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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Changes in expression of steroid receptors, their downstream target genes and their associated co-regulators during the sequential acquisition of tamoxifen resistance in vitro.
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“(Lavinsky et al., 1998).”
Transient over-expression of estrogen receptor-α in breast cancer cells promotes cell survival and estrogen-independent growth
Tolhurst, R., Thomas, R. S., Kyle, F., Patel, H., Periyasamy, M., Photiou, A., Thiruchelvam, P., Lai, C., Al-sabbagh, M., Fisher, R., et al. (2011) · Breast Cancer Research and Treatment · doi:10.1007/s10549-010-1122-6 · Cited by 31
Gper and erα mediate estradiol enhancement of mitochondrial function in inflamed adipocytes through a pka dependent mechanism
Bauzá-Thorbrügge, M., Rodríguez-Cuenca, S., Vidal-Puig, A., Galmés-Pascual, B. M., Sbert-Roig, M., Gianotti, M., Lladó, I., & Proenza, A. M. (2019) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2018.09.013 · Cited by 30
Targeting of the adaptor protein Tab2 as a novel approach to revert tamoxifen resistance in breast cancer cells
Cutrupi, S., Reineri, S., Panetto, A., Grosso, E., Caizzi, L., Ricci, L., Friard, O., Agati, S., Scatolini, M., Chiorino, G., et al. (2012) · Oncogene · doi:10.1038/onc.2011.627 · Cited by 30
Role of SUMOylation in Full Antiestrogenicity
Hilmi, K., Hussein, N., Mendoza-Sanchez, R., El-Ezzy, M., Ismail, H., Durette, C., Bail, M., Rozendaal, M., Bouvier, M., Thibault, P., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00290-12 · Cited by 30
“AEs prevent ER activation through the induction of an altered conformation of the receptor ligand binding domain (LBD) that suppresses the recruitment of coactivators (8, 66, 79) and/or increases the recruitment of corepressors (23, 34, 45, 61, 77, 83, 94).”
Background
Differential expression of genes for transcription factors in theca and granulosa cells following selection of a dominant follicle in cattle
Zielak, A., Canty, M., Forde, N., Coussens, P., Smith, G., Lonergan, P., Ireland, J., & Evans, A. (2008) · Molecular Reproduction and Development · doi:10.1002/mrd.20819 · Cited by 30
“Several studies (Chen and Evans, 1995; Lavinsky et al., 1998; Zhang et al., 1998; Jepsen et al., 2000) have demonstrated that the oestrogen receptor, in the presence of its antagonist tamoxifen, interacts with NCOR1.”
Background
Both N- and C-terminal transactivation functions of DNA-bound ERalpha are blocked by a novel synthetic estrogen ligand.
Yamamoto, Y., Wada, O., Takada, I., Yogiashi, Y., Shibata, J., Yanagisawa, J., Kitazato, K., & Kato, S. (2003) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2003.10.178 · Cited by 30
Regulation of nuclear receptor and cofactor expression in breast cancer cell lines.
Vienonen, A., Miettinen, S., Manninen, T., Altucci, L., Wilhelm, E., & Ylikomi, T. (2003) · European Journal of Endocrinology · doi:10.1530/eje.0.1480469 · Cited by 30
Effects of iron modulation on mesenchymal stem cell-induced drug resistance in estrogen-receptor-positive breast cancer
Buschhaus, J. M., Rajendran, S., Humphries, B. A., Cutter, A. C., Muñiz, A., Ciavattone, N. G., Buschhaus, A. M., Cañeque, T., Nwosu, Z., Sahoo, D., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02385-9 · Cited by 29
SIAH ubiquitin ligases regulate breast cancer cell migration and invasion independent of the oxygen status
Adam, M., Matt, S., Christian, S., Hess‐Stumpp, H., Haegebarth, A., Hofmann, T. G., & Algire, C. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1104441 · Cited by 34
Mini-review: estrogen action in the uterus and insulin-like growth factor-I.
