Abstract
Steroid hormones, i.e., androgens, estrogens, glucocorticoids, mineralocorticoids, and progestins, bind with high affinity to their respective steroid hormone receptors (SR). SRs are members of a family of nuclear receptors (NR). Ligand-activated SRs dissociate from hsp90 chaperone complexes in the cytoplasm and enter the nucleus where they bind to specific DNA sequences: hormone response elements (HREs). SRs interact with coregulator proteins (coactivators and corepressors) as well as chromatin remodeling complexes to regulate target gene expression. In addition, some SRs are also associated with the plasma membrane (PM) and PM proteins. Hormone binding to PM-associated SRs activates G-protein coupled receptors (GPCR) and intracellular signaling pathways ultimately regulating gene transcription and other downstream sequelae. This chapter will review of SR/NR including protein structure, ligand activation, gene regulation, examples of rapid “non-genomic” signaling, and the roles of these receptors in human health and disease.
This is a preview of subscription content, log in via an institution to check access.
References
Acconcia F, Ascenzi P, Bocedi A, Spisni E, Tomasi V, Trentalance A, Visca P, Marino M. Palmitoylation-dependent estrogen receptor {alpha} membrane localization: regulation by 17{beta}-Estradiol. Mol Biol Cell. 2005;16:231–7.
Altuwaijri S, Lee DK, Chuang KH, Ting HJ, Yang Z, Xu Q, Tsai MY, Yeh S, Hanchett LA, Chang HC, Chang C. Androgen receptor regulates expression of skeletal muscle-specific proteins and muscle cell types. Endocrine. 2004;25:27–32.
Anolik JH, Klinge CM, Bambara RA, Hilf R. Differential impact of flanking sequences on estradiol- versus 4-hydroxytamoxifen-liganded estrogen receptor binding to estrogen responsive element DNA. J Steroid Biochem Mol Biol. 1993;46:713–30.
Anolik JH, Klinge CM, Hilf R, Bambara RA. Cooperative binding of estrogen receptor to DNA depends on spacing of binding sites, flanking sequence, and ligand. Biochemistry (Mosc). 1995;34:2511–20.
Anolik JH, Klinge CM, Brolly CL, Bambara RA, Hilf R. Stability of the ligand of estrogen response element-bound estrogen receptor depends on flanking sequences and cellular factors. J Steroid Biochem Mol Biol. 1996;59:413–29.
Archer TK, Fryer CJ, Lee H-L, Zaniewski E, Liang T, Mymryk JS. Steroid hormone receptor status defines the MMTV promoter chromatin structure in vivo. J Steroid Biochem Mol Biol. 1995;53:421–9.
Audet-Walsh E, Giguere V. The multiple universes of estrogen-related receptor alpha and gamma in metabolic control and related diseases. Acta Pharmacol Sin. 2015;36:51–61.
Aumais JP, Lee HS, DeGannes C, Horsford J, White J. Function of directly repeated half sites as response elements for steroid hormones. J Biol Chem. 1996;271:12568–77.
Banerjee M, Robbins D, Chen T. Modulation of xenobiotic receptors by steroids. Molecules (Basel, Switzerland). 2013;18:7389–406.
Banerjee M, Robbins D, Chen T. Targeting xenobiotic receptors PXR and CAR in human diseases. Drug Discov Today. 2015;20:618–28.
Barletta F, Wong CW, McNally C, Komm BS, Katzenellenbogen B, Cheskis BJ. Characterization of the interactions of estrogen receptor and MNAR in the activation of cSrc. Mol Endocrinol. 2004;18:1096–108.
Barton M, Prossnitz ER. Emerging roles of GPER in diabetes and atherosclerosis. Trends Endocrinol Metab. 2015;26:185–92.
Bastien J, Rochette-Egly C. Nuclear retinoid receptors and the transcription of retinoid-target genes. Gene. 2004;328:1–16.
Baulieu EE, Robel P. Non-genomic mechanisms of action of steroid hormones. Ciba Found Symp. 1995;191:24–37.
Baulieu EE, Schumacher M. Neurosteroids, with special reference to the effect of progesterone on myelination in peripheral nerves. Mult Scler. 1997;3:105–12.
Beato M, Chalepakis G, Schauer M, Slater EP. DNA regulatory elements for steroid hormones. J Steroid Biochem. 1989;32:737–47.
Benoit G, Malewicz M, Perlmann T. Digging deep into the pockets of orphan nuclear receptors: insights from structural studies. Trends Cell Biol. 2004;14:369–76.
Berger S, Bleich M, Schmid W, Cole TJ, Peters J, Watanabe H, Kriz W, Warth R, Greger R, Schutz G. Mineralocorticoid receptor knockout mice: pathophysiology of Na+ metabolism. Proc Natl Acad Sci U S A. 1998;95:9424–9.
Boonyaratanakornkit V. Scaffolding proteins mediating membrane-initiated extra-nuclear actions of estrogen receptor. Steroids. 2011;76:877–84.
Böttner M, Thelen P, Jarry H. Estrogen receptor beta: tissue distribution and the still largely enigmatic physiological function. J Steroid Biochem Mol Biol. 2014;139:245–51.
Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXRα. Nature. 1995;375:377–82.
Bourguet W, Germain P, Gronemeyer H. Nuclear receptor ligand-binding domains: three-dimensional structures, molecular interactions and pharmacological implications. Trends Pharmacol Sci. 2000;21:381–8.
Braun AM, Thomas P. Biochemical characterization of a membrane androgen receptor in the ovary of the atlantic croaker (Micropogonias undulatus). Biol Reprod. 2004;71:146–55.
Brzozowski AM, Pike AC, Dauter Z, Hubbard RE, Bonn T, Engstrom O, Ohma L, Greene GL, Gustafsson JA, Carlquist M. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature. 1997;389:753–8.
Bulayeva NN, Watson CS. Xenoestrogen-induced ERK-1 and ERK-2 activation via multiple membrane-initiated signaling pathways. Environ Health Perspect. 2004;112:1481–7.
Bulayeva NN, Gametchu B, Watson CS. Quantitative measurement of estrogen-induced ERK 1 and 2 activation via multiple membrane-initiated signaling pathways. Steroids. 2004a;69:181–92.
Bulayeva NN, Wozniak A, Lash LL, Watson CS. Mechanisms of membrane estrogen receptor-{alpha}-mediated rapid stimulation of Ca2+ levels and prolactin release in a pituitary cell line. Am J Physiol Endocrinol Metab. 2004b. doi:10.1152/ajpendo.00349.2004.
Burns KA, Li Y, Arao Y, Petrovich RM, Korach KS. Selective mutations in estrogen receptor α D-domain alters nuclear translocation and non-estrogen response element gene regulatory mechanisms. J Biol Chem. 2011;286:12640–9.
Cammarata PR, Chu S, Moor A, Wang Z, Yang S-H, Simpkins JW. Subcellular distribution of native estrogen receptor [alpha] and [beta] subtypes in cultured human lens epithelial cells. Exp Eye Res. 2004;78:861–71.
Capobianco E. RNA-Seq data: a complexity journey. Comput Struct Biotechnol J. 2014;11:123–30.
Carroll JS, Brown M. Estrogen receptor target gene: an evolving concept. Mol Endocrinol. 2006;20:1707–14.
Carroll JS, Liu XS, Brodsky AS, Li W, Meyer CA, Szary AJ, Eeckhoute J, Shao W, Hestermann EV, Geistlinger TR, Fox EA, Silver PA, Brown M. Chromosome-wide mapping of estrogen receptor binding reveals long-range regulation requiring the forkhead protein FoxA1. Cell. 2005;122:33–43.
Carroll JS, Meyer CA, Song J, Li W, Geistlinger TR, Eeckhoute J, Brodsky AS, Keeton EK, Fertuck KC, Hall GF, Wang Q, Bekiranov S, Sementchenko V, Fox EA, Silver PA, Gingeras TR, Liu XS, Brown M. Genome-wide analysis of estrogen receptor binding sites. Nat Genet. 2006;38:1289–97.
Carruthers CW, Suh JH, Gustafsson J-A, Webb P. Phosphorylation of glucocorticoid receptor tau1c transactivation domain enhances binding to CREB binding protein (CBP) TAZ2. Biochem Biophys Res Commun. 2015;457:119–23.
Cattin AL, Le Beyec J, Barreau F, Saint-Just S, Houllier A, Gonzalez FJ, Robine S, Pincon-Raymond M, Cardot P, Lacasa M, Ribeiro A. Hepatocyte nuclear factor 4alpha, a key factor for homeostasis, cell architecture, and barrier function of the adult intestinal epithelium. Mol Cell Biol. 2009;29:6294–308.
Chai X, Zeng S, Xie W. Nuclear receptors PXR and CAR: implications for drug metabolism regulation, pharmacogenomics and beyond. Expert Opin Drug Metab Toxicol. 2013;9:253–66.
Chambliss KL, Wu Q, Oltmann S, Konaniah ES, Umetani M, Korach KS, Thomas GD, Mineo C, Yuhanna IS, Kim SH, Madak-Erdogan Z, Maggi A, Dineen SP, Roland CL, Hui DY, Brekken RA, Katzenellenbogen JA, Katzenellenbogen BS, Shaul PW. Non-nuclear estrogen receptor alpha signaling promotes cardiovascular protection but not uterine or breast cancer growth in mice. J Clin Invest. 2010;120:2319–30.
Chandran UR, Attardi B, Friedman R, Zheng ZW, Roberts JL, DeFranco DB. Glucocorticoid repression of the mouse gonadotropin-releasing hormone gene is mediated by promoter elements that are recognized by heteromeric complexes containing glucocorticoid receptor. J Biol Chem. 1996;271:20412–20.
Chang C, Lee SO, Wang R-S, Yeh S, Chang T-M. Androgen receptor (AR) physiological roles in male and female reproductive systems: lessons learned from AR-knockout mice lacking AR in selective cells. Biol Reprod. 2013;89(21):1–16.
Chappell PE, Lydon JP, Conneely OM, O’Malley BW, Levine JE. Endocrine defects in mice carrying a null mutation for the progesterone receptor gene. Endocrinology. 1997;138:4147–52.
Charn TH, Liu ET-B, Chang EC, Lee YK, Katzenellenbogen JA, Katzenellenbogen BS. Genome-wide dynamics of chromatin binding of estrogen receptors {alpha} and {beta}: mutual restriction and competitive site selection. Mol Endocrinol. 2010;24:47–59.
Cheng S-Y, Leonard JL, Davis PJ. Molecular aspects of thyroid hormone actions. Endocr Rev. 2010;31:139–70.
Cherian MT, Chai SC, Chen T. Small-molecule modulators of the constitutive androstane receptor. Expert Opin Drug Metab Toxicol. 2015;11:1099–114.
Cheskis BJ. Regulation of cell signalling cascades by steroid hormones. J Cell Biochem. 2004;93:20–7.
Cheung E, Acevedo ML, Cole PA, Kraus WL. Altered pharmacology and distinct coactivator usage for estrogen receptor-dependent transcription through activating protein-1. Proc Natl Acad Sci U S A. 2005;102:559–64.
Chiang JY. Bile acid regulation of gene expression: roles of nuclear hormone receptors. Endocr Rev. 2002;23:443–63.
