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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Background
Augmentation of estrogen receptor-mediated transcription by steroid and xenobiotic receptor
Rokutanda, N., Iwasaki, T., Odawara, H., Nagaoka, R., Miyazaki, W., Takeshita, A., Koibuchi, Y., Horiguchi, J., Shimokawa, N., Iino, Y., et al. (2008) · Endocrine · doi:10.1007/s12020-008-9091-9 · Cited by 11
Dual-target inhibitors based on ERα: Novel therapeutic approaches for endocrine resistant breast cancer
Xiong, S., Song, K., Xiang, H., & Luo, G. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116393 · Cited by 10
Naringenin Inhibits Proliferation and Survival of Tamoxifen‐ Resistant Breast Cancer Cells
Ramos, J., Hatkevich, T., Eanes, L. A., Santos-Sanchez, I., & Patel, Y. (2017) · doi:10.5772/66698 · Cited by 11
Nuclear corepressor 1 expression predicts response to first-line endocrine therapy for breast cancer patients on relapse.
Zhang, Z.-H., Yamashita, H., Toyama, T., Yamamoto, Y., Kawasoe, T., Ibusuki, M., Tomita, S., Sugiura, H., Kobayashi, S., Fujii, Y., et al. (2009) · Chinese Medical Journal · doi:10.3760/cma.j.issn.0366-6999.2009.15.009 · Cited by 11
Corepressor subnuclear organization is regulated by estrogen receptor via a mechanism that requires the DNA-binding domain.
Voss, T., Demarco, I. A., Booker, C. F., & Day, R. N. (2005) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2004.12.003 · Cited by 11
Endocrine therapy and other targeted therapies for metastatic breast cancer
Hussain, S. A., Palmer, D. H., Moon, S., & Rea, D. W. (2004) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.4.6.1179 · Cited by 11
Reporter gene assay demonstrates functional differences in estrogen receptor activity in purified breast cancer cells: A pilot study
Singh, A., Ali, S., Kothari, M., de Bella, M. T., Smith, C. W., Timms, E., Slade, M., Foxwell, B., & Coombes, R. C. (2003) · International Journal of Cancer · doi:10.1002/ijc.11469 · Cited by 11
Genetic engineering of the glucocorticoid receptor by fusion with the herpes viral protein VP22 causes selective loss of transactivation
Soden, J., Stevens, A., & Ray, D. W. (2002) · Journal of Endocrinology · doi:10.1677/joe.0.1720615 · Cited by 9
Cellular Mechanisms of Endocrine Disruption
Adler, S. (2007) · Humana Press eBooks · doi:10.1007/1-59745-107-x_6 · Cited by 11
Breast cancer plasticity is restricted by a LATS1-NCOR1 repressive axis
Aylon, Y., Furth, N., Mallel, G., Friedlander, G., Nataraj, N. B., Dong, M., Hassin, O., Zoabi, R., Cohen, B., Drendel, V., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34863-9 · Cited by 14
Nuclear Receptors Are Differentially Expressed and Activated in KAIMRC1 Compared to MCF7 and MDA-MB231 Breast Cancer Cells
Nehdi, A., Ali, R., Alhallaj, A., Alzahrani, H., Samman, N., Mashhour, A., Baz, O., Barhoumi, T., Alghanem, B., Khan, A., et al. (2019) · Molecules · doi:10.3390/molecules24112028 · Cited by 10
“Nuclear receptors function as transcription factors to regulate the gene-expression through the interaction with other coactivators and corepressors [54].”
Background
αNAC interacts with histone deacetylase corepressors to control Myogenin and Osteocalcin gene expression.
Jafarov, T., Alexander, J. M., & St-Arnaud, R. (2012) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagrm.2012.10.005 · Cited by 10
“Posttranslational modifications such as phosphorylation [42], acetylation [43], methylation [44], or SUMOylation [45] have also been characterized asmechanisms thatmediate differential recruitment of coregulator complexes.”
Application of Aptamers in Food Safety
Xu, D.-M., Wu, M., Zou, Y., Zhang, Q., Wu, C., Zhou, Y., & Liu, X.-J. (2011) · doi:10.1016/s1872-2040(10)60447-1 · Cited by 10
PPARγ and PPARδ as Modulators of Neoplasia and Cell Fate
Glazer, R., Yuan, H.-Y., Xie, Z., & Yin, Y.-Z. (2008) · PPAR Research · doi:10.1155/2008/247379 · Cited by 10
The AF-2 cofactor binding region is key for the selective SUMOylation of estrogen receptor alpha by antiestrogens
Vallet, A., Ezzy, M. E., Diennet, M., Haidar, S., Bouvier, M., & Mader, S. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102757 · Cited by 9
“This drastic conformational change prevents the binding of coactivators by AF-2 and favors the recruitment of corepressors SMRT and NCoR (25–29).”