Moyano, P., & Rotwein, P. (2004) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2004.09.001 · Cited by 29
Coactivators PGC-1β and SRC-1 Interact Functionally to Promote the Agonist Activity of the Selective Estrogen Receptor Modulator Tamoxifen
Kressler, D., Hock, M. B., & Kralli, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705596200 · Cited by 26
Steroid hormone receptors and coregulators in endocrine‐resistant and estrogen‐independent breast cancer cells
Sarvilinna, N., Eronen, H., Miettinen, S., Vienonen, A., & Ylikomi, T. (2006) · International Journal of Cancer · doi:10.1002/ijc.21431 · Cited by 28
“This is congruent with the result that decreased N-CoR protein levels have been observed to correlate with the acquisition of TAM resistance in a mouse model system.(13) High levels of coactivator AIB1 alone or together with high levels of HER-2/neu have also been shown to be associated with worse DFS in TAM-treated p…”
Result
An Antiestrogen-responsive Estrogen Receptor-α Mutant (D351Y) Shows Weak AF-2 Activity in the Presence of Tamoxifen*
Webb, P., Nguyen, P., Valentine, C. D., Weatherman, R., Scanlan, T., & Kushner, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007435200 · Cited by 28
A fusion protein of the estrogen receptor (ER) and nuclear receptor corepressor (NCoR) strongly inhibits estrogen-dependent responses in breast cancer cells.
Chien, P.-Y., Ito, M., Park, Y.-K., Tagami, T., Gehm, B. D., & Jameson, J. (1999) · Molecular Endocrinology · doi:10.1210/mend.13.12.0394 · Cited by 28
“Transcriptional silencing by unliganded TR and RAR involves the recruitment of CoRs such as NCoR and SMRT, which in turn recruit a complex containing Sin3 and HDAC (36).”
BackgroundInfluential
Pharmacology of Nuclear Receptor–Coregulator Recognition
Savkur, R. S., Bramlett, K. S., Clawson, D. K., & Burris, T. P. (2004) · Vitamins and hormones · doi:10.1016/s0083-6729(04)68005-8 · Cited by 34
Identification and Molecular Characterization of HOS15-interacting Proteins in Arabidopsis thaliana
Park, J., Lim, C. J., Khan, I. U., Jan, M., Khan, H. A., Park, H. J., Guo, Y., & Yun, D. (2018) · Journal of Plant Biology · doi:10.1007/s12374-018-0313-2 · Cited by 28
Hakai acts as a coregulator of estrogen receptor alpha in breast cancer cells
Gong, E.-Y., Park, E., & Lee, K. (2010) · Cancer Science · doi:10.1111/j.1349-7006.2010.01636.x · Cited by 27
Interactions between the estrogen receptor, its cofactors and microRNAs in breast cancer
McCafferty, M. P. J., McNeill, R. E., Miller, N., & Kerin, M. J. (2009) · Breast Cancer Research and Treatment · doi:10.1007/s10549-009-0429-7 · Cited by 28
“However, in the case of a partial agonist like tamoxifen, corepressors may become rate limiting such that a decrease in their levels may suppress the inhibitory effects of tamoxifen on the ER resulting in development of resistance [48, 49 ] and shorter disease-free survival [50].”
Background
IFI27/ISG12 Downregulates Estrogen Receptor α Transactivation by Facilitating Its Interaction With CRM1/XPO1 in Breast Cancer Cells
Cervantes-Badillo, M. G., Paredes-Villa, A., Gómez-Romero, V., Cervantes-Roldán, R., Arias-Romero, L. E., Villamar-Cruz, O., González-Montiel, M., Barrios-Garcia, T., Cabrera-Quintero, A. J., Rodríguez-Gómez, G., et al. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.568375 · Cited by 26
“For example, increased expression the coactivators SRC-1 and NHERF2 or the loss of expression of corepressors such as NCoR and TTP correlate with cell proliferation, tumor development and progression (19, 20, 34, 52).”