Chinenov Y, Gupte R, Rogatsky I. Nuclear receptors in inflammation control: repression by GR and beyond. Mol Cell Endocrinol. 2013;380:55–64.
Cho E, Montgomery RB, Mostaghel EA. Minireview: SLCO and ABC transporters: a role for steroid transport in prostate cancer progression. Endocrinology. 2014;155:4124–32.
Chodankar R, Wu DY, Schiller BJ, Yamamoto KR, Stallcup MR. Hic-5 is a transcription coregulator that acts before and/or after glucocorticoid receptor genome occupancy in a gene-selective manner. Proc Natl Acad Sci U S A. 2014;111:4007–12.
Chodankar R, Wu DY, Gerke DS, Stallcup MR. Selective coregulator function and restriction of steroid receptor chromatin occupancy by Hic-5. Mol Endocrinol. 2015;29:716–29.
Christakos S, Dhawan P, Verstuyf A, Verlinden L, Carmeliet G. Vitamin D: metabolism, molecular mechanism of action, and pleiotropic effects. Physiol Rev. 2016;96:365–408.
Chu S, Nishi Y, Yanase T, Nawata H, Fuller PJ. Transrepression of estrogen receptor {beta} signaling by nuclear factor-{kappa}B in ovarian granulosa cells. Mol Endocrinol. 2004;18:1919–28.
Clemens JW, Robker RL, Kraus WL, Katzenellenbogen BS, Richards JS. Hormone induction of progesterone receptor (PR) messenger ribonucleic acid and activation of PR promoter regions in ovarian granulosa cells: evidence for a role of cyclic adenosine 3′,5′-monophosphate but not estradiol. Mol Endocrinol. 1998;12:1201–14.
Coelho MB, Attig J, Ule J, Smith CWJ. Matrin3: connecting gene expression with the nuclear matrix. Wiley Interdiscip Rev: RNA. 2016. doi:10.1002/wrna.1336,n/a-n/a.
Cole TJ, Blendy JA, Schmid W, Strahle U, Schutz G. Expression of the mouse glucocorticoid receptor and its role during development. J Steroid Biochem Mol Biol. 1993;47:49–53.
Cook DN, Kang HS, Jetten AM. Retinoic acid-related orphan receptors (RORs): regulatory functions in immunity, development, circadian rhythm, and metabolism. Nucl Recept Res. 2015;2:2314.
Cooney AJ, Lee CT, Lin SC, Tsai SY, Tsai MJ. Physiological function of the orphans GCNF and COUP-TF. Trends Endocrinol Metab. 2001;12:247–51.
Couse JF, Korach KS. Exploring the role of sex steroids through studies of receptor deficient mice. J Mol Med. 1998;75:497–511.
Couse JF, Korach KS. Estrogen receptor null mice: what have we learned and where will they lead us? Endocr Rev. 1999;20:358–417.
Couse JF, Curtis SW, Washburn TF, Lindzey J, Golding TS, Lubahn DB, Smithies O, Korach KS. Analysis of transcription and estrogen insensitivity in the female mouse after targeted disruption of the estrogen receptor gene. Mol Endocrinol. 1995;9:1441–54.
Couse JF, Curtis Hewitt S, Korach KS. Receptor null mice reveal contrasting roles for estrogen receptor alpha and beta in reproductive tissues. J Steroid Biochem Mol Biol. 2000;74:287–96.
Cruz-Topete D, Cidlowski JA. One hormone, two actions: anti- and pro-inflammatory effects of glucocorticoids. Neuroimmunomodulation. 2015;22:20–32.
Dallas PB, Cheney IW, Liao D-W, Bowrin V, Byam W, Pacchione S, Kobayashi R, Yaciuk P, Moran E. p300/CREB binding protein-related protein p270 is a component of mammalian SWI/SNF complexes. Mol Cell Biol. 1998;18:3596–603.
Daniel AR, Gaviglio AL, Knutson TP, Ostrander JH, D’Assoro AB, Ravindranathan P, Peng Y, Raj GV, Yee D, Lange CA. Progesterone receptor-B enhances estrogen responsiveness of breast cancer cells via scaffolding PELP1- and estrogen receptor-containing transcription complexes. Oncogene. 2015;34:506–15.
Danielian PS, White R, Lees JA, Parker MG. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 1992;11:1025–33.
Danzo BJ, Joseph DR. Structure-function relationships of rat androgen – binding protein/human sex-hormone binding globulin: the effect of mutagenesis on steroid- binding parameters. Endocrinology. 1994;135:157–67.
Dasgupta S, Lonard DM, O’Malley BW. Nuclear receptor coactivators: master regulators of human health and disease. Annu Rev Med. 2014;65:279–92.
Davies MPA, O’Neill PA, Innes H, Sibson DR, Prime W, Holcombe C, Foster CS. Correlation of mRNA for oestrogen receptor beta splice variants ER{beta}1, ER{beta}2/ER{beta}cx and ER{beta}5 with outcome in endocrine-treated breast cancer. J Mol Endocrinol. 2004;33:773–82.
De Amicis F, Zupo S, Panno ML, Malivindi R, Giordano F, Barone I, Mauro L, Fuqua SAW, Ando S. Progesterone receptor B recruits a repressor complex to a half-pre site of the estrogen receptor {alpha} gene promoter. Mol Endocrinol. 2009;23:454–65.
De Martino MU, Bhattachryya N, Alesci S, Ichijo T, Chrousos GP, Kino T. The glucocorticoid receptor and the orphan nuclear receptor chicken ovalbumin upstream promoter-transcription factor II interact with and mutually affect each other’s transcriptional activities: implications for intermediary metabolism. Mol Endocrinol. 2004;18:820–33.
Deblois G, Giguere V. Functional and physiological genomics of estrogen-related receptors (ERRs) in health and disease. Biochim Biophys Acta. 2011;1812:1032–40.
Deblois G, St-Pierre J, Giguere V. The PGC-1/ERR signaling axis in cancer. Oncogene. 2013;32:3483–90.
DeFranco DB. Subnuclear trafficking of steroid receptors. Biochem Soc Trans. 1997;25:592–7.
DeLuca HF, Zierold C. Mechanisms and functions of vitamin D. Nutr Rev. 1998;56:S4–10. discussion S 54–75.
Demonacos CV, Karayanni N, Hatzoglou E, Tsiriyiotis C, Spandidos DA, Sekeris CE. Mitochondrial genes as sites of primary action of steroid hormones. Steroids. 1996;61:226–32.
Dey P, Barros RPA, Warner M, Ström A, Gustafsson J-Å. Insight into the mechanisms of action of estrogen receptor β in the breast, prostate, colon, and CNS. J Mol Endocrinol. 2013;51:T61–74.
Diamond MI, Miner JN, Yoshinaga SK, Yamamoto KR. Transcription factor interactions: selectors of positive or negative regulation from a single DNA element. Science. 1990;249:1266–72.
Dickmeis T, Weger BD, Weger M. The circadian clock and glucocorticoids – interactions across many time scales. Mol Cell Endocrinol. 2013;380:2–15.
Ding XF, Anderson CM, Ma H, Hong H, Uht RM, Kushner PJ, Stallcup MR. Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): multiple motifs with different binding specificities. Mol Endocrinol. 1998;12:302–13.
Dittmar KD, Demady DR, Stancato LF, Krishna P, Pratt WB. Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery: the role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70. J Biol Chem. 1997;272:21213–20.
Djebali S, Davis CA, Merkel A, Dobin A, Lassmann T, Mortazavi A, Tanzer A, Lagarde J, Lin W, Schlesinger F, Xue C, Marinov GK, Khatun J, Williams BA, Zaleski C, Rozowsky J, Roder M, Kokocinski F, Abdelhamid RF, Alioto T, Antoshechkin I, Baer MT, Bar NS, Batut P, Bell K, Bell I, Chakrabortty S, Chen X, Chrast J, Curado J, Derrien T, Drenkow J, Dumais E, Dumais J, Duttagupta R, Falconnet E, Fastuca M, Fejes-Toth K, Ferreira P, Foissac S, Fullwood MJ, Gao H, Gonzalez D, Gordon A, Gunawardena H, Howald C, Jha S, Johnson R, Kapranov P, King B, Kingswood C, Luo OJ, Park E, Persaud K, Preall JB, Ribeca P, Risk B, Robyr D, Sammeth M, Schaffer L, See L-H, Shahab A, Skancke J, Suzuki AM, Takahashi H, Tilgner H, Trout D, Walters N, Wang H, Wrobel J, Yu Y, Ruan X, Hayashizaki Y, Harrow J, Gerstein M, Hubbard T, Reymond A, Antonarakis SE, Hannon G, Giddings MC, Ruan Y, Wold B, Carninci P, Guigo R, Gingeras TR. Landscape of transcription in human cells. Nature. 2012;489:101–8.
Dooley R, Harvey BJ, Thomas W. Non-genomic actions of aldosterone: from receptors and signals to membrane targets. Mol Cell Endocrinol. 2012;350:223–34.
Drewes T, Senkel S, Holewa B, Ryffel GU. Human hepatocyte nuclear factor 4 isoforms are encoded by distinct and differentially expressed genes. Mol Cell Biol. 1996;16:925–31.
Driscoll MD, Klinge CM, Hilf R, Bambara RA. Footprint analysis of estrogen receptor binding to adjacent estrogen response elements. J Steroid Biochem Mol Biol. 1996;58:45–61.
Driscoll MD, Sathya G, Muyan M, Klinge CM, Hilf R, Bambara RA. Sequence requirements for estrogen receptor binding to estrogen response elements. J Biol Chem. 1998;273:29321–30.
Drouin J, Sun YL, Chamberland M, Gauthier Y, De Lean A, Nemer M, Schmidt TJ. Novel glucocorticoid receptor complex with DNA element of the hormone- repressed POMC gene. EMBO J. 1993;12:145–56.
Duan R, Porter W, Safe S. Estrogen-induced c-fos protooncogene expression in MCF-7 human breast cancer cells: role of estrogen receptor Sp1 complex formation. Endocrinology. 1998;139:1981–90.
Durand B, Saunders M, Gaudon C, Roy B, Losson R, Chambon P. Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity. EMBO J. 1994;13:5370–82.
Eeckhoute J, Carroll JS, Geistlinger TR, Torres-Arzayus MI, Brown M. A cell-type-specific transcriptional network required for estrogen regulation of cyclin D1 and cell cycle progression in breast cancer. Genes Dev. 2006;20:2513–26.
Eeckhoute J, Keeton EK, Lupien M, Krum SA, Carroll JS, Brown M. Positive cross-regulatory loop ties GATA-3 to estrogen receptor {alpha} expression in breast cancer. Cancer Res. 2007;67:6477–83.
Elbi C, Walker DA, Romero G, Sullivan WP, Toft DO, Hager GL, DeFranco DB. Molecular chaperones function as steroid receptor nuclear mobility factors. Proc Natl Acad Sci U S A. 2004;101:2876–81.
Eng FCS, Barsalou A, Akutsu N, Mercier I, Zechel C, Made S, White JH. Different classes of coactivators recognize distinct but overlapping binding sites on the estrogen receptor ligand binding domain. J Biol Chem. 1998;273:28371–7.
Evans RM. The steroid and thyroid hormone receptor superfamily. Science. 1988;240:889–95.
