Journal Menu
- About this Journal
- Abstracting and Indexing
- Aims and Scope
- Article Processing Charges
- Articles in Press
- Author Guidelines
- Bibliographic Information
- Citations to this Journal
- Contact Information
- Editorial Board
- Editorial Workflow
- Free eTOC Alerts
- Publication Ethics
- Reviewers Acknowledgment
- Submit a Manuscript
- Subscription Information
- Table of Contents
International Journal of Endocrinology
Volume 2013 (2013), Article ID 601246, 21 pages
http://dx.doi.org/10.1155/2013/601246
Review Article
Small-Molecule Hormones: Molecular Mechanisms of Action
1Department of Human Epigenetics, Mossakowski Medical Research Centre, 5 Pawinskiego Street, 02-106 Warsaw, Poland
2Department of Geriatrics and Gerontology, Medical Center of Postgraduate Education, 61/63 Kleczewska Street,
01-826 Warsaw, Poland
Received 28 August 2012; Revised 30 December 2012; Accepted 17 January 2013
Academic Editor: A. L. Barkan
Copyright © 2013 Monika Puzianowska-Kuznicka et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Linked References
- S. Suzuki, S. Shigematsu, H. Inaba, M. Takei, T. Takeda, and M. Komatsu, “Pituitary resistance to thyroid hormones: pathophysiology and therapeutic options,” Endocrine, vol. 40, no. 3, pp. 366–371, 2011. View at Publisher · View at Google Scholar
- A. M. Ferrara, K. Onigata, O. Ercan, H. Woodhead, R. E. Weiss, and S. Refetoff, “Homozygous thyroid hormone receptor b gene mutations in resistance to thyroid hormone: three new cases and review of the literature,” Journal of Clinical Endocrinology and Metabolism, vol. 97, no. 4, pp. 1328–1336, 2012. View at Publisher · View at Google Scholar
- S. Kannan and J. D. Safer, “Finding the right balance between resistance and sensitivity: a review of the cardiac manifestations of the syndrome of resistance to thyroid hormone and the implications for treatment,” Endocrine Practice, vol. 18, no. 2, pp. 252–255, 2012. View at Publisher · View at Google Scholar
- A. van Mullem, R. van Heerebeek, D. Chrysis, et al., “Clinical phenotype and mutant TRa1,” The New England Journal of Medicine, vol. 366, no. 15, pp. 1451–1453, 2012.
- O. Turowska, A. Nauman, M. Pietrzak et al., “Overexpression of E2F1 in clear cell renal cell carcinoma: a potential impact of erroneous regulation by thyroid hormone nuclear receptors,” Thyroid, vol. 17, no. 11, pp. 1039–1048, 2007. View at Publisher · View at Google Scholar · View at Scopus
- C. Lu and S. Y. Cheng, “Extranuclear signaling of mutated thyroid hormone receptors in promoting metastatic spread in thyroid carcinogenesis,” Steroids, vol. 76, no. 9, pp. 885–891, 2011. View at Publisher · View at Google Scholar · View at Scopus
- M. D. Rosen and M. L. Privalsky, “Thyroid hormone receptor mutations in cancer and resistance to thyroid hormone: perspective and prognosis,” Journal of Thyroid Research, Article ID 361304, 2011. View at Publisher · View at Google Scholar
- C. Lu, A. Mishra, Y. J. Zhu, P. Meltzer, and S. Y. Cheng, “Global expression profiling reveals gain-of-function oncogenic activity of a mutated thyroid hormone receptor in thyroid carcinogenesis,” American Journal of Cancer Research, vol. 1, no. 2, pp. 168–191, 2011.
- M. D. Rosen, I. H. Chan, and M. L. Privalsky, “Mutant thyroid hormone receptors (TRs) isolated from distinct cancer types display distinct target gene specificities: a unique regulatory repertoire associated with two renal clear cell carcinomas,” Molecular Endocrinology, vol. 25, no. 8, pp. 1311–1325, 2011. View at Publisher · View at Google Scholar · View at Scopus
- Z. Chen, Z. Y. Wang, and S. J. Chen, “Acute promyelocytic leukemia: cellular and molecular basis of differentiation and apoptosis,” Pharmacology and Therapeutics, vol. 76, no. 1–3, pp. 141–149, 1997. View at Publisher · View at Google Scholar · View at Scopus
- J. Olasz, A. Juhász, E. Remenár, et al., “RARβ2 suppression in head and neck squamous cell carcinoma correlates with site, histology and age,” Oncology Reports, vol. 18, no. 1, pp. 105–112, 2007.
