregulator and signal transduction complexes. Natural and synthetic ERĪ± ligands are classified as agonists (17Ī²-estradiol/E<sub>2</sub>), selective estrogen receptor modulators (SERMs: Tamoxifen/Tam and Raloxifene/Ral), and pure antagonists (ICI 182,780-Fulvestrant/ICI), according to the response they elicit in hormone-responsive cells. Crystallographic analyses reveal ligand-dependent ERĪ± conformations, characterized by specific surface docking sites for functional proteinā€“protein interactions, whose identification is needed to understand antiestrogen effects on estrogen target tissues, in particular breast cancer (BC). Tandem affinity purification (TAP) coupled to mass spectrometry was applied here to map nuclear ERĪ± interactomes dependent upon different classes of ligands in hormone-responsive BC cells. Comparative analyses of agonist (E<sub>2</sub>)- vs antagonist (Tam, Ral or ICI)-bound ERĪ± interacting proteins reveal significant differences among ER ligands that relate with their biological activity, identifying novel functional partners of antiestrogenā€“ERĪ± complexes in human BC cell nuclei. In particular, the E<sub>2</sub>-dependent nuclear ERĪ± interactome is different and more complex than those elicited by Tam, Ral, or ICI, which, in turn, are significantly divergent from each other, a result that provides clues to explain the pharmacological specificities of these compounds

    Additional file 12: Table S9. of The nuclear receptor ERĪ² engages AGO2 in regulation of gene transcription, RNA splicing and RISC loading

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    Genes whose transcription rate is modulated by ERĪ² and AGO2. Table S9a. Genes showing transcriptional regulation by ERĪ² (Ct-ERĪ² vs wild type). Table S9b. Genes responding to AGO2 silencing in ERĪ²ā€‰+ā€‰cells (shAGO2 vs Ct-ERĪ²). Table S9c. Genes showing transcriptional regulation by both ERĪ² (Ct-ERĪ² vs wild type) and AGO2 (shAGO2 vs Ct-ERĪ²). Table S9d. Genes differentially expressed in Ct-ERĪ² vs wild-type cells harboring both ERĪ² and AGO2 binding sites and showing an inversion of the ERĪ²-induced transcriptional trend after AGO2 silencing. (XLSX 1259 kb
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