Evans RM. The nuclear receptor superfamily: a rosetta stone for physiology. Mol Endocrinol. 2005;19:1429–38.
Evans RM, Mangelsdorf DJ. Nuclear receptors, RXR, and the Big Bang. Cell. 2014;157:255–66.
Fan W, Evans R. PPARs and ERRs: molecular mediators of mitochondrial metabolism. Curr Opin Cell Biol. 2015;33:49–54.
Feige JN, Auwerx J. Transcriptional coregulators in the control of energy homeostasis. Trends Cell Biol. 2007;17:292–301.
Feldman RD. Aldosterone and blood pressure regulation: recent milestones on the long and winding road from electrocortin to KCNJ5, GPER, and beyond. Hypertension. 2014;63:19–21.
Feldman RD, Gros R. Vascular effects of aldosterone: sorting out the receptors and the ligands. Clin Exp Pharmacol Physiol. 2013. doi:10.1111/1440-1681.12157,n/a-n/a.
Filardo EJ, Thomas P. Minireview: G protein-coupled estrogen receptor-1, GPER-1: its mechanism of action and role in female reproductive cancer, renal and vascular physiology. Endocrinology. 2012;153:2953–62.
Fischle W, Mootz HD, Schwarzer D. Synthetic histone code. Curr Opin Chem Biol. 2015;28:131–40.
Flototto T, Niederacher D, Hohmann D, Heimerzheim T, Dall P, Djahansouzi S, Bender HG, Hanstein B. Molecular mechanism of estrogen receptor (ER)[alpha]-specific, estradiol-dependent expression of the progesterone receptor (PR) B-isoform. J Steroid Biochem Mol Biol. 2004;88:131–42.
Freedman OC, Fletcher GG, Gandhi S, Mates M, Dent SF, Trudeau ME, Eisen A. Adjuvant endocrine therapy for early breast cancer: a systematic review of the evidence for the 2014 Cancer Care Ontario systemic therapy guideline. Curr Oncol (Toronto, Ont). 2015;22:S95–s113.
Fu M, Wang C, Zhang X, Pestell RG. Acetylation of nuclear receptors in cellular growth and apoptosis. Biochem Pharmacol. 2004;68:1199–208.
Fuller PJ. Novel interactions of the mineralocorticoid receptor. Mol Cell Endocrinol. 2015;408:33–7.
Funakoshi T, Yanai A, Shinoda K, Kawano MM, Mizukami Y. G protein-coupled receptor 30 is an estrogen receptor in the plasma membrane. Biochem Biophys Res Commun. 2006;346:904–10.
Galvani A, Thiriet C. Nucleosome dancing at the tempo of histone tail acetylation. Genes. 2015;6:607–21.
Gao T, McPhaul MJ. Functional activities of the A and B forms of the human androgen receptor in response to androgen receptor agonists and antagonists. Mol Endocrinol. 1998;12:654–63.
Gardner KE, Allis CD, Strahl BD. OPERating ON chromatin, a colorful language where context matters. J Mol Biol. 2011;409:36–46.
Gaudet HM, Cheng SB, Christensen EM, Filardo EJ. The G-protein-coupled estrogen receptor, GPER: the inside and inside-out story. Mol Cell Endocrinol. 2015;418:207–19.
Gehring U. Steroid hormone receptors and heat shock proteins. Vitam Horm. 1998;54:167–205.
Germain P, Staels B, Dacquet C, Spedding M, Laudet V. Overview of nomenclature of nuclear receptors. Pharmacol Rev. 2006;58:685–704.
Gertz J, Reddy TE, Varley KE, Garabedian MJ, Myers RM. Genistein and bisphenol A exposure cause estrogen receptor 1 to bind thousands of sites in a cell type-specific manner. Genome Res. 2012;22:2153–62.
Geserick C, Meyer H-A, Haendler B. The role of DNA response elements as allosteric modulators of steroid receptor function. Mol Cell Endocrinol. 2005;236:1–7.
Giguere V. Retinoic acid receptors and cellular retinoid binding proteins: complex interplay in retinoid signaling. Endocr Rev. 1994;15:61–79.
Giordano Attianese GM, Desvergne B. Integrative and systemic approaches for evaluating PPARbeta/delta (PPARD) function. Nucl Recept Signal. 2015;13, e001.
Girard BJ, Daniel AR, Lange CA, Ostrander JH. PELP1: a review of PELP1 interactions, signaling, and biology. Mol Cell Endocrinol. 2014;382:642–51.
Goodwin B, Jones SA, Price RR, Watson MA, McKee DD, Moore LB, Galardi C, Wilson JG, Lewis MC, Roth ME, Maloney PR, Willson TM, Kliewer SA. A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis. Mol Cell. 2000;6:517–26.
Gorski J, Williams D, Giannopoulos G, Stancel G. The continuing evolution of an estrogen-receptor model. Adv Exp Med Biol. 1973;36:1–14.
Goswami D, Callaway C, Pascal BD, Kumar R, Edwards DP, Griffin PR. Influence of domain interactions on conformational mobility of the progesterone receptor detected by hydrogen/deuterium exchange mass spectrometry. Structure. 2014;22:961–73.
Gottlicher M, Heck S, Herrlich P. Transcriptional cross-talk, the second mode of steroid hormone receptor action. J Mol Med. 1998;76:480–9.
Graber R, Sumida C, Vallette G, Nunez EA. Rapid and long-term effects of 17 beta-estradiol on PIP2-phospholipase C-specific activity of MCF-7 cells. Cell Signal. 1993;5:181–6.
Granner DK, Wang JC, Yamamoto KR. Regulatory actions of glucocorticoid hormones: from organisms to mechanisms. Adv Exp Med Biol. 2015;872:3–31.
Green S, Chambon P. Oestradiol induction of a glucocorticoid-responsive gene by a chimaeric receptor. Nature. 1987;325:75–8.
Green SM, Mostaghel EA, Nelson PS. Androgen action and metabolism in prostate cancer. Mol Cell Endocrinol. 2012;360:3–13.
Greenblatt J. RNA polymerase II holoenzyme and transcriptional regulation. Curr Opin Cell Biol. 1997;9:310–9.
Greger JG, Guo Y, Henderson R, Ross JF, Cheskis BJ. Characterization of MNAR expression. Steroids. 2006;71:317–22.
Greschik H, Jean-Marie Wurtz PH, Köhler F, Moras D, Schüle R. Characterization of the DNA-binding and dimerization properties of the nuclear orphan receptor germ cell nuclear factor. Mol Cell Biol. 1999;19:690–703.
Guennoun R, Labombarda F, Gonzalez Deniselle MC, Liere P, De Nicola AF, Schumacher M. Progesterone and allopregnanolone in the central nervous system: response to injury and implication for neuroprotection. J Steroid Biochem Mol Biol. 2015;146:48–61.
Guiochon-Mantel A, Delabre K, Lescop P, Milgrom E. Intracellular traffic of steroid hormone receptors. J Steroid Biochem Mol Biol. 1996;56:1–6.
Hah N, Kraus WL. Hormone-regulated transcriptomes: lessons learned from estrogen signaling pathways in breast cancer cells. Mol Cell Endocrinol. 2014;382:652–64.
Hamilton KJ, Arao Y, Korach KS. Estrogen hormone physiology: reproductive findings from estrogen receptor mutant mice. Reprod Biol. 2014;14:3–8.
Hammes A, Andreassen TK, Spoelgen R, Raila J, Hubner N, Schulz H, Metzger J, Schweigert FJ, Luppa PB, Nykjaer A, Willnow TE. Role of endocytosis in cellular uptake of sex steroids. Cell. 2005;122:751–62.
Hammond GL, Bocchinfuso WP. Sex hormone-binding globulin/androgen-binding protein: steroid-binding and dimerization domains. J Steroid Biochem Mol Biol. 1995;53:543–52.
Hawk JD, Bookout AL, Poplawski SG, Bridi M, Rao AJ, Sulewski ME, Kroener BT, Manglesdorf DJ, Abel T. NR4A nuclear receptors support memory enhancement by histone deacetylase inhibitors. J Clin Invest. 2012;122:3593–602.
Hawkins MB, Thomas P. The unusual binding properties of the third distinct teleost estrogen receptor subtype ERbetaa are accompanied by highly conserved amino acid changes in the ligand binding domain. Endocrinology. 2004;145:2968–77.
Hawkinson JE, Kimbrough CL, Belelli D, Lambert JJ, Purdy RH, Lan NC. Correlation of neuroactive steroid modulation of [35S]t- butylbicyclophosphorothionate and [3H]flunitrazepam binding and gamma aminobutyric acidA receptor function. Mol Pharmacol. 1994;46:977–85.
Heintzman ND, Hon GC, Hawkins RD, Kheradpour P, Stark A, Harp LF, Ye Z, Lee LK, Stuart RK, Ching CW, Ching KA, Antosiewicz-Bourget JE, Liu H, Zhang X, Green RD, Lobanenkov VV, Stewart R, Thomson JA, Crawford GE, Kellis M, Ren B. Histone modifications at human enhancers reflect global cell-type-specific gene expression. Nature. 2009;459:108–12.
Helsen C, Claessens F. Looking at nuclear receptors from a new angle. Mol Cell Endocrinol. 2014;382:97–106.
Herynk MH, Fuqua SAW. Estrogen receptor mutations in human disease. Endocr Rev. 2004;25:869–98.
Hewitt SC, Harrell JC, Korach KS. Lessons in estrogen biology from knockout and transgenic animals. Annu Rev Physiol. 2005;67:285–308.
Hirose T, O’Brien DA, Jetten AM. RTR: a new member of the nuclear receptor superfamily that is highly expressed in murine testis. Gene. 1995;152:247–51.
Hisamoto K, Bender JR. Vascular cell signaling by membrane estrogen receptors. Steroids. 2005;70:382–7.
Hollenberg SM, Evans RM. Multiple and cooperative trans-activation domains of the human glucocorticoid receptor. Cell. 1988;55:899–906.
Holmes KA, Hurtado A, Brown GD, Launchbury R, Ross-Innes CS, Hadfield J, Odom DT, Carroll JS. Transducin-like enhancer protein 1 mediates estrogen receptor binding and transcriptional activity in breast cancer cells. Proc Natl Acad Sci. 2012;109:2748–53.
Horwitz KB, McGuire WL. Nuclear mechanisms of estrogen action. Effects of estradiol and anti- estrogens on estrogen receptors and nuclear receptor processing. J Biol Chem. 1978;253:8185–91.
Hua G, Paulen L, Chambon P. GR SUMOylation and formation of an SUMO-SMRT/NCoR1-HDAC3 repressing complex is mandatory for GC-induced IR nGRE-mediated transrepression. Proc Natl Acad Sci. 2016;113:E626–34.
Huang EY, Zhang J, Miska EA, Guenther MG, Kouzarides T, Lazar MA. Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev. 2000;14:45–54.
Huang B, Warner M, Gustafsson J-Å. Estrogen receptors in breast carcinogenesis and endocrine therapy. Mol Cell Endocrinol. 2015;418:240–4. Part 3.
Hubert C, Gasc J-M, Berger S, Günther Schütz G, Corvol P. Effects of mineralocorticoid receptor gene disruption on the components of the renin-angiotensin system in 8-day-old mice. Mol Endocrinol. 1999;13:297–306.