- S. van Neerven, E. Kampmann, and J. Mey, “RAR/RXR and PPAR/RXR signaling in neurological and psychiatric diseases,” Progress in Neurobiology, vol. 85, no. 4, pp. 433–451, 2008. View at Publisher · View at Google Scholar · View at Scopus
- T. M. Nguyen, P. Adiceam, M. L. Kottler et al., “Tryptophan missense mutation in the ligand-binding domain of the vitamin D receptor causes severe resistance to 1,25-dihydroxyvitamin D,” Journal of Bone and Mineral Research, vol. 17, no. 9, pp. 1728–1737, 2002. View at Scopus
- J. M. Aljubeh, J. Wang, S. S. Al-Remeithi, P. J. Malloy, and D. Feldman, “Report of two unrelated patients with hereditary vitamin D resistant rickets due to the same novel mutation in the vitamin D receptor,” Journal of Pediatric Endocrinology and Metabolism, vol. 24, no. 9-10, pp. 793–799, 2011.
- P. J. Malloy, Y. Zhou, J. Wang, O. Hiort, and D. Feldman, “Hereditary vitamin D-resistant rickets (HVDRR) owing to a heterozygous mutation in the vitamin D receptor,” Journal of Bone and Mineral Research, vol. 26, no. 11, pp. 2710–2718, 2011. View at Publisher · View at Google Scholar
- F. Massart, G. Marcucci, and M. L. Brandt, “Pharmacogenetics of bone treatments: the VDR and ERα gene story,” Pharmacogenomics, vol. 9, no. 6, pp. 733–746, 2008. View at Publisher · View at Google Scholar · View at Scopus
- P. J. Malloy and D. Feldman, “The role of vitamin D receptor mutations in the development of alopecia,” Molecular and Cellular Endocrinology, vol. 347, no. 1-2, pp. 90–96, 2011. View at Publisher · View at Google Scholar
- K. Köstner, N. Denzer, C. S. L. Müller, R. Klein, W. Tilgen, and J. Reichrath, “The relevance of Vitamin D Receptor (VDR) gene polymorphisms for cancer: a review of the literature,” Anticancer Research, vol. 29, no. 9, pp. 3511–3536, 2009. View at Scopus
- S. Field and J. A. Newton-Bishop, “Melanoma and vitamin D,” Molecular Oncology, vol. 5, no. 2, pp. 197–214, 2011. View at Publisher · View at Google Scholar · View at Scopus
- J. Welsh, “Cellular and molecular effects of vitamin D on carcinogenesis,” Archives of Biochemistry and Biophysics, vol. 523, no. 1, pp. 107–114, 2012. View at Publisher · View at Google Scholar
- S. Wu and J. Sun, “Vitamin D, vitamin D receptor, and macroautophagy in inflammation and infection,” Discovery Medicine, vol. 11, no. 59, pp. 325–335, 2011. View at Publisher · View at Google Scholar
- S. Zúñiga, D. Firrincieli, C. Housset, and N. Chignard, “Vitamin D and the vitamin D receptor in liver pathophysiology,” Clinics and Research in Hepatology and Gastroenterology, vol. 35, no. 4, pp. 295–302, 2011. View at Publisher · View at Google Scholar · View at Scopus
- M. E. Visser, E. Kropman, M. E. Kranendonk et al., “Characterisation of non-obese diabetic patients with marked insulin resistance identifies a novel familial partial lipodystrophy-associated PPARγ mutation (Y151C),” Diabetologia, vol. 54, no. 7, pp. 1639–1644, 2011. View at Publisher · View at Google Scholar · View at Scopus
- E. H. Jeninga and E. Kalkhoven, “Central players in inherited lipodystrophies,” Trends in Endocrinology and Metabolism, vol. 21, no. 10, pp. 581–588, 2010. View at Publisher · View at Google Scholar · View at Scopus
- C. Vigouroux, M. Caron-Debarle, C. Le Dour, J. Magré, and J. Capeau, “Molecular mechanisms of human lipodystrophies: from adipocyte lipid droplet to oxidative stress and lipotoxicity,” International Journal of Biochemistry and Cell Biology, vol. 43, no. 6, pp. 862–876, 2011. View at Publisher · View at Google Scholar · View at Scopus
- M. Anbalagan, B. Huderson, L. Murphy, and B. G. Rowan, “Post-translational modifications of nuclear receptors and human disease,” Nuclear Receptor Signaling, vol. 10, article e001, 2012.
