The DOI matches its Crossref record; 156 of the 156 references it cites were found in a registry or an index.
Estrogen receptor signaling mechanisms
Open accessAbstract
The primary female sex hormones, estrogens, are responsible for the control of functions of the female reproductive system, as well as the development of secondary sexual characteristics that appear during puberty and sexual maturity. Estrogens exert their actions by binding to specific receptors, the estrogen receptors (ERs), which in turn activate transcriptional processes and/or signaling events that result in the control of gene expression. These actions can be mediated by direct binding of estrogen receptor complexes to specific sequences in gene promoters (genomic effects), or by mechanisms that do not involve direct binding to DNA (non-genomic effects). Whether acting via direct nuclear effects, indirect non-nuclear actions, or a combination of both, the effects of estrogens on gene expression are controlled by highly regulated complex mechanisms. In this chapter, we summarize the knowledge gained in the past 60 years since the discovery of the estrogen receptors on the mechanisms governing estrogen-mediated gene expression. We provide an overview of estrogen biosynthesis, and we describe the main mechanisms by which the female sex hormone controls gene transcription in different tissues and cell types. Specifically, we address the molecular events governing regulation of gene expression via the nuclear estrogen receptors (ERα, and ERβ) and the membrane estrogen receptor (GPER1). We also describe mechanisms of cross-talk between signaling cascades activated by both nuclear and membrane estrogen receptors. Finally, we discuss natural compounds that are able to target specific estrogen receptors and their implications for human health and medical therapeutics.
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Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, K., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,203
Cloning of a novel receptor expressed in rat prostate and ovary.
Kuiper, G. G., Enmark, E., Pelto-Huikko, M., Nilsson, S., & Gustafsson, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5925 · Cited by 4,788
Interaction of Estrogenic Chemicals and Phytoestrogens with Estrogen Receptor β
Kuiper, G. G. J. M., Lemmen, J. G., Carlsson, B., Corton, J. C., Safe, S. H., van der Saag, P. T., van der Burg, B., & Gustafsson, J.-Å. (1998) · Endocrinology · doi:10.1210/endo.139.10.6216 · Cited by 4,203
Shiau, A. K., Barstad, D., Loria, P. M., Cheng, L., Kushner, P. J., Agard, D. A., & Greene, G. L. (1998) · Cell · doi:10.1016/s0092-8674(00)81717-1 · Cited by 2,729
Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily
Oñate, S. A., Tsai, S. Y., Tsai, M.-J., & O'Malley, B. W. (1995) · Science · doi:10.1126/science.270.5240.1354 · Cited by 2,387
Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A
Green, S., Walter, P., Kumar, V., Krust, A., Bornert, J.-M., Argos, P., & Chambon, P. (1986) · Nature · doi:10.1038/320134a0 · Cited by 2,321
A transmembrane intracellular estrogen receptor mediates rapid cell signaling
Revankar, C. M., Cimino, D. F., Sklar, L. A., Arterburn, J. B., & Prossnitz, E. R. (2005) · Science · doi:10.1126/science.1106943 · Cited by 2,302
A signature motif in transcriptional co-activators mediates binding to nuclear receptors
Heery, D. M., Kalkhoven, E., Hoare, S., & Parker, M. G. (1997) · Nature · doi:10.1038/42750 · Cited by 2,128
Nilsson, S., Mäkelä, S., Treuter, E., Tujague, M., Thomsen, J., Andersson, G., Enmark, E., Pettersson, K., Warner, M., & Gustafsson, J.-Å. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.4.1535 · Cited by 1,996
Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase
Kato, S., Endoh, H., Masuhiro, Y., Kitamoto, T., Uchiyama, S., Sasaki, H., Masushige, S., Gotoh, Y., Nishida, E., Kawashima, H., et al. (1995) · Science · doi:10.1126/science.270.5241.1491 · Cited by 1,964