Hübner MR, Eckersley-Maslin MA, Spector DL. Chromatin organization and transcriptional regulation. Curr Opin Genet Dev. 2013;23:89–95.
Husmann DA, Wilson CM, McPhaul MJ, Tilley WD, Wilson JD. Antipeptide antibodies to two distinct regions of the androgen receptor localize the receptor protein to the nuclei of target cells in the rat and human prostate. Endocrinology. 1990;126:2359–68.
Huss JM, Garbacz WG, Xie W. Constitutive activities of estrogen-related receptors: transcriptional regulation of metabolism by the ERR pathways in health and disease. Biochim Biophys Acta. 2015;1852:1912–27.
Hutchison KA, Dittmar KD, Stancato LF, Pratt WB. Ability of various members of the hsp70 family of chaperones to promote assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90. J Steroid Biochem Mol Biol. 1996;58:251–8.
Improta-Brears T, Whorton AR, Codazzi F, York JD, Meyer T, McDonnell DP. Estrogen-induced activation of mitogen-activated protein kinase requires mobilization of intracellular calcium. Proc Natl Acad Sci U S A. 1999;96:4686–91.
Islam MM, Zhang C-L. TLX: a master regulator for neural stem cell maintenance and neurogenesis. Biochim Biophys Acta (BBA) – Gene Regul Mech. 2015;1849:210–6.
Iwafuchi-Doi M, Zaret KS. Pioneer transcription factors in cell reprogramming. Genes Dev. 2014;28:2679–92.
Jackson TA, Richer JK, Bain DL, Takimoto GS, Tung I, Horwitz KB. The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and the corepressors N-CoR or SMRT. Mol Endocrinol. 1997;11:693–705.
Jacobsen BM, Horwitz KB. Progesterone receptors, their isoforms and progesterone regulated transcription. Mol Cell Endocrinol. 2012;357:18–29.
Jadhav U, Harris RM, Jameson JL. Hypogonadotropic hypogonadism in subjects with DAX1 mutations. Mol Cell Endocrinol. 2011;346:65–73.
Jaisser F, Farman N. Emerging roles of the mineralocorticoid receptor in pathology: toward new paradigms in clinical pharmacology. Pharmacol Rev. 2016;68:49–75.
Jantzen HM, Strahle U, Gloss B, Stewart F, Schmid W, Boshart M, Miksicek R, Schutz G. Cooperativity of glucocorticoid response elements located far upstream of the tyrosine aminotransferase gene. Cell. 1987;49:29–38.
Jensen EV, DeSombre ER. Estrogen-receptor interaction. Science. 1973;182:126–34.
Jiang C, Xie C, Li F, Zhang L, Nichols RG, Krausz KW, Cai J, Qi Y, Fang ZZ, Takahashi S, Tanaka N, Desai D, Amin SG, Albert I, Patterson AD, Gonzalez FJ. Intestinal farnesoid X receptor signaling promotes nonalcoholic fatty liver disease. J Clin Invest. 2014. doi:10.1172/jci76738.
Josefsberg Ben-Yehoshua L, Lewellyn AL, Thomas P, Maller JL. The role of xenopus membrane progesterone receptor {beta} in mediating the effect of progesterone on oocyte maturation. Mol Endocrinol. 2007;21:664–73.
Joseph DR. Structure, function, and regulation of androgen-binding protein/sex hormone-binding globulin. Vitam Horm. 1994;49:197–280.
Kadiyala V, Sasse SK, Altonsy MO, Berman R, Chu HW, Phang TL, Gerber AN. Cistrome-based cooperation between airway epithelial glucocorticoid receptor and nf-kappab orchestrates anti-inflammatory effects. J Biol Chem. 2016a. doi:10.1074/jbc.M116.721217.
Kadiyala V, Sasse SK, Altonsy MO, Phang TL, Gerber AN. Cistrome analysis of glucocorticoid receptor activity in bronchial epithelial cells defines novel mechanisms of steroid efficacy. Ann Am Thorac Soc. 2016b;13 Suppl 1:S103.
Kastner P, Krust A, Turcotte B, Stropp U, Tora L, Gronemeyer H, Chambon P. Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B. EMBO J. 1990;9:1603–14.
Khan SH, Awasthi S, Guo C, Goswami D, Ling J, Griffin PR, Simons Jr SS, Kumar R. Binding of the N-terminal region of coactivator TIF2 to the intrinsically disordered AF1 domain of the glucocorticoid receptor is accompanied by conformational reorganizations. J Biol Chem. 2012;287:44546–60.
Kim KH, Bender JR. Rapid, estrogen receptor-mediated signaling: why is the endothelium so special? Sci STKE. 2005;2005:pe28.
Kim KH, Young BD, Bender JR. Endothelial estrogen receptor isoforms and cardiovascular disease. Mol Cell Endocrinol. 2014;389:65–70.
King WJ, Greene GL. Monoclonal antibodies localize oestrogen receptor in the nuclei of target cells. Nature. 1984;307:745–7.
Kininis M, Chen BS, Diehl AG, Isaacs GD, Zhang T, Siepel AC, Clark AG, Kraus WL. Genomic analyses of transcription factor binding, histone acetylation, and gene expression reveal mechanistically distinct classes of estrogen-regulated promoters. Mol Cell Biol. 2007;27:5090–104.
Kinyamu HK, Fryer CJ, Horwitz KB, Archer TK. The mouse mammary tumor virus promoter adopts distinct chromatin structures in human breast cancer cells with and without glucocorticoid receptor. J Biol Chem. 2000;275:20061–8.
Klein-Hitpass L, Ryffel GU, Heitlinger E, Cato AC. A 13 bp palindrome is a functional estrogen responsive element and interacts specifically with estrogen receptor. Nucleic Acids Res. 1988;16:647–63.
Klinge CM. Estrogen receptor interaction with estrogen response elements. Nucleic Acids Res. 2001;29:2905–19.
Klinge CM, Bambara RA, Hilf R. Antiestrogen-liganded estrogen receptor interaction with estrogen responsive element DNA in vitro. J Steroid Biochem Mol Biol. 1992a;43:249–62.
Klinge CM, Peale Jr FV, Hilf R, Bambara RA, Zain S. Cooperative estrogen receptor interaction with consensus or variant estrogen responsive elements in vitro. Cancer Res. 1992b;52:1073–81.
Klinge CM, Jernigan SC, Mattingly KA, Risinger KE, Zhang J. Estrogen response element-dependent regulation of transcriptional activation of estrogen receptors alpha and beta by coactivators and corepressors. J Mol Endocrinol. 2004;33:387–410.
Klock G, Strahle U, Schutz G. Oestrogen and glucocorticoid responsive elements are closely related but distinct. Nature. 1987;329:734–6.
Klug A, Schwabe JWR. Zinc fingers. FASEB J. 1995;9:597–604.
Knutson TP, Lange CA. Tracking progesterone receptor-mediated actions in breast cancer. Pharmacol Ther. 2014;142:114–25.
Kobayashi K, Hashimoto M, Honkakoski P, Negishi M. Regulation of gene expression by CAR: an update. Arch Toxicol. 2015;89:1045–55.
Kojetin DJ, Burris TP. REV-ERB and ROR nuclear receptors as drug targets. Nat Rev Drug Discov. 2014;13:197–216.
Korach KS, Emmen JMA, Walker VR, Hewitt SC, Yates M, Hall JM, Swope DL, Harrell JC, Couse JF. Update on animal models developed for analyses of estrogen receptor biological activity. J Steroid Biochem Mol Biol. 2003;86:387–91.
Koukouritaki SB, Margioris AN, Gravanis A, Hartig R, Stournaras C. Dexamethasone induces rapid actin assembly in human endometrial cells without affecting its synthesis. J Cell Biochem. 1997;65:492–500.
Kowalik MK, Rekawiecki R, Kotwica J. The putative roles of nuclear and membrane-bound progesterone receptors in the female reproductive tract. Reprod Biol. 2013;13:279–89.
Krishnan V, Wang X, Safe S. Estrogen receptor-SP1 complexes mediate estrogen-induced cathepsin D gene expression in MCF-7 human breast cancer cells. J Biol Chem. 1994;269:15912–7.
Kuiper GG, Enmark E, Pelto-Huikko M, Nilsson S, Gustafsson J-A. Cloning of a novel estrogen receptor expressed in rat prostate and ovary. Proc Natl Acad Sci U S A. 1996;93:5925–30.
Kuiper GG, Carlsson B, Grandien J, Enmark E, Haggblad J, Nilsson S, Gustafsson J-A. Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors α and β. Endocrinology. 1997;138:863–70.
Kurakula K, Koenis DS, van Tiel CM, de Vries CJM. NR4A nuclear receptors are orphans but not lonesome. Biochim Biophys Acta (BBA) – Mol Cell Res. 2014;1843:2543–55.
Kuznetsova T, Wang SY, Rao NA, Mandoli A, Martens JH, Rother N, Aartse A, Groh L, Janssen-Megens EM, Li G, Ruan Y, Logie C, Stunnenberg HG. Glucocorticoid receptor and nuclear factor kappa-b affect three-dimensional chromatin organization. Genome Biol. 2015;16:264.
Kwon Y-S, Garcia-Bassets I, Hutt KR, Cheng CS, Jin M, Liu D, Benner C, Wang D, Ye Z, Bibikova M, Fan J-B, Duan L, Glass CK, Rosenfeld MG, Fu X-D. Sensitive ChIP-DSL technology reveals an extensive estrogen receptor {alpha}-binding program on human gene promoters. Proc Natl Acad Sci U S A. 2007;104:4852–7.
Lam MTY, Li W, Rosenfeld MG, Glass CK. Enhancer RNAs and regulated transcriptional programs. Trends Biochem Sci. 2014;39:170–82.
Lange CA. Integration of progesterone receptor action with rapid signaling events in breast cancer models. J Steroid Biochem Mol Biol. 2008;108:203–12.
Lannigan DA. Estrogen receptor phosphorylation. Steroids. 2003;68:1–9.
Laudet V. Evolution of the nuclear receptor superfamily: early diversification from an ancestral orphan receptor. J Mol Endocrinol. 1997;19:207–26.
Le Billan F, Khan JA, Lamribet K, Viengchareun S, Bouligand J, Fagart J, Lombès M. Cistrome of the aldosterone-activated mineralocorticoid receptor in human renal cells. FASEB J. 2015;29:3977–89.
Le Menuet D, Lombès M. The neuronal mineralocorticoid receptor: from cell survival to neurogenesis. Steroids. 2014;91:11–9.
Le Romancer M, Poulard C, Cohen P, Sentis S, Renoir JM, Corbo L. Cracking the estrogen receptor’s posttranslational code in breast tumors. Endocr Rev. 2011;32:597–622.
Le TN, Nestler JE, Strauss Iii JF, Wickham Iii EP. Sex hormone-binding globulin and type 2 diabetes mellitus. Trends Endocrinol Metab. 2012;23:32–40.
Lee WS, Kim J. Peroxisome proliferator-activated receptors and the heart: lessons from the past and future directions. PPAR Res. 2015;2015:271983.