- G. T. Robbins and D. Nie, “PPARg, bioactive lipids, and cancer progression,” Frontiers in Bioscience, vol. 17, pp. 1816–1834, 2012. View at Publisher · View at Google Scholar
- N. Wang, R. Yin, Y. Liu, G. Mao, and F. Xi, “Role of peroxisome proliferator-activated receptor-γ in atherosclerosis: an update,” Circulation Journal, vol. 75, no. 3, pp. 528–535, 2011. View at Publisher · View at Google Scholar · View at Scopus
- H. Martin, “Role of PPAR-gamma in inflammation. Prospects for therapeutic intervention by food components,” Mutation Research, vol. 690, no. 1-2, pp. 57–63, 2010. View at Publisher · View at Google Scholar · View at Scopus
- H. Fahmi, J. Martel-Pelletier, J. P. Pelletier, and M. Kapoor, “Peroxisome proliferator-activated receptor gamma in osteoarthritis,” Modern Rheumatology, vol. 21, no. 1, pp. 1–9, 2011. View at Publisher · View at Google Scholar · View at Scopus
- E. T. Jacobs, M. E. Martínez, P. T. Campbell et al., “Genetic variation in the retinoid X receptor and calcium-sensing receptor and risk of colorectal cancer in the Colon Cancer Family Registry,” Carcinogenesis, vol. 31, no. 8, pp. 1412–1416, 2010. View at Publisher · View at Google Scholar · View at Scopus
- C. H. Hsieh, D. Pei, Y. J. Hung, and F. C. Hsiao, “Association between retinoid-X receptor g genetic polymorphisms and diabetic retinopathy,” Genetics and Molecular Research, vol. 10, no. 4, pp. 3545–3551, 2011. View at Publisher · View at Google Scholar
- H. Shi, X. Yu, Q. Li, et al., “Association between PPARγ and RXRα gene polymorphism and metabolic syndrome risk: a case-control study of a Chinese Han population,” Archives of Medical Research, vol. 43, no. 3, pp. 233–242, 2012. View at Publisher · View at Google Scholar
- I. Barone, L. Brusco, and S. A. W. Fuqua, “Estrogen receptor mutations and changes in downstream gene expression and signaling,” Clinical Cancer Research, vol. 16, no. 10, pp. 2702–2708, 2010. View at Publisher · View at Google Scholar · View at Scopus
- M. D. Valentin, S. D. da Silva, M. Privat, M. Alaoui-Jamali, and Y. J. Bignon, “Molecular insights on basal-like breast cancer,” Breast Cancer Research and Treatment, vol. 134, no. 1, pp. 21–30, 2012. View at Publisher · View at Google Scholar
- W. Eiermann, J. Bergh, F. Cardoso, et al., “Triple negative breast cancer: proposals for a pragmatic definition and implications for patient management and trial design,” Breast, vol. 21, no. 1, pp. 20–26, 2012. View at Publisher · View at Google Scholar
- M. Le Romancer, C. Poulard, P. Cohen, S. Sentis, J. M. Renoir, and L. Corbo, “Cracking the estrogen receptor's posttranslational code in breast tumors,” Endocrine Reviews, vol. 32, no. 5, pp. 597–622, 2011. View at Publisher · View at Google Scholar
- S. E. Bulun, D. Monsavais, M. E. Pavone, et al., “Role of estrogen receptor β in endometriosis,” Seminars in Reproductive Medicine, vol. 30, no. 1, pp. 39–45, 2012. View at Publisher · View at Google Scholar
- A. E. Drummond and P. J. Fuller, “Ovarian actions of estrogen receptor b: an update,” Seminars in Reproductive Medicine, vol. 30, no. 1, pp. 32–38, 2012. View at Publisher · View at Google Scholar
- M. H. Faulds, C. Zhao, K. Dahlman-Wright, and J. Å. Gustafsson, “The diversity of sex steroid action: regulation of metabolism by estrogen signaling,” Journal of Endocrinology, vol. 212, no. 1, pp. 3–12, 2012. View at Publisher · View at Google Scholar
- S. Rajender, L. Singh, and K. Thangaraj, “Phenotypic heterogeneity of mutations in androgen receptor gene,” Asian Journal of Andrology, vol. 9, no. 2, pp. 147–179, 2007. View at Publisher · View at Google Scholar · View at Scopus
- A. Galani, S. Kitsiou-Tzeli, C. Sofokleous, E. Kanavakis, and A. Kalpini-Mavrou, “Androgen insensitivity syndrome: clinical features and molecular defects,” Hormones, vol. 7, no. 3, pp. 217–229, 2008. View at Scopus