Background
Tristetraprolin: A cytosolic regulator of mRNA turnover moonlighting as transcriptional corepressor of gene expression
Rodríguez-Gómez, G., Paredes-Villa, A., Cervantes-Badillo, M. G., Gómez-Sonora, J. P., Jorge-Pérez, J. H., Cervantes-Roldán, R., & León‐Del‐Río, A. (2021) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2021.03.015 · Cited by 11
Molecular Mechanisms of Endocrine Resistance
Fu, X., Angelis, C. D., Veeraraghavan, J., Osborne, C. K., & Schiff, R. (2018) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-99350-8_11 · Cited by 8
Self-citation
Zinc finger protein 131 inhibits estrogen signaling by suppressing estrogen receptor α homo-dimerization.
Oh, Y., & Chung, K. (2013) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2012.11.031 · Cited by 9
E-cadherin mediates the aggregation of breast cancer cells induced by tamoxifen and epidermal growth factor
Mauro, L., Pellegrino, M., Lappano, R., Vivacqua, A., Giordano, F., Palma, M. G., Andò, S., & Maggiolini, M. (2010) · Breast Cancer Research and Treatment · doi:10.1007/s10549-009-0456-4 · Cited by 9
“Of interest, partial antagonists of ERα, such as 4-hydroxytamoxifen (OHT), may display cell- and promoter-specific agonist effects that are thought to be due, at least in part, to AF1 activity and/or to the ability to recruit cofactors [10-12].”
Background
Expression of ZER6 in ERα-Positive Breast Cancer
Stabach, P., Thiyagarajan, M., & Weigel, R. (2005) · doi:10.1016/j.jss.2005.02.006 · Cited by 9
“In addition, co-repressors including N-CoR [12] and SMRT [12, 13] have the ability to inhibit or diminish transactivation by ER .”
Background
Genetic network identification by high density, multiplexed reversed transcriptional (HD-MRT) analysis in steroidogenic axis model cell lines
Clipsham, R. C., Zhang, Y.-H., Huang, B., & McCabe, E. R. B. (2002) · Molecular Genetics and Metabolism · doi:10.1016/s1096-7192(02)00119-1 · Cited by 8
Coactivators and Corepressors
McKenna, N. J., Nawaz, Z., Tsai, S. Y., & Tsai, M. (2000) · Humana Press eBooks · doi:10.1007/978-1-59259-032-2_22 · Cited by 7
Epigenetic factors in breast cancer therapy
Mathur, R., Jha, N. K., Saini, G., Jha, S. K., Shukla, S. P., Filipejová, Z., Kesari, K. K., Iqbal, D., Nand, P., Upadhye, V. J., et al. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.886487 · Cited by 13
“, the ER isoform) culminates in an endocrine-insensitive phenotype, that is rare (Lavinsky et al., 1998; Shou et al., 2004; Musgrove and Sutherland, 2009).”
Background
The ETS Family Member TEL Binds to Nuclear Receptors RAR and RXR and Represses Gene Activation
Meester-Smoor, M. A., Janssen, M. J. F. W., ter Haar, W. M., van Wely, K. V., Aarnoudse, A., van Oord, G. V., van Tilburg, G. B. A., & Zwarthoff, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023620 · Cited by 8
“associate with RAR and recruit complexes with histone deacetylase (HDAC) activity [4,5].”
Background
Non‐steroidal antiandrogens act as AF‐1 agonists under conditions of high androgen‐receptor expression
Fuse, H., Korenaga, S., Sakari, M., Hiyama, T., Ito, T., Kimura, K., & Kato, S. (2007) · The Prostate · doi:10.1002/pros.20269 · Cited by 8
“It has also been proposed in a study on the breast cancer cell, MCF-7, that these cells may acquire resistance to tamoxifen through enhancement of ER AF-1 activity [35].”
Reproductive toxicity assessment of lasofoxifene, a selective estrogen receptor modulator (SERM), in female rats.
Cappon, G., Horimoto, M., & Hurtt, M. (2004) · Birth defects research. Part B. Developmental and reproductice toxicology · doi:10.1002/bdrb.20008 · Cited by 8
Mechanisms of Resistance to Endocrine Therapy
Hynes, N. (2002) · doi:10.1201/b14067-21 · Cited by 8
Single-tube gene-specific expression analysis by high primer density multiplex reverse transcription.