Background
Nuclear Receptor Corepressor 1 Expression and Output Declines with Prostate Cancer Progression
Lopez, S. M., Agoulnik, A. I., Zhang, M., Peterson, L. E., Suarez, E., Gandarillas, G. A., Frolov, A., Li, R., Rajapakshe, K., Coarfa, C., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-1983 · Cited by 25
“cancer (50) and with breast cancer recurrence in human patients (51).”
Background
Agonist-dependent Repression Mediated by Mutant Estrogen Receptor α That Lacks the Activation Function 2 Core Domain*
Jung, D., Lee, S.-K., & Lee, J. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106860200 · Cited by 26
The dual function steroid receptor coactivator/ubiquitin protein-ligase integrator E6-AP is overexpressed in mouse mammary tumorigenesis
Sivaraman, L., Nawaz, Z., Medina, D., Conneely, O. M., & O’Malley, B. W. (2000) · Breast Cancer Research and Treatment · doi:10.1023/a:1006410111706 · Cited by 22
Evolving concepts of selective estrogen receptor action: from basic science to clinical applications.
Smith, C., & O'Malley, B. (1999) · Trends in endocrinology and metabolism · doi:10.1016/s1043-2760(99)00183-6 · Cited by 26
Comparison of tamoxifen ligands on estrogen receptor interaction with estrogen response elements.
Klinge, C., Studinski-Jones, A. L., Kulakosky, P. C., Bambara, R., & Hilf, R. (1998) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(98)00130-0 · Cited by 26
Melatonin inhibits mitogenic cross-talk between retinoic acid-related orphan receptor alpha (RORα) and ERα in MCF-7 human breast cancer cells
Dong, C., Yuan, L., Dai, J., Lai, L., Mao, L., Xiang, S., Rowan, B. G., & Hill, S. M. (2010) · Steroids · doi:10.1016/j.steroids.2010.06.002 · Cited by 27
SRA coactivation of estrogen receptor-alpha is phosphorylation-independent, and enhances 4-hydroxytamoxifen agonist activity.
Coleman, K. M., Lam, V., Jaber, B. M., Lanz, R., & Smith, C. L. (2004) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2004.08.090 · Cited by 25
Identification of a Novel Testicular Orphan Receptor-4 (TR4)-associated Protein as Repressor for the Selective Suppression of TR4-mediated Transactivation*
Yang, Y., Wang, X., Dong, T., Kim, E., Lin, W.-J., & Chang, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207116200 · Cited by 25
Selective estrogen receptor modulators (SERMS): keys to understanding their function
Liu, J. H. (2020) · Menopause · doi:10.1097/gme.0000000000001585 · Cited by 24
“The mechanism of action for 4-hydroxytamoxifen is believed to be recruitment of transcription factor proteins such as nuclear receptor corepressor (NCoR) and silencing mediator of retinoid and thyroid hormone receptors (SMRT) responsible for estrogen action in breast cancer cells.(20)”
Background
Class I Lysine Deacetylases Facilitate Glucocorticoid-induced Transcription*
Kadiyala, V., Patrick, N. M., Mathieu, W., Jaime-Frias, R., Pookhao, N., An, L.-L., & Smith, C. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.505115 · Cited by 24
Extranuclear expression of hormone receptors in primary breast cancer
Kim, R., Kaneko, M., Arihiro, K., Emi, M., Tanabe, K., Murakami, S., Osaki, A., & Inai, K. (2006) · Annals of Oncology · doi:10.1093/annonc/mdl118 · Cited by 22
“The expression of these target genes is coregulated by corepressors such as nuclear receptor corepressor (NCoR) [13] and histone deacetylase 1 (HDAC1) [14] which compete with coactivators for binding, and mediate the inhibitory effects of estrogen receptor antagonists such as tamoxifen.”
Background
Analysis of co-factor function in a glucocorticoid-resistant small cell carcinoma cell line.
Waters, C., Stevens, A., White, A., & Ray, D. (2004) · Journal of Endocrinology · doi:10.1677/joe.1.05804 · Cited by 24
“It has previously been shown that the level of expression of co-activator and co-repressor proteins can modulate nuclear receptor function (Jackson et al. 1997, Smith et al. 1997, Lavinsky et al. 1998, Fryer et al. 2000).”