Lee S-O, Jin U-H, Kang JH, Kim SB, Guthrie AS, Sreevalsan S, Lee J-S, Safe S. The orphan nuclear receptor NR4A1 (Nur77) regulates oxidative and endoplasmic reticulum stress in pancreatic cancer cells. Mol Cancer Res. 2014;12:527–38.
Lefebvre P, Benomar Y, Staels B. Retinoid X receptors: common heterodimerization partners with distinct functions. Trends Endocrinol Metab. 2010;21:676–83.
Leid M, Kastner P, Lyons R, Nakshatri H, Saunders M, Zacharewski T, Chen JY, Staub A, Garnier JM, Mader S, et al. Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently. Cell. 1992;68:377–95.
Levin ER. Extranuclear steroid receptors are essential for steroid hormone actions. Annu Rev Med. 2015;66:271–80.
Li L, Haynes MP, Bender JR. Plasma membrane localization and function of the estrogen receptor alpha variant (ER46) in human endothelial cells. Proc Natl Acad Sci U S A. 2003;100:4807–12.
Li W, Notani D, Ma Q, Tanasa B, Nunez E, Chen AY, Merkurjev D, Zhang J, Ohgi K, Song X, Oh S, Kim HS, Glass CK, Rosenfeld MG. Functional roles of enhancer RNAs for oestrogen-dependent transcriptional activation. Nature. 2013;498:516–20.
Lin CY, Vega VB, Thomsen JS, Zhang T, Kong SL, Xie M, Chiu KP, Lipovich L, Barnett DH, Stossi F, Yeo A, George J, Kuznetsov VA, Lee YK, Charn TH, Palanisamy N, Miller LD, Cheung E, Katzenellenbogen BS, Ruan Y, Bourque G, Wei CL, Liu ET. Whole-genome cartography of estrogen receptor alpha binding sites. PLoS Genet. 2007;3, e87.
Lin F-J, Qin J, Tang K, Tsai SY, Tsai M-J. Coup d’Etat: an orphan takes control. Endocr Rev. 2011. doi:10.1210/er.2010-0021,er.2010-0021.
Litchfield LM, Riggs KA, Hockenberry AM, Oliver LD, Barnhart KG, Cai J, Pierce Jr WM, Ivanova MM, Bates PJ, Appana SN, Datta S, Kulesza P, McBryan J, Young LS, Klinge CM. Identification and characterization of nucleolin as a COUP-TFII coactivator of retinoic acid receptor β transcription in breast cancer cells. PLoS One. 2012;7, e38278.
Liu Y, Gao H, Marstrand TT, Strom A, Valen E, Sandelin A, Gustafsson J-A, Dahlman-Wright K. The genome landscape of ER{alpha}- and ER{beta}-binding DNA regions. Proc Natl Acad Sci. 2008. doi:10.1073/pnas.0712085105,0712085105.
Lu NZ, Cidlowski JA. The origin and functions of multiple human glucocorticoid receptor isoforms. Ann N Y Acad Sci. 2004;1024:102–23.
Lubahn DB, Moyer JS, Golding TS, Couse JF, Korach KS, Smithies O. Alteration of reproductive function but not prenatal sexual development after insertional disruption of the mouse estrogen receptor gene. Proc Natl Acad Sci U S A. 1993;90:11162–6.
Lupien M, Eeckhoute J, Meyer CA, Wang Q, Zhang Y, Li W, Carroll JS, Liu XS, Brown M. FoxA1 translates epigenetic signatures into enhancer-driven lineage-specific transcription. Cell. 2008;132:958–70.
Lydon JP, Edwards DP. Finally! A model for progesterone receptor action in normal human breast. Endocrinology. 2009;150:2988–90.
Lydon JP, DeMayo FJ, Funk CR, Mani SK, Hughes AR, Montgomery CAJ, Shyamala G, Conneely OM, O’Malley BW. Mice lacking progesterone receptor exhibit pleiotropic reproductive abnormalities. Genes Dev. 1995;9:2266–78.
Ma X, Chen J, Tian Y. Pregnane X receptor as the “sensor and effector” in regulating epigenome. J Cell Physiol. 2015;230:752–7.
Magnani L, Lupien M. Chromatin and epigenetic determinants of estrogen receptor alpha (ESR1) signaling. Mol Cell Endocrinol. 2014;382:633–41.
Maller JL. Signal transduction. Fishing at the cell surface. Science. 2003;300:594–5.
Mangelsdorf DJ, Evans RM. The RXR heterodimers and orphan receptors. Cell. 1995;83:841–50.
Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM. Nuclear receptor that identifies a novel retinoic acid response pathway. Nature. 1990;345:224–9.
Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RM. The nuclear receptor superfamily: the second decade. Cell. 1995;83:835–9.
Maroder M, Farina AR, Vacca A, Felli MP, Meco D, Screpanti I, Frati L, Gulino A. Cell-specific bifunctional role of Jun oncogene family members on glucocorticoid receptor-dependent transcription. Mol Endocrinol. 1993;7:570–84.
Marrone AK, Beland FA, Pogribny IP. Noncoding RNA response to xenobiotic exposure: an indicator of toxicity and carcinogenicity. Expert Opin Drug Metab Toxicol. 2014: 1–14 doi: 10.1517/17425255.2014.954312
Mathisen GH, Fallgren ÅB, Strøm BO, Boldingh Debernard KA, Mohebi BU, Paulsen RE. Delayed translocation of NGFI–B/RXR in glutamate stimulated neurons allows late protection by 9-cis retinoic acid. Biochem Biophys Res Commun. 2011;414:90–5.
Matsuda K, Ochiai I, Nishi M, Kawata M. Colocalization and ligand-dependent discrete distribution of the estrogen receptor (ER)alpha and ERbeta. Mol Endocrinol. 2002;16:2215–30.
Mazur EC, Vasquez YM, Li X, Kommagani R, Jiang L, Chen R, Lanz RB, Kovanci E, Gibbons WE, DeMayo FJ. Progesterone receptor transcriptome and cistrome in decidualized human endometrial stromal cells. Endocrinology. 2015;156:2239–53.
McCabe ERB. DAX1: increasing complexity in the roles of this novel nuclear receptor. Mol Cell Endocrinol. 2007;265–266:179–82.
McFall T, Patki M, Rosati R, Ratnam M. Role of the short isoform of the progesterone receptor in breast cancer cell invasiveness at estrogen and progesterone levels in the pre- and post-menopausal ranges. Oncotarget. 2015;6:33146–64.
McGuire WL, Clark GM, Dressler LG, Owens MA. Role of steroid hormone receptors as prognostic factors in primary breast cancer. NCI Monogr. 1986;1986:19–23.
McIntyre WR, Samuels HH. Triamcinolone acetonide regulates glucocorticoid-receptor levels by decreasing the half-life of the activated nuclear-receptor form. J Biol Chem. 1985;260:418–27.
Meijsing SH. Mechanisms of glucocorticoid-regulated gene transcription. Adv Exp Med Biol. 2015;872:59–81.
Metivier R, Penot G, Flouriot G, Pakdel F. Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains. Mol Endocrinol. 2001;15:1953–70.
Meyer ME, Gronemeyer H, Turcotte B, Bocquel MT, Tasset D, Chambon P. Steroid hormone receptors compete for factors that mediate their enhancer function. Cell. 1989;57:433–42.
Michalek RD, Gerriets VA, Nichols AG, Inoue M, Kazmin D, Chang C-Y, Dwyer MA, Nelson ER, Pollizzi KN, Ilkayeva O, Giguere V, Zuercher WJ, Powell JD, Shinohara ML, McDonnell DP, Rathmell JC. Estrogen-related receptor-α is a metabolic regulator of effector T-cell activation and differentiation. Proc Natl Acad Sci. 2011;108:18348–53.
Migliaccio A, Castoria G, Auricchio F. Analysis of androgen receptor rapid actions in cellular signaling pathways: receptor/Src association. Methods Mol Biol. 2011;776:361–70.
Mikkonen L, Pihlajamaa P, Sahu B, Zhang F-P, Jänne OA. Androgen receptor and androgen-dependent gene expression in lung. Mol Cell Endocrinol. 2010;317:14–24.
Mizutani T, Kawabe S, Ishikane S, Imamichi Y, Umezawa A, Miyamoto K. Identification of novel steroidogenic factor 1 (SF-1)-target genes and components of the SF-1 nuclear complex. Mol Cell Endocrinol. 2015;408:133–7.
Mohan HM, Aherne CM, Rogers AC, Baird AW, Winter DC, Murphy EP. Molecular pathways: the role of nr4a orphan nuclear receptors in cancer. Clin Cancer Res. 2012;18:3223–8.
Monroe DG, Secreto FJ, Subramaniam M, Getz BJ, Khosla S, Spelsberg TC. Estrogen receptor {alpha} and {beta} heterodimers exert unique effects on estrogen- and tamoxifen-dependent gene expression in human U2OS osteosarcoma cells. Mol Endocrinol. 2005;19:1555–68.
Moriarty K, Kim KH, Bender JR. Estrogen receptor-mediated rapid signaling. Endocrinology. 2006;147:5557–63.
Morrill GA, Kostellow AB, Gupta RK. Transmembrane helices in “classical” nuclear reproductive steroid receptors: a perspective. Nucl Recept Signal. 2015;13, e003.
Mosselman S, Polman J, Dijkrms R. ERb: identification and characterization of a novel human estrogen receptor. FEBS Lett. 1996;392:49–53.
Mullican SE, DiSpirito JR, Lazar MA. The orphan nuclear receptors at their 25-year reunion. J Mol Endocrinol. 2013;51:T115–40.
Musatov S, Chen W, Pfaff DW, Mobbs CV, Yang X-J, Clegg DJ, Kaplitt MG, Ogawa S. Silencing of estrogen receptor {alpha} in the ventromedial nucleus of hypothalamus leads to metabolic syndrome. Proc Natl Acad Sci U S A. 2007;104:2501–6.
Muscatelli F, Strom TM, Walker AP, Zanaria E, Recan D, Meindl A, Bardoni B, Guioli S, Zehetner G, Rabl W, Schwara HP, Kaplan J-C, Camerino G, Meitinger T, Monaco AP. Mutations in the DAX-1 gene give rise to both X-linked adrenal hypoplasia congenita and hypogonadotropic hypogonadism. Nature. 1994;372:672–6.
Nakajima Y, Yamada M, Taguchi R, Shibusawa N, Ozawa A, Tomaru T, Hashimoto K, Saito T, Tsuchiya T, Okada S, Satoh T, Mori M. NR4A1 (Nur77) mediates thyrotropin-releasing hormone-induced stimulation of transcription of the thyrotropin beta gene: analysis of TRH knockout mice. PLoS One. 2012;7, e40437.
Nardulli AM, Greene GL, BW OM, Katzenellenbogen BS. Regulation of progesterone receptor messenger ribonucleic acid and protein levels in MCF-7 cells by estradiol: analysis of estrogen’s effect on progesterone receptor synthesis and degradation. Endocrinology. 1988;122:935–44.
Nardulli AM, Greene GL, Shapiro DJ. Human estrogen receptor bound to an estrogen response element bends DNA. Mol Endocrinol. 1993;7:331–40.
O’Malley BW. The steroid receptor superfamily: more excitement predicted for the future. Mol Endocrinol. 1990;4:363–9.