- I. A. Hughes, J. D. Davies, T. I. Bunch, V. Pasterski, K. Mastroyannopoulou, and J. MacDougall, “Androgen insensitivity syndrome,” The Lancet, vol. 380, no. 9851, pp. 1419–1428, 2012. View at Publisher · View at Google Scholar
- P. Saraon, K. Jarvi, and E. P. Diamandis, “Molecular alterations during progression of prostate cancer to androgen independence,” Clinical Chemistry, vol. 57, no. 10, pp. 1366–1375, 2011. View at Publisher · View at Google Scholar
- R. Kumar, H. Atamna, M. N. Zakharov, S. Bhasin, S. H. Khan, and R. Jasuja, “Role of the androgen receptor CAG repeat polymorphism in prostate cancer, and spinal and bulbar muscular atrophy,” Life Sciences, vol. 88, no. 13-14, pp. 565–571, 2011. View at Publisher · View at Google Scholar · View at Scopus
- J. P. Bergerat and J. Céraline, “Pleiotropic functional properties of androgen receptor mutants in prostate cancer,” Human Mutation, vol. 30, no. 2, pp. 145–157, 2009. View at Publisher · View at Google Scholar · View at Scopus
- M. Katsuno, H. Banno, K. Suzuki, H. Adachi, F. Tanaka, and G. Sobue, “Clinical features and molecular mechanisms of spinal and bulbar muscular atrophy (SBMA),” Advances in Experimental Medicine and Biology, vol. 685, pp. 64–74, 2010. View at Publisher · View at Google Scholar · View at Scopus
- B. Gottlieb, R. Lombroso, L. K. Beitel, and M. A. Trifiro, “Molecular pathology of the androgen receptor in male (in )fertility,” Reproductive BioMedicine Online, vol. 10, no. 1, pp. 42–48, 2005. View at Scopus
- S. E. Bulun, Y. H. Cheng, M. E. Pavone et al., “Estrogen receptor-β, estrogen receptor-α, and progesterone resistance in endometriosis,” Seminars in Reproductive Medicine, vol. 28, no. 1, pp. 36–43, 2010. View at Publisher · View at Google Scholar · View at Scopus
- S. Abid, J. Gokral, A. Maitra et al., “Altered expression of progesterone receptors in testis of infertile men,” Reproductive BioMedicine Online, vol. 17, no. 2, pp. 175–184, 2008. View at Scopus
- E. F. C. van Rossum and S. W. J. Lamberts, “Glucocorticoid resistance syndrome: a diagnostic and therapeutic approach,” Best Practice and Research, vol. 20, no. 4, pp. 611–626, 2006. View at Publisher · View at Google Scholar · View at Scopus
- N. C. Nicolaides, Z. Galata, T. Kino, G. P. Chrousos, and E. Charmandari, “The human glucocorticoid receptor: molecular basis of biologic function,” Steroids, vol. 75, no. 1, pp. 1–12, 2010. View at Publisher · View at Google Scholar · View at Scopus
- R. H. DeRijk and E. R. de Kloet, “Corticosteroid receptor polymorphisms: determinants of vulnerability and resilience,” European Journal of Pharmacology, vol. 583, no. 2-3, pp. 303–311, 2008. View at Publisher · View at Google Scholar · View at Scopus
- T. Kino and G. P. Chrousos, “Glucocorticoid and mineralocorticoid receptors and associated diseases,” Essays in Biochemistry, vol. 40, pp. 137–155, 2004. View at Scopus
- M. E. Rafestin-Oblin, A. Souque, B. Bocchi, G. Pinon, J. Fagart, and A. Vandewalle, “The severe form of hypertension caused by the activating S810L mutation in the mineralocorticoid receptor is cortisone related,” Endocrinology, vol. 144, no. 2, pp. 528–533, 2003. View at Publisher · View at Google Scholar · View at Scopus
- Nuclear Receptors Nomenclature Committee, “A unified nomenclature system for the nuclear receptor superfamily,” Cell, vol. 97, no. 2, pp. 161–163, 1999. View at Publisher · View at Google Scholar
- H. Escriva, S. Bertrand, and V. Laudet, “The evolution of the nuclear receptor superfamily,” Essays in Biochemistry, vol. 40, pp. 11–26, 2004. View at Scopus
- P. Germain, B. Staels, C. Dacquet, M. Spedding, and V. Laudet, “Overview of nomenclature of nuclear receptors,” Pharmacological Reviews, vol. 58, no. 4, pp. 685–704, 2006. View at Publisher · View at Google Scholar · View at Scopus
