Cited by 660Estrogen and related hormone effectsNuclear Receptors and SignalingGenomics and Chromatin Dynamics

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Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes.

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Lavinsky, Robert M., Jepsen, Kristen, Heinzel, Thorsten, Torchia, Joseph, Mullen, Tina-Marie, Schiff, Rachel, Del-Rio, Alfonso Leon, Ricote, Mercedes, Ngo, Sally, Gemsch, Joslin, Hilsenbeck, Susan G., Osborne, C. Kent, Glass, Christopher K., Rosenfeld, Michael G., Rose, David W.·1998·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.95.6.2920PMC PMC19670

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Abstract

Several lines of evidence indicate that the nuclear receptor corepressor (N-CoR) complex imposes ligand dependence on transcriptional activation by the retinoic acid receptor and mediates the inhibitory effects of estrogen receptor antagonists, such as tamoxifen, suppressing a constitutive N-terminal, Creb-binding protein/coactivator complex-dependent activation domain. Functional interactions between specific receptors and N-CoR or SMRT corepressor complexes are regulated, positively or negatively, by diverse signal transduction pathways. Decreased levels of N-CoR correlate with the acquisition of tamoxifen resistance in a mouse model system for human breast cancer. Our data suggest that N-CoR- and SMRT-containing complexes act as rate-limiting components in the actions of specific nuclear receptors, and that their actions are regulated by multiple signal transduction pathways.

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“Accumulating evidence suggests that coactivators and corepressors are critical for controlling the expression and activity of the nuclear receptors in a given cell or tissue (24, 32).”
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Breast Cancer Chemoprevention Phase I Evaluation of Biomarker Modulation by Arzoxifene, a Third Generation Selective Estrogen Receptor Modulator
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Estrogen Sensitivity of Target Genes and Expression of Nuclear Receptor Co-Regulators in Rat Prostate after Pre- and Postnatal Exposure to the Ultraviolet Filter 4-Methylbenzylidene Camphor
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“Such a preference has been reported by some in a variety of cell-free and cellular systems (25, 40, 47, 48), but not confirmed by others (26, 49).”
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Dissociation of Steroid Receptor Coactivator 1 and Nuclear Receptor Corepressor Recruitment to the Human Glucocorticoid Receptor by Modification of the Ligand-Receptor Interface: The Role of Tyrosine 735
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“Other investigators have also described discrepant results when they compared mammalian two-hybrid against GST pull-down assays when examining steroid receptor interactions with NCoR proteins (16); as a result, additional controls on steroid receptor interactions with corepressors in living cells have been proposed (1…”
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Binding of the N-terminal Region of Coactivator TIF2 to the Intrinsically Disordered AF1 Domain of the Glucocorticoid Receptor Is Accompanied by Conformational Reorganizations
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“The majority of reported ER co-repressors, such as nuclear receptor corepressor (NCoR) [29], silencing mediator for retinoid and thyroid hormone receptors (SMRT) [30], receptorinteracting protein (RIP)140 [31] and breast cancer susceptibility gene (BRCA)1 [32, 33], bind to the AF2 domain of ER .”
Background
Role of estrogen receptor α transcriptional coregulators in tamoxifen resistance in breast cancer
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An NRSF/REST‐like repressor downstream of Ebi/SMRTER/Su(H) regulates eye development in Drosophila
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“Extracellular signaling may modulate this competition, as diverse signaling pathways modulate the functions of N-CoR/SMRT (Lavinsky et al, 1998).”
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Glucocorticoid receptor ligand binding domain is sufficient for the modulation of glucocorticoid induction properties by homologous receptors, coactivator transcription intermediary factor 2, and Ubc9.
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Background
Deregulation of cofactor of BRCA1 expression in breast cancer cells
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Background
3-phosphoinositide-dependent protein kinase-1 activates the peroxisome proliferator-activated receptor-gamma and promotes adipocyte differentiation.
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“In the presence of 4-OH-tamoxifen (OHTam), ER has been shown to interact with the N-CoR corepressor and this binding is decreased by intracellular pathways which switch OHTam from an antagonist to an agonist function (in response for instance to forskolin or growth factors) (Lavinsky et al. 1998).”
Background
New antiprogestins with partial agonist activity: potential selective progesterone receptor modulators (SPRMs) and probes for receptor- and coregulator-induced changes in progesterone receptor induction properties.
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Estrogen Receptors Recruit SMRT and N-CoR Corepressors through Newly Recognized Contacts between the Corepressor N Terminus and the Receptor DNA Binding Domain
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“The pSG5-hER and pSG5-Myc-SMRT (1-2470) clones”
BackgroundMethodInfluential
Identification of Tamoxifen-Induced Coregulator Interaction Surfaces within the Ligand-Binding Domain of Estrogen Receptors
Heldring, N., Nilsson, M., Buehrer, B., Treuter, E., & Gustafsson, J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3445-3459.2004 · Cited by 50
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Acyl-CoA Esters Antagonize the Effects of Ligands on Peroxisome Proliferator-activated Receptor α Conformation, DNA Binding, and Interaction with Co-factors*
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Resistance to endocrine therapy in breast cancer
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Background
Selection of Estrogen Receptor β- and Thyroid Hormone Receptor β-Specific Coactivator-Mimetic Peptides Using Recombinant Peptide Libraries
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Glucocorticoid-independent Repression of Tumor Necrosis Factor (TNF) α-stimulated Interleukin (IL)-6 Expression by the Glucocorticoid Receptor
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Estrogen Receptor Regulates E2F1 Expression to Mediate Tamoxifen Resistance
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“However, the role of ERα in the development of tamoxifen-resistant breast cancer remains unclear (1-5).”
Background
Differences in the abilities of estrogen receptors to integrate activation functions are critical for subtype-specific transcriptional responses.
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“How do antagonists mediate ER subtype-specific responses as partial agonists? 4-OHT and ICI as antagonists exert their effects by impeding the interaction of both ER and ER with AF-2-dependent cofactors by inducing distinct conformation in the ligand-binding domain and recruitment of corepressor proteins (26, 86).”
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Neuroactive steroids: an update of their roles in central and peripheral nervous system.
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“NCoR and SMRT have been shown to interact with nuclear receptors other than the thyroid and retinoid hormone receptor; they act as corepressor molecules for androgen receptors (Yoon and Wong, 2006), estrogen receptors (Lavinsky et al., 1998), and progesterone receptors (Liu et al.”
Comparative gene expression profiling reveals partially overlapping but distinct genomic actions of different antiestrogens in human breast cancer cells
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Background
The Flt3 internal tandem duplication mutant inhibits the function of transcriptional repressors by blocking interactions with SMRT.
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“A full-length GFP-SMRT (1-1495) fusion protein, upon transient expression in 293T cells, was located almost exclusively in the nucleus of unstimulated transfected cells (Figure 4A left).”
BackgroundMethodInfluential
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“17) were mutated or downregulated (1, 17).”