O’Malley BW, Malovannaya A, Qin J. Minireview: nuclear receptor and coregulator proteomics – 2012 and beyond. Mol Endocrinol. 2012;26:1646–50.
Ogawa S, Inoue S, Watanabe T, Hiroi H, Orimao A. The complete primary structure of human estrogen receptor beta (hER beta) and its heterodimerization with ER alpha in vivo and in vitro. Biochem Biophys Res Commun. 1998;243:122–6.
Ohlsson C, Hellberg N, Parini P, Vidal O, Bohlooly M, Rudling M, Lindberg MK, Warner M, Angelin B, Gustafsson JA. Obesity and disturbed lipoprotein profile in estrogen receptor-alpha-deficient male mice. Biochem Biophys Res Commun. 2000;278:640–5.
Okret S, Dong Y, Bronnegard M, Gustafsson JA. Regulation of glucocorticoid receptor expression. Biochimie. 1991;73:51–9.
Okulicz WC, Evans RW, Leavitt WW. Progesterone regulation of the occupied form of nuclear estrogen receptor. Science. 1981;213:1503–5.
Okun JG, Conway S, Schmidt KV, Schumacher J, Wang X, de Guia R, Zota A, Klement J, Seibert O, Peters A, Maida A, Herzig S, Rose AJ. Molecular regulation of urea cycle function by the liver glucocorticoid receptor. Mol Metab. 2015;4:732–40.
Otte K, Kranz H, Kober I, Thompson P, Hoefer M, Haubold B, Remmel B, Voss H, Kaiser C, Albers M, Cheruvallath Z, Jackson D, Casari G, Koegl M, Paabo S, Mous J, Kremoser C, Deuschle U. Identification of farnesoid X receptor beta as a novel mammalian nuclear receptor sensing lanosterol. Mol Cell Biol. 2003;23:864–72.
Paakinaho V, Kaikkonen S, Makkonen H, Benes V, Palvimo JJ. SUMOylation regulates the chromatin occupancy and anti-proliferative gene programs of glucocorticoid receptor. Nucleic Acids Res. 2014;42:1575–92.
Paech K, Webb P, Kuiper GG, Nilsson S, Gustafsson J, Kushner PJ, Scanlan TS. Differential ligand activation of estrogen receptors ERalpha and ERbeta at AP1 sites. Science. 1997;277:1508–10.
Palstra RJ, Grosveld F. Transcription factor binding at enhancers: shaping a genomic regulatory landscape in flux. Front Genet. 2012;3:195.
Pappas TC, Gametchu B, Watson CS. Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding. FASEB J. 1995;9:404–10.
Parks DJ, Blanchard SG, Bledsoe RK, Chandra G, Consler TG, Kliewer SA, Stimmel JB, Willson TM, Zavacki AM, Moore DD, Lehmann JM. Bile acids: natural ligands for an orphan nuclear receptor [see comments]. Science. 1999;284:1365–8.
Patel SR, Skafar DF. Modulation of nuclear receptor activity by the F domain. Mol Cell Endocrinol. 2015. doi:10.1016/j.mce.2015.07.009.
Pawlak M, Lefebvre P, Staels B. Molecular mechanism of PPARalpha action and its impact on lipid metabolism, inflammation and fibrosis in non-alcoholic fatty liver disease. J Hepatol. 2015;62:720–33.
Pedram A, Razandi M, Levin ER. Nature of functional estrogen receptors at the plasma membrane. Mol Endocrinol. 2006;20:1996–2009.
Pedram A, Razandi M, Sainson RCA, Kim JK, Hughes CC, Levin ER. A conserved mechanism for steroid receptor translocation to the plasma membrane. J Biol Chem. 2007;282:22278–88.
Peluso JJ, Pru JK. Non-canonical progesterone signaling in granulosa cell function. Reproduction. 2014;147:R169–78.
Peluso JJ, DeCerbo J, Lodde V. Evidence for a genomic mechanism of action for progesterone receptor membrane component-1. Steroids. 2012;77:1007–12.
Perrot-Applanat M, Groyer-Picard MT, Logeat F, Milgrom E. Ultrastructural localization of the progesterone receptor by an immunogold method: effect of hormone administration. J Cell Biol. 1986;102:1191–9.
Petz LN, Nardulli AM, Kim J, Horwitz KB, Freedman LP, Shapiro DJ. DNA bending is induced by binding of the glucocorticoid receptor DNA binding domain and progesterone receptors to their response element. J Steroid Biochem Mol Biol. 1997;60:31–41.
Picard D, Kumar V, Chambon P, Yamamoto KR. Signal transduction by steroid hormones: nuclear localization is differentially regulated in estrogen and glucocorticoid receptors. Cell Regul. 1990;1:291–9.
Pietras RJ, Marquez-Garban DC. Membrane-associated estrogen receptor signaling pathways in human cancers. Clin Cancer Res. 2007;13:4672–6.
Porter W, Saville B, Hoivik D, Safe S. Functional synergy between the transcription factor Sp1 and the estrogen receptor. Mol Endocrinol. 1997;11:1569–80.
Porto CS, Lazari MF, Abreu LC, Bardin CW, Gunsalus GL. Receptors for androgen-binding proteins: internalization and intracellular signalling. J Steroid Biochem Mol Biol. 1995;53:561–5.
Powell E, Xu W. Intermolecular interactions identify ligand-selective activity of estrogen receptor alpha/beta dimers. Proc Natl Acad Sci. 2008;105:19012–7.
Pratt WB, Toft DO. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev. 1997;18:306–60.
Prendergast P, Pan Z, Edwards DP. Progesterone receptor-induced bending of its target DNA: distinct effects of the A and B receptor forms. Mol Endocrinol. 1996;10:393–407.
Prossnitz ER, Barton M. Estrogen biology: new insights into GPER function and clinical opportunities. Mol Cell Endocrinol. 2014;389:71–83.
Querol Cano L, Lavery DN, Bevan CL. Mini-review: foldosome regulation of androgen receptor action in prostate cancer. Mol Cell Endocrinol. 2013;369:52–62.
Rajbhandari P, Finn G, Solodin NM, Singarapu KK, Sahu SC, Markley JL, Kadunc KJ, Ellison-Zelski SJ, Kariagina A, Haslam SZ, Lu KP, Alarid ET. Regulation of estrogen receptor α N-terminus conformation and function by peptidyl prolyl isomerase Pin1. Mol Cell Biol. 2012;32:445–57.
Rana K, Davey RA, Zajac JD. Human androgen deficiency: insights gained from androgen receptor knockout mouse models. Asian J Androl. 2014;16:169–77.
Ratman D, Vanden Berghe W, Dejager L, Libert C, Tavernier J, Beck IM, De Bosscher K. How glucocorticoid receptors modulate the activity of other transcription factors: a scope beyond tethering. Mol Cell Endocrinol. 2013;380:41–54.
Razandi M, Pedram A, Greene GL, Levin ER. Cell membrane and nuclear estrogen receptors (ERs) originate from a single transcript: studies of ERα and ERβ expressed in Chinese hamster ovary cells. Mol Endocrinol. 1999;13:307–19.
Razandi M, Pedram A, Park ST, Levin ER. Proximal events in signaling by plasma membrane estrogen receptors. J Biol Chem. 2003;278:2701–12.
Rechoum Y, Rovito D, Iacopetta D, Barone I, Ando S, Weigel NL, O’Malley BW, Brown PH, Fuqua SA. AR collaborates with ERalpha in aromatase inhibitor-resistant breast cancer. Breast Cancer Res Treat. 2014;147:473–85.
Renaud J-P, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature. 1995;378:681–9.
Revelli A, Massobrio M, Tesarik J. Nongenomic actions of steroid hormones in reproductive tissues. Endocrine Rev. 1998;19:3–17.
Riggins RB, Mazzotta MM, Maniya OZ, Clarke R. Orphan nuclear receptors in breast cancer pathogenesis and therapeutic response. Endocr Relat Cancer. 2010;17:R213–31.
Rishi AK, Gerald TM, Shao ZM, Li XS, Baumann RG, Dawson MI, Fontana JA. Regulation of the human retinoic acid receptor alpha gene in the estrogen receptor negative human breast carcinoma cell lines SKBR-3 and MDA-MB-435. Cancer Res. 1996;56:5246–52.
Rodgers JT, Lerin C, Haas W, Gygi SP, Spiegelman BM, Puigserver P. Nutrient control of glucose homeostasis through a complex of PGC-1[alpha] and SIRT1. Nature. 2005;434:113–8.
Rogerson FM, Fuller PJ. Interdomain interactions in the mineralocorticoid receptor. Mol Cell Endocrinol. 2003;200:45–55.
Romanoski CE, Glass CK, Stunnenberg HG, Wilson L, Almouzni G. Epigenomics: roadmap for regulation. Nature. 2015;518:314–6.
Rose AJ, Herzig S. Metabolic control through glucocorticoid hormones: an update. Mol Cell Endocrinol. 2013;380:65–78.
Rosenfeld MG, Glass CK. Coregulator codes of transcriptional regulation by nuclear receptors. J Biol Chem. 2001;276:36865–8.
Rosenfeld MG, Lunyak VV, Glass CK. Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response. Genes Dev. 2006;20:1405–28.
Rosner W, Hryb DJ, Khan MS, Nakhla AM, Romas NA. Sex hormone-binding globulin: anatomy and physiology of a new regulatory system. J Steroid Biochem Mol Biol. 1991;40:813–20.
Ruh MF, Chrivia JC, Cox LK, Ruh TS. The interaction of the estrogen receptor with mononucleosomes. Mol Cell Endocrinol. 2004;214:71–9.
Sabbah M, Ricousse SL, Redeuilh G, Baulieu EE. Estrogen receptor-induced bending of the Xenopus vitellogenin A2 gene hormone response element. Biochem Biophys Res Commun. 1992;185:944–52.
Safe S, Kim K. Non-classical genomic estrogen receptor (ER)/specificity protein and ER/activating protein-1 signaling pathways. J Mol Endocrinol. 2008;41:263–75.
Safe S, Jin UH, Hedrick E, Reeder A, Lee SO. Minireview: role of orphan nuclear receptors in cancer and potential as drug targets. Mol Endocrinol. 2014;28:157–72.
Safe S, Jin U-H, Morpurgo B, Abudayyeh A, Singh M, Tjalkens RB. Nuclear receptor 4A (NR4A) family – orphans no more. J Steroid Biochem Mol Biol. 2016;157:48–60.
Safer JD, Cohen RN, Hollenberg AN, Wondisford FE. Defective release of corepressor by hinge mutants of the thyroid hormone receptor found in patients with resistance to thyroid hormone. J Biol Chem. 1998;273:30175–82.
Sauer S. Ligands for the nuclear peroxisome proliferator-activated receptor gamma. Trends Pharmacol Sci. 2015;36:688–704.
Sauer F, Tjian R. Mechanisms of transcriptional activation: differences and similarities between yeast, Drosophila, and man. Curr Opin Genet Dev. 1997;7:176–81.
Scafoglio C, Ambrosino C, Cicatiello L, Altucci L, Ardovino M, Bontempo P, Medici N, Molinari AM, Nebbioso A, Facchiano A, Calogero RA, Elkon R, Menini N, Ponzone R, Biglia N, Sismondi P, De Bortoli M, Weisz A. Comparative gene expression profiling reveals partially overlapping but distinct genomic actions of different antiestrogens in human breast cancer cells. J Cell Biochem. 2006;98:1163–84.