The Histone Demethylase Enzymes KDM3A and KDM4B Co-Operatively Regulate Chromatin Transactions of the Estrogen Receptor in Breast Cancer
Jones, D., Wilson, L., Thomas, H., Gaughan, L., & Wade, M. (2019) · Cancers · doi:10.3390/cancers11081122 · Cited by 23
HEXIM1 is a critical determinant of the response to tamoxifen
Ketchart, W., Ogba, N., Kresak, A., Albert, J., Pink, J., & Montano, M. (2011) · Oncogene · doi:10.1038/onc.2011.76 · Cited by 23
“Proposed bases for tamoxifen resistance include loss of ER expression/function, activation of growth factor signaling pathways that circumvent tumor reliance on ERa signaling, and alterations in the expression of co-regulatory proteins involved in mediating ER target gene transcription (Lavinsky et al., 1998; Ring and…”
BackgroundInfluential
Progressive Loss of Estrogen Receptor α Cofactor Recruitment in Endocrine Resistance
Naughton, C., Macleod, K., Kuske, B., Clarke, R., Cameron, D., & Langdon, S. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0110 · Cited by 23
Development and characterization of a tamoxifen-resistant breast carcinoma xenograft
Naundorf, H., Becker, M., Lykkesfeldt, A., Elbe, B., Neumann, C., Büttner, B., & Fichtner, I. (2000) · British Journal of Cancer · doi:10.1054/bjoc.2000.1156 · Cited by 23
“– Involvement of different co-factors in transcriptional machinery (Landel et al, 1994; Lavinsky et al, 1998).”
Sorafenib and nilotinib resensitize tamoxifen resistant breast cancer cells to tamoxifen treatment via estrogen receptor α
PEDERSEN, A. M., Thrane, S., Lykkesfeldt, A. E., & Yde, C. W. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2619 · Cited by 21
“ER co-regulators play important roles for determining whether tamoxifen functions as an antagonist or agonist (4).”
Background
Oestrogen receptor-alpha regulates non-canonical Hedgehog-signalling in the mammary gland
Okolowsky, N., Furth, P. A., & Hamel, P. A. (2014) · Developmental Biology · doi:10.1016/j.ydbio.2014.04.007 · Cited by 20
Negative regulation of ERα by a novel protein CAC1 through association with histone demethylase LSD1
Kim, J., Park, U.-H., Moon, M., Um, S., & kim, E.-J. (2013) · FEBS Letters · doi:10.1016/j.febslet.2012.10.054 · Cited by 22
“Different from other NRs, antagonist-loaded ERa binds to target gene EREs and recruits NCoR and SMRT corepressor complexes for transcriptional repression [9,10].”
Background
Potential of Selective Estrogen Receptor Modulators as Treatments and Preventives of Breast Cancer
Peng, J., Sengupta, S., & Jordan, V. (2009) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152009788451833 · Cited by 22
“It has been shown that inhibition of NCoR or SMRT with monoclonal antibodies can enhance the agonistic property of 4-hydroxytamoxifen [46].”
Acetylation of nuclear receptors in health and disease: an update
Ashton, A. W., Dhanjal, H. K., Rossner, B., Mahmood, H., Patel, V. I., Mohammad, N., Lota, M., Shahid, F., Li, Z., Joyce, D. A., et al. (2022) · FEBS Journal · doi:10.1111/febs.16695 · Cited by 27
“Activation of epidermal growth factor receptor (EGFR), a tyrosine kinase receptor, regulates SMRT and N-CoR function, inhibiting recruitment to ER a , PR and RAR but stimulating recruitment to PPAR c [142,143].”
Background
Nuclear Receptor Coregulators in Hormone-Dependent Cancers
Jafari, H., Hussain, S., & Campbell, M. (2022) · Cancers · doi:10.3390/cancers14102402 · Cited by 21

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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