Research works printed but not linked: 12
- Allen, 1983, Landmark article Sept 8, 1923. An ovarian hormone. Preliminary report on its localization, extraction and partial purification, and action in test animals. By Edgar Allen and Edward A. Doisy, JAMA, 250, 2681, 10.1001/jama.1983.03340190083041 · doi:10.1001/jama.1983.03340190083041
- Aravindakshan, 2004, Consequences of xenoestrogen exposure on male reproductive function in spottail shiners (Notropis hudsonius), Toxicological Sciences: An Official Journal of the Society of Toxicology, 78, 156, 10.1093/toxsci/kfh042 · doi:10.1093/toxsci/kfh042
- Blizzard, 2006, Androstenediol analogs as ER-beta-selective SERMs, Bioorganic & Medicinal Chemistry Letters, 16, 834, 10.1016/j.bmcl.2005.11.014 · doi:10.1016/j.bmcl.2005.11.014
- Blizzard, 2007, Androstene-3,5-dienes as ER-beta selective SERMs, Bioorganic & Medicinal Chemistry Letters, 17, 6295, 10.1016/j.bmcl.2007.09.001 · doi:10.1016/j.bmcl.2007.09.001
- Hu, 2015, Molecular mechanisms of tamoxifen-associated endometrial cancer (Review), Oncology Letters, 9, 1495, 10.3892/ol.2015.2962 · doi:10.3892/ol.2015.2962
- ITTRICH, 1963, PARTICIPATION OF THE FETUS IN ESTROGEN METABOLISM OF THE MOTHER, Ceskoslovenská Gynekologie, 28, 454
- Jensen, 1967, Estrogen-binding substances of target tissues, Science (New York, N.Y.), 158, 529, 10.1126/science.158.3800.529-c · doi:10.1126/science.158.3800.529-c
- Laliotis, 2013, Immunohistochemical study of pElk-1 expression in human breast cancer: Association with breast cancer biologic profile and clinicopathologic features, Breast, 22, 89, 10.1016/j.breast.2012.09.013 · doi:10.1016/j.breast.2012.09.013
- Papapetropoulos, 2007, A ginseng-derived oestrogen receptor beta (ERbeta) agonist, Rb1 ginsenoside, attenuates capillary morphogenesis, British Journal of Pharmacology, 152, 172, 10.1038/sj.bjp.0707360 · doi:10.1038/sj.bjp.0707360
- Scheidereit, 1986, Mechanism of gene regulation by steroid hormones, Journal of Steroid Biochemistry, 24, 19, 10.1016/0022-4731(86)90026-9 · doi:10.1016/0022-4731(86)90026-9
- Turner, 2007, Molecular aspects of phytoestrogen selective binding at estrogen receptors, Journal of Pharmaceutical Sciences, 96, 1879, 10.1002/jps.20987 · doi:10.1002/jps.20987
- Williams, 1998, Xenobiotics and xenoestrogens in fish: Modulation of cytochrome P450 and carcinogenesis, Mutation Research, 399, 179, 10.1016/S0027-5107(97)00255-8 · doi:10.1016/s0027-5107(97)00255-8
Cited by
Role of estrogen receptors in health and disease
Chen, P., Li, B., & Ou-Yang, L. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.839005 · Cited by 339
Intrinsically disordered proteins play diverse roles in cell signaling
Bondos, S. E., Dunker, A. K., & Uversky, V. N. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00821-7 · Cited by 222
Obesity I: Overview and molecular and biochemical mechanisms
Lustig, R. H., Collier, D., Kassotis, C., Roepke, T. A., Kim, M. J., Blanc, E., Barouki, R., Bansal, A., Cave, M. C., Chatterjee, S., et al. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115012 · Cited by 203
Estrogens in adipose tissue physiology and obesity-related dysfunction
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Minireview: parabens exposure and breast cancer
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Metadata
- Venue
- Advances in Protein Chemistry and Structural Biology
- Publisher
- Elsevier
- Published
- 2019
- Volume
- 116
- Pages
- 135-170
- ISSN
- 1876-1623 (ISSN-L)
- OpenAlex
- W2914371319
- Cited by
- 988
- References
- 156
- FWCI
- 201.87
- Type
- book chapter
- Language
- en
- Open access
- green
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Funders
- National Institutes of Health (K01HL133520, R03HL141618)
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