Scarpin KM, Graham JD, Mote PA, Clarke CL. Progesterone action in human tissues: regulation by progesterone receptor (PR) isoform expression, nuclear positioning and coregulator expression. Nucl Recept Signal. 2009;7, e009.
Scherrer LC, Pratt WB. Association of the transformed glucocorticoid receptor with a cytoskeletal protein complex. J Steroid Biochem Mol Biol. 1992;41:719–21.
Schorderet DF, Escher P. NR2E3 mutations in enhanced S-cone sensitivity syndrome (ESCS), Goldmann-Favre syndrome (GFS), clumped pigmentary retinal degeneration (CPRD), and retinitis pigmentosa (RP). Hum Mutat. 2009;30:1475–85.
Schweizer MT, Yu EY. Persistent androgen receptor addiction in castration-resistant prostate cancer. J Hematol Oncol. 2015;8:128.
Seielstad DA, Carlson KE, Kushner PJ, Greene GL, Katzenellenbogen JA. Analysis of the structural core of the human estrogen receptor ligand binding domain by selective proteolysis/mass spectrometric analysis. Biochemistry (Mosc). 1995;34:12605–15.
Sentis S, Le Romancer M, Bianchin C, Rostan M-C, Corbo L. Sumoylation of the estrogen receptor {alpha} hinge region regulates its transcriptional activity. Mol Endocrinol. 2005;19:2671–84.
Seol W, Choi HS, Moore DD. An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors. Science. 1996;272:1336–9.
Seol W, Chung M, Moore DD. Novel receptor interaction and repression domains in the orphan receptor SHP. Mol Cell Biol. 1997;17:7126–31.
Shang Y, Hu X, DiRenzo J, Lazar MA, Brown M. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell. 2000;103:843–52.
Shao X, Wang M, Wei X, Deng S, Fu N, Peng Q, Jiang Y, Ye L, Lin Y. Peroxisome proliferator-activated receptor-gamma: master regulator of adipogenesis and obesity. Curr Stem Cell Res Ther. 2015. doi:10.1159/000438585.
Shibata H, Spencer TE, Onate SA, Jenster G, Tsai SY, Tsai MJ, O’Malley BW. Role of co-activators and co-repressors in the mechanism of steroid/thyroid receptor action. Recent Prog Horm Res. 1997;52:141–64.
Shulemovich K, Dimaculangan DD, Katz D, Lazar MA. DNA bending by thyroid hormone receptor: influence of half-site spacing and RXR. Nucleic Acids Res. 1995;23:811–8.
Simpkins JW, Yang S-H, Sarkar SN, Pearce V. Estrogen actions on mitochondria – physiological and pathological implications. Mol Cell Endocrinol. 2008;290:51–9.
Singh M, Su C, Ng S. Non-genomic mechanisms of progesterone action in the brain. Front Neurosci. 2013;7:159.
Sionov RV, Cohen O, Kfir S, Zilberman Y, Yefenof E. Role of mitochondrial glucocorticoid receptor in glucocorticoid-induced apoptosis. J Exp Med. 2006;203:189–201.
Smith CL, O’Malley BW. Coregulator function: a key to understanding tissue specificity of selective receptor modulators. Endocr Rev. 2004;25:45–71.
Solt LA, Burris TP. Action of RORs and their ligands in (patho)physiology. Trends Endocrinol Metab. 2012;23:619–27.
Song I-H, Buttgereit F. Non-genomic glucocorticoid effects to provide the basis for new drug developments. Mol Cell Endocrinol. 2006;246:142–6.
Song RX, Barnes CJ, Zhang Z, Bao Y, Kumar R, Santen RJ. The role of Shc and insulin-like growth factor 1 receptor in mediating the translocation of estrogen receptor {alpha} to the plasma membrane. Proc Natl Acad Sci U S A. 2004;101:2076–81.
Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou J, Mizzen CA, McKenna NJ, Onate SA, Tsai S, Tsai MJ, O’Malley BW. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature. 1997;389:194–8.
Stashi E, York B, O’Malley BW. Steroid receptor coactivators: servants and masters for control of systems metabolism. Trends Endocrinol Metab. 2014;25:337–47.
Stedronsky K, Telgmann R, Tillmann G, Walther N, Ivell R. The affinity and activity of the multiple hormone response element in the proximal promoter of the human oxytocin gene. J Neuroendocrinol. 2002;14:472–85.
Stein S, Schoonjans K. Molecular basis for the regulation of the nuclear receptor LRH-1. Curr Opin Cell Biol. 2015;33:26–34.
Stender JD, Kim K, Charn TH, Komm B, Chang KCN, Kraus WL, Benner C, Glass CK, Katzenellenbogen BS. Genome-wide analysis of estrogen receptor {alpha} DNA binding and tethering mechanisms identifies Runx1 as a Novel tethering factor in receptor-mediated transcriptional activation. Mol Cell Biol. 2010;30:3943–55.
Stenoien DL, Patel K, Mancini MG, Dutertre M, Smith CL, O’Malley BW, Mancini MA. FRAP reveals that mobility of oestrogen receptor-alpha is ligand- and proteasome-dependent. Nat Cell Biol. 2001;3:15–23.
Sternglanz R. Histone acetylation: a gateway to transcriptional activation. Trends Biochem Sci. 1996;21:357–8.
Stoica GE, Franke TF, Wellstein A, Czubayko F, List HJ, Reiter R, Morgan E, Martin MB, Stoica A. Estradiol rapidly activates Akt via the ErbB2 signaling pathway. Mol Endocrinol. 2003;17:818–30.
Stoner M, Wormke M, Saville B, Samudio I, Qin C, Abdelrahim M, Safe S. Estrogen regulation of vascular endothelial growth factor gene expression in ZR-75 breast cancer cells through interaction of estrogen receptor alpha and SP proteins. Oncogene. 2004;23:1052–63.
Stunnenberg HG. Mechanisms of transactivation by retinoic acid receptors. Bioessays. 1993;15:309–15.
Subramaniam N, Cairns W, Okret S. Studies on the mechanism of glucocorticoid-mediated repression from a negative glucocorticoid response element from the bovine prolactin gene. DNA Cell Biol. 1997;16:153–63.
Suntharalingham JP, Buonocore F, Duncan AJ, Achermann JC. DAX-1 (NR0B1) and steroidogenic factor-1 (SF-1, NR5A1) in human disease. Best Pract Res Clin Endocrinol Metab. 2015;29:607–19.
Surjit M, Ganti KP, Mukherji A, Ye T, Hua G, Metzger D, Li M, Chambon P. Widespread negative response elements mediate direct repression by agonist- liganded glucocorticoid receptor. Cell. 2011;145:224–41.
Swanson HI, Wada T, Xie W, Renga B, Zampella A, Distrutti E, Fiorucci S, Kong B, Thomas AM, Guo GL, Narayanan R, Yepuru M, Dalton JT, Chiang JY. Role of nuclear receptors in lipid dysfunction and obesity-related diseases. Drug Metab Dispos. 2013;41:1–11.
Syms AJ, Norris JS, Panko WB, Smith RG. Mechanism of androgen-receptor augmentation. Analysis of receptor synthesis and degradation by the density-shift technique. J Biol Chem. 1985;260:455–61.
Tadepally HD, Burger G, Aubry M. Evolution of C2H2-zinc finger genes and subfamilies in mammals: species-specific duplication and loss of clusters, genes and effector domains. BMC Evol Biol. 2008;8:176.
Talabér G, Jondal M, Okret S. Extra-adrenal glucocorticoid synthesis: immune regulation and aspects on local organ homeostasis. Mol Cell Endocrinol. 2013;380:89–98.
Tan MH, Zhou XE, Soon FF, Li X, Li J, Yong EL, Melcher K, Xu HE. The crystal structure of the orphan nuclear receptor NR2E3/PNR ligand binding domain reveals a dimeric auto-repressed conformation. PLoS One. 2013;8, e74359.
Tang Y, Getzenberg RH, Vietmeier BN, Stallcup MR, Eggert M, Renkawitz R, DeFranco DB. The DNA-binding and tau2 transactivation domains of the rat glucocorticoid receptor constitute a nuclear matrix-targeting signal. Mol Endocrinol. 1998;12:1420–31.
Tan-Wong SM, French JD, Proudfoot NJ, Brown MA. Dynamic interactions between the promoter and terminator regions of the mammalian BRCA1 gene. Proc Natl Acad Sci. 2008;105:5160–5.
Taraborrelli S. Physiology, production and action of progesterone. Acta Obstet Gynecol Scand. 2015;94:8–16.
Teng Y, Radde BN, Litchfield LM, Ivanova MM, Prough RA, Clark BJ, Doll MA, Hein DW, Klinge CM. Dehydroepiandrosterone activation of G-protein-coupled estrogen receptor rapidly stimulates, microRNA-21 transcription in human hepatocellular carcinoma cells. J Biol Chem. 2015;290:15799–811.
Tesarik J, Mendoza C. Direct non-genomic effects of follicular steroids on maturing human oocytes: oestrogen versus androgen antagonism. Hum Reprod Update. 1997;3:95–100.
Theodorou V, Stark R, Menon S, Carroll JS. GATA3 acts upstream of FOXA1 in mediating ESR1 binding by shaping enhancer accessibility. Genome Res. 2013;23:12–22.
Thomas P. Characteristics of membrane progestin receptor alpha (mPR[alpha]) and progesterone membrane receptor component 1 (PGMRC1) and their roles in mediating rapid progestin actions. Front Neuroendocrinol. 2008;29:292–312.
Thomas C, Gustafsson J-Å. The different roles of ER subtypes in cancer biology and therapy. Nat Rev Cancer. 2011;11:597–608.
Thomas P, Pang Y, Zhu Y, Detweiler C, Doughty K. Multiple rapid progestin actions and progestin membrane receptor subtypes in fish. Steroids. 2004;69:567–73.
Thompson EB. Steroid hormones. Membrane transporters of steroid hormones. Curr Biol. 1995;5:730–2.
Thornton JW. Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions. Proc Natl Acad Sci U S A. 2001;98:5671–6.
Thornton JW, Need E, Crews D. Resurrecting the ancestral steroid receptor: ancient origin of estrogen signaling. Science. 2003;301:1714–7.
Toran-Allerand CD. Minireview: a plethora of estrogen receptors in the brain: where will it end? Endocrinology. 2004;145:1069–74.
Traina TA. Results from a phase 2 study of enzalutamide (ENZA), an androgen receptor (AR) inhibitor, in advanced AR+ triple-negative breast cancer (TNBC). In 2015 ASSCO Annual meeting, Vol. 33. J Clin Oncol. 2015.
Tzukerman M, Zhang XK, Pfahl M. Inhibition of estrogen receptor activity by the tumor promoter 12-O- tetradeconylphorbol-13-acetate: a molecular analysis. Mol Endocrinol. 1991;5:1983–92.
Umesono K, Murakami KK, Thompson CC, Evans RM. Direct repeats as selective response elements for thyroid hormone, retinoic acid, and vitamin D3 receptors. Cell. 1991;65:1255–66.