Authors: Lavinsky, R. M., Jepsen, K., Heinzel, T., Torchia, J., Mullen, T.-M., Schiff, R., Del-Rio, A. L., Ricote, M., Ngo, S., Gemsch, J., Hilsenbeck, S. G., Osborne, C. K., Glass, C. K., Rosenfeld, M. G., & Rose, D. W.
Affiliations: Howard Hughes Medical Institute (US)
Howard Hughes Medical Institute, Cellular and Molecular Medicine, Whittier Diabetes Program, and UCSD Graduate Program in Biology, Department and School of Medicine, University of California at San Diego, La Jolla, CA 92093-0648; and Department of Medicine, Division of Medical Oncology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78284-7884
Corresponding author: Rose, David W.
ORCID: Jepsen, Kristen
Heinzel, Thorsten
Torchia, Joseph
Mullen, Tina-Marie
Schiff, Rachel
Ricote, Mercedes
Hilsenbeck, Susan G.
Osborne, C. Kent
Glass, Christopher K.
Rosenfeld, Michael G.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1998-03-17
Volume: 95
Issue: 6
Pages: 2920-2925
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.95.6.2920
PMC: PMC19670
OpenAlex: W2128003724
Cited by: 660
References: 52
Citations by year: 2026: 5 · 2025: 2 · 2024: 6 · 2023: 3 · 2022: 10 · 2021: 6 · 2020: 10 · 2019: 13 · 2018: 10 · 2017: 11 · 2016: 13 · 2015: 15 · 2014: 13 · 2013: 12 · 2012: 20
FWCI: 30.37
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: National Science Foundation
Howard Hughes Medical Institute
American Diabetes Association
National Institutes of Health
National Cancer Institute (P30CA 54174, P30CA054174, P50 CA58183, P50CA058183)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: nuclear receptor corepressor, SMRT, signaling pathways, retinoic acid receptor, estrogen receptor, tamoxifen resistance, breast cancer, transcriptional repression, ligand-dependent transcription, CREB-binding protein, coactivator complexes
MeSH terms: Animals, Breast Neoplasms, Disease Models, Animal, DNA-Binding Proteins, Drug Resistance, Estrogen Antagonists, Gene Expression Regulation, Humans, Models, Biological, Nuclear Proteins, Protein Binding, Protein Kinases, Receptors, Estrogen, Repressor Proteins, Tamoxifen, Signal Transduction, Genes, Reporter, Receptors, Retinoic Acid, Mice, Nuclear Receptor Co-Repressor 1, Nuclear Receptor Co-Repressor 2

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Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes.

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