Clipsham, R., & Mccabe, E. R. B. (2001) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2001.3261 · Cited by 8
Promise and failure of targeted therapy in breast cancer
Giordano, A. (2011) · Frontiers in Bioscience-Scholar · doi:10.2741/273 · Cited by 5
Drugs affecting growth of tumours
Pinedo, H., & Smorenburg, C. (2006) · doi:10.1007/3-7643-7407-1 · Cited by 8
Chemoprevention of Breast Cancer
Fabian, C., & Kimler, B. (2002) · Drugs & Aging · doi:10.2165/00002512-200219010-00004 · Cited by 8
“Clinical resistance to SERMs may be because of a variety of factors, including: (i) loss of ER-α expression through methylation;[309] (ii) increase in ER-β relative to ER-α;[310] (iii) increased availability of coactivators as a result of growth factor receptor-mediated tyrosine kinase activity;[120,121,311-315] (iv)…”
Background
Exploring new pathways in endocrine-resistant breast cancer
de Pinho, I. S., Abreu, C., Gomes, I., Casimiro, S., Pacheco, T. R., Sousa, R., & Costa, L. (2022) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2022.00086 · Cited by 8
In-silico identification of potential inhibitors targeting the DNA binding domain of estrogen receptor α for the treatment of hormone therapy-resistant breast cancer
Bouricha, E. M., Hakmi, M., Akachar, J., Zouaidia, F., & Ibrahimi, A. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1869094 · Cited by 7
Contribution of HDAC3 to transcriptional repression by the human papillomavirus 31 E8^E2 protein.
Dreer, M., Blondzik, S., Straub, E., Iftner, T., & Stubenrauch, F. (2020) · Journal of General Virology · doi:10.1099/jgv.0.001438 · Cited by 7
An occult urothelial carcinoma with wide multiorgan metastases and its genetic alteration profiling
Bu, K., Shi, Z., Lu, Y., Zhao, J., & Li, B. (2019) · Medicine · doi:10.1097/md.0000000000015245 · Cited by 7
“However, in breast cancer, patients with a high expression of NCOR1 have a better prognosis than those with low expression.([41]) In this case, the patient with occult urothelial carcinoma had a NCOR1 S1952∗ mutation which resulted in protein truncation.”
Background
Minireview: The Versatile Roles of Lysine Deacetylases in Steroid Receptor Signaling
Kadiyala, V., & Smith, C. L. (2014) · Molecular Endocrinology · doi:10.1210/me.2014-1002 · Cited by 5
An overview of nuclear receptor coregulators involved in cerebellar development
Nishihara, E. (2008) · The Cerebellum · doi:10.1007/s12311-008-0018-z · Cited by 9
“While a variety of kinase-mediated cellular signaling pathways modulate NRs (102), their phosphorylation decreases their interaction with corepressors (103) and leads to recruitment of coactivators, including SRC-1 (104).”
Background
Flow cytometry-based FRET identifies binding intensities in PPARγ1 protein-protein interactions in living cells
Trümper, V., von Knethen, A., Preuß, A., Ermilov, E. A., Hackbarth, S., Kuchler, L., Gunne, S., Schäfer, A., Bornhütter, T., Vereb, G., et al. (2019) · Theranostics · doi:10.7150/thno.29367 · Cited by 10
“In recent years, a multitude of studies have described NHR – N-CoR2 binding and protein interactions [66, 67, 85, 86].”
PPARδ as a Metabolic Initiator of Mammary Neoplasia and Immune Tolerance
Glazer, R. (2016) · PPAR Research · doi:10.1155/2016/3082340 · Cited by 6
A tale of two estrogen receptors (ERs): how differential ER-estrogen responsive element interactions contribute to subtype-specific transcriptional responses
Huang, J., Li, X.-D., Qiao, T., Bambara, R., Hilf, R., & Muyan, M. (2006) · Nuclear Receptor Signaling · doi:10.1621/nrs.04015 · Cited by 6
“Studies indicate that ERα interacts, albeit weakly, with SMRT and NCoR, in the absence of E2 [Lavinsky et al., 1998; Webb et al., 2003].”
Background
Stroma-mediated expression of estrogen and its role in cancer.
Sachdeva, M., & Mo, Y. (2010) · Frontiers in Bioscience · doi:10.2741/3618 · Cited by 6
Anti-hormone Therapy: Principles of Endocrine Therapy of Cancer
Hoffmann, J., & Sommer, A. (2006) · Topics in medicinal chemistry · doi:10.1007/7355_2006_002 · Cited by 7
Clinical Approaches to Discovering and Testing New Breast Cancer Prevention Drugs
Fabian, C., Kimler, B., Mayo, M., Grizzle, W., Masood, S., & Ursin, G. (2005) · Humana Press eBooks · doi:10.1007/978-1-59259-768-0_17 · Cited by 6

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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