Valley CC, Solodin NM, Powers GL, Ellison SJ, Alarid ET. Temporal variation in estrogen receptor-{alpha} protein turnover in the presence of estrogen. J Mol Endocrinol. 2008;40:23–34.
Vaquerizas JM, Kummerfeld SK, Teichmann SA, Luscombe NM. A census of human transcription factors: function, expression and evolution. Nat Rev Genet. 2009;10:252–63.
Viengchareun S, Le Menuet D, Martinerie L, Munier M, Pascual-Le Tallec L, Lombes M. The mineralocorticoid receptor: insights into its molecular and (patho)physiological biology. Nucl Recept Signal. 2007;5, e012.
Vinas R, Watson CS. Bisphenol S disrupts estradiol-induced nongenomic signaling in a rat pituitary cell line: effects on cell functions. Environ Health Perspect. 2013;121:352–8.
Wagner RL, Apriletti JW, McGrath ME, West BL, Baxter JD, Fletterick RJ. A structural role for hormone in the thyroid hormone receptor. A structural role for hormone in the thyroid hormone receptor. Nature. 1995;378:690–7.
Walesky C, Apte U. Role of hepatocyte nuclear factor 4alpha (HNF4alpha) in cell proliferation and cancer. Gene Expr. 2015;16:101–8.
Waltering KK, Urbanucci A, Visakorpi T. Androgen receptor (AR) aberrations in castration-resistant prostate cancer. Mol Cell Endocrinol. 2012;360:38–43.
Wang Q, Cooney AJ. Revisiting the role of GCNF in embryonic development. Semin Cell Dev Biol. 2013;24:679–86.
Wang T, Xiong JQ. The orphan nuclear receptor TLX/NR2E1 in neural stem cells and diseases. Neurosci Bull. 2016;32:108–14.
Wang Z-Y, Yin L. Estrogen receptor alpha-36 (ER-α36): a new player in human breast cancer. Mol Cell Endocrinol. 2015. doi:10.1016/j.mce.2015.04.017.
Wang Y, Fischle W, Cheung W, Jacobs S, Khorasanizadeh S, Allis CD. Beyond the double helix: writing and reading the histone code. Novartis Found Symp. 2004;259:3–17. discussion 17-21, 163-9.
Watson CS, Lange CA. Steadying the boat: integrating mechanisms of membrane and nuclear-steroid-receptor signalling. EMBO Rep. 2005;6:116–9.
Watson CS, Pappas TC, Gametchu B. The other estrogen receptor in the plasma membrane: implications for the actions of environmental estrogens. Environ Health Perspect. 1995;103 Suppl 7:41–50.
Watson CS, Campbell CH, Gametchu B. The dynamic and elusive membrane estrogen receptor-alpha. Steroids. 2002;67:429–37.
Watson CS, Bulayeva NN, Wozniak AL, Finnerty CC. Signaling from the membrane via membrane estrogen receptor-[alpha]: estrogens, xenoestrogens, and phytoestrogens. Steroids. 2005;70:364–71.
Watson CS, Jeng Y-J, Kochukov MY. Nongenomic signaling pathways of estrogen toxicity. Toxicol Sci. 2010;115:1–11.
Watson CS, Jeng Y-J, Hu G, Wozniak A, Bulayeva N, Guptarak J. Estrogen- and xenoestrogen-induced ERK signaling in pituitary tumor cells involves estrogen receptor-α interactions with G protein-αi and caveolin I. Steroids. 2012;77:424–32.
Webb P, Lopez GN, Uht RM, Kushner PJ. Tamoxifen activation of the estrogen receptor/AP-1 pathway. Mol Endocrinol. 1995;9:443–56.
Weiser MJ, Foradori CD, Handa RJ. Estrogen receptor beta in the brain: from form to function. Brain Res Rev. 2008;57:309–20.
Welboren W-J, Sweep FCGJ, Span PN, Stunnenberg HG. Genomic actions of estrogen receptor {alpha}: what are the targets and how are they regulated? Endocr Relat Cancer. 2009a;16:1073–89.
Welboren W-J, van Driel MA, Janssen-Megens EM, van Heeringen SJ, Sweep FCGJ, Span PN, Stunnenberg HG. ChIP-Seq of ER[alpha] and RNA polymerase II defines genes differentially responding to ligands. EMBO J. 2009b;28:1418. advanced online publication.
Westphal U. Steroid-protein interactions II. Monogr Endocrinol. 1986;27:1–603.
Willson TM, Moore JT. Genomics versus orphan nuclear receptors – a half-time report. Mol Endocrinol. 2002;16:1135–44.
Willson TM, Brown PJ, Sternbach DD, Henke BR. The PPARs: from orphan receptors to drug discovery. J Med Chem. 2000;43:527–50.
Wong M, Ramayya MS, Chrousos GP, Driggers PH, Parker KL. Cloning and sequence analysis of the human gene encoding steroidogenic factor 1. J Mol Endocrinol. 1996;17:139–47.
Wu C-T, Altuwaijri S, Ricke WA, Huang S-P, Yeh S, Zhang C, Niu Y, Tsai M-Y, Chang C. Increased prostate cell proliferation and loss of cell differentiation in mice lacking prostate epithelial androgen receptor. Proc Natl Acad Sci. 2007;104:12679–84.
Wu Q, Chambliss K, Lee W-R, Yuhanna IS, Mineo C, Shaul PW. Point mutations in the ERα Gαi binding domain segregate nonnuclear from nuclear receptor function. Mol Endocrinol. 2013;27:2–11.
Xue K, Liu J-y, Murphy BD, Tsang BK. Orphan nuclear receptor NR4A1 is a negative regulator of DHT-induced rat preantral follicular growth. Mol Endocrinol. 2012;26:2004–15.
Yamagata K. Chapter sixteen – roles of HNF1α and HNF4α in pancreatic β-Cells: lessons from a monogenic form of diabetes (MODY. In: Gerald L, editor. Vitamins and hormones, vol. 95. New York: Academic; 2014. p. 407–23.
Yang L, Guerrero J, Hong H, DeFranco DB, Stallcup MR. Interaction of the tau2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix. Mol Biol Cell. 2000;11:2007–18.
Yeh S, Tsai M-Y, Xu Q, Mu X-M, Lardy H, Huang K-E, Lin H, Yeh S-D, Altuwaijri S, Zhou X, Xing L, Boyce BF, Hung M-C, Zhang S, Gan L, Chang C. Generation and characterization of androgen receptor knockout (ARKO) mice: an in vivo model for the study of androgen functions in selective tissues. Proc Natl Acad Sci. 2002;99:13498–503.
Yi P, Wang Z, Feng Q, Pintilie GD, Foulds CE, Lanz RB, Ludtke SJ, Schmid MF, Chiu W, O’Malley BW. Structure of a biologically active estrogen receptor-coactivator complex on DNA. Mol Cell. 2015;57:1047–58.
Yin L, Wu N, Lazar MA. Nuclear receptor Rev-erbalpha: a heme receptor that coordinates circadian rhythm and metabolism. Nucl Recept Signal. 2010;8, e001.
York B, O’Malley BW. Steroid receptor coactivator (SRC) family: masters of systems biology. J Biol Chem. 2010;285:38743–50.
Yoshinaga SK, Peterson CL, Herskowitz I, Yamamoto KR. Roles of SWI1, SWI2, and SWI3 proteins for transcriptional enhancement by steroid receptors. Science. 1992;258:1598–604.
Young MJ, Rickard AJ. Mineralocorticoid receptors in the heart: lessons from cell-selective transgenic animals. J Endocrinol. 2015;224:R1–13.
Zarif JC, Lamb LE, Schulz VV, Nollet EA, Miranti CK. Androgen receptor non-nuclear regulation of prostate cancer cell invasion mediated by Src and matriptase. Oncotarget. 2015;6:6862–76.
Zboray L, Pluciennik A, Curtis D, Liu Y, Berman-Booty LD, Orr C, Kesler CT, Berger T, Gioeli D, Paschal BM, Merry DE. Preventing the androgen receptor N/C interaction delays disease onset in a mouse model of SBMA. Cell Rep. 2015;13:2312–23.
Zhang Y, Dufau ML. EAR2 and EAR3/COUP-TFI regulate transcription of the rat LH receptor. Mol Endocrinol. 2001;15:1891–905.
Zhang J, Lazar MA. The mechanism of action of thyroid hormones. Annu Rev Physiol. 2000;62:439–66.
Zhang Y, Wang L. Nuclear receptor small heterodimer partner in apoptosis signaling and liver cancer. Cancers (Basel). 2011;3:198–212.
Zhang G, Zhang L, Duff GW. A negative regulatory region containing a glucocorticosteroid response element (nGRE) in the human interleukin-1beta gene. DNA Cell Biol. 1997;16:145–52.
Zhang X, Tanaka K, Yan J, Li J, Peng D, Jiang Y, Yang Z, Barton MC, Wen H, Shi X. Regulation of estrogen receptor α by histone methyltransferase SMYD2-mediated protein methylation. Proc Natl Acad Sci. 2013;110:17284–9.
Zhang L, Fang C, Xu X, Li A, Cai Q, Long X. Androgen receptor, EGFR, and BRCA1 as biomarkers in triple-negative breast cancer: a meta-analysis. Biomed Res Int. 2015;2015:357485.
Zhao Y, Bruemmer D. NR4A orphan nuclear receptors: transcriptional regulators of gene expression in metabolism and vascular biology. Arterioscler Thromb Vasc Biol. 2010;30:1535–41.
Zhao C, Dahlman-Wright K, Gustafsson J-Å. Estrogen signaling via estrogen receptor β. J Biol Chem. 2010;285:39575–9.
Zhou W, Slingerland JM. Links between oestrogen receptor activation and proteolysis: relevance to hormone-regulated cancer therapy. Nat Rev Cancer. 2014;14:26–38.
Zhou G, Cummings R, Li Y, Mitra S, Wilkinson HA, Elbrecht A, Hermes JD, Schaeffer JM, Smith RG, Moller DE. Nuclear receptors have distinct affinities for coactivators: characterization by fluorescence resonance energy transfer. Mol Endocrinol. 1998;12:1594–604.
Zhu Y, Rice CD, Pang Y, Pace M, Thomas P. Cloning, expression, and characterization of a membrane progestin receptor and evidence it is an intermediary in meiotic maturation of fish oocytes. Proc Natl Acad Sci U S A. 2003a;100:2231–6.
Zhu Y, Rice CD, Pang Y, Pace M, Thomas P. From the cover: cloning, expression, and characterization of a membrane progestin receptor and evidence it is an intermediary in meiotic maturation of fish oocytes. Proc Natl Acad Sci U S A. 2003b;100:2231–6.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2016 Springer International Publishing AG
About this entry
Cite this entry
Klinge, C.M. (2016). Part III: Steroid Hormone Receptors and Signal Transduction Processes. In: Belfiore, A., LeRoith, D. (eds) Principles of Endocrinology and Hormone Action. Endocrinology. Springer, Cham. https://doi.org/10.1007/978-3-319-27318-1_9-1
Download citation
DOI: https://doi.org/10.1007/978-3-319-27318-1_9-1
Received:
Accepted:
Published:
Publisher Name: Springer, Cham
Online ISBN: 978-3-319-27318-1
eBook Packages: Springer Reference MedicineReference Module Medicine