- C. Rochette-Egly, M. P. Gaub, Y. Lutz, S. Ali, I. Scheuer, and P. Chambon, “Retinoic acid receptor-β: immunodetection and phosphorylation on tyrosine residues,” Molecular Endocrinology, vol. 6, no. 12, pp. 2197–2209, 1992. View at Publisher · View at Google Scholar · View at Scopus
- C. E. Juge-Aubry, E. Hammar, C. Siegrist-Kaiser et al., “Regulation of the transcriptional activity of the peroxisome proliferator-activated receptor by phosphorylation of a ligand-independent trans-activating domain,” Journal of Biological Chemistry, vol. 274, no. 15, pp. 10505–10510, 1999. View at Publisher · View at Google Scholar · View at Scopus
- M. Nordzell, P. Aarnisalo, G. Benoit, D. S. Castro, and T. Perlmann, “Defining an N-terminal activation domain of the orphan nuclear receptor Nurr1,” Biochemical and Biophysical Research Communications, vol. 313, no. 1, pp. 205–211, 2004. View at Publisher · View at Google Scholar · View at Scopus
- P. Rajbhandari, G. Finn, N. M. Solodin, et al., “Regulation of estrogen receptor N-terminus conformation and function by peptidyl prolyl isomerase Pin1,” Molecular and Cellular Biology, vol. 32, no. 2, pp. 445–457, 2012. View at Publisher · View at Google Scholar
- B. F. Luisi, W. X. Xu, Z. Otwinowski, L. P. Freedman, K. R. Yamamoto, and P. B. Sigler, “Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA,” Nature, vol. 352, no. 6335, pp. 497–505, 1991. View at Publisher · View at Google Scholar · View at Scopus
- J. W. R. Schwabe, L. Chapman, J. T. Finch, and D. Rhodes, “The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements,” Cell, vol. 75, no. 3, pp. 567–578, 1993. View at Publisher · View at Google Scholar · View at Scopus
- T. Miyamoto, T. Kakizawa, K. Ichikawa et al., “The role of hinge domain in heterodimerization and specific DNA recognition by nuclear receptors,” Molecular and Cellular Endocrinology, vol. 181, no. 1-2, pp. 229–238, 2001. View at Publisher · View at Google Scholar · View at Scopus
- J. M. Wurtz, W. Bourguet, J. P. Renaud, et al., “A canonical structure for the ligand-binding domain of nuclear receptors,” Nature Structural Biology, vol. 3, no. 1, pp. 87–94, 1996. View at Publisher · View at Google Scholar
- J. Uppenberg, C. Svensson, M. Jaki, G. Bertilsson, L. Jendeberg, and A. Berkenstam, “Crystal structure of the ligand binding domain of the human nuclear receptor PPARγ,” Journal of Biological Chemistry, vol. 273, no. 47, pp. 31108–31112, 1998. View at Publisher · View at Google Scholar · View at Scopus
- W. Bourguet, M. Ruff, P. Chambon, H. Gronemeyer, and D. Moras, “Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α,” Nature, vol. 375, no. 6530, pp. 377–382, 1995. View at Scopus
- S. Nayeri, J. P. Kahlen, and G. Carlberg, “The high affinity ligand binding conformation of the nuclear 1,25-dihydroxyvitamin D3 receptor is functionally linked to the transactivation domain 2 (AF-2),” Nucleic Acids Research, vol. 24, no. 22, pp. 4513–4518, 1996. View at Publisher · View at Google Scholar · View at Scopus
- A. M. Brzozowski, A. C. W. Pike, Z. Dauter et al., “Molecular basis of agonism and antagonism in the oestrogen receptor,” Nature, vol. 389, no. 6652, pp. 753–758, 1997. View at Publisher · View at Google Scholar · View at Scopus
- R. L. Wagner, J. W. Apriletti, M. E. McGrath, B. L. West, J. D. Baxter, and R. J. Fletterick, “A structural role for hormone in the thyroid hormone receptor,” Nature, vol. 378, no. 6558, pp. 690–697, 1995. View at Scopus
- M. D. M. Huq, S. G. Ha, and L. N. Wei, “Modulation of retinoic acid receptor alpha activity by lysine methylation in the DNA binding domain,” Journal of Proteome Research, vol. 7, no. 10, pp. 4538–4545, 2008. View at Publisher · View at Google Scholar · View at Scopus
- P. La Rosa, V. Pesiri, G. Leclercq, M. Marino, and F. Acconcia, “Palmitoylation regulates 17β-estradiol-induced estrogen receptor α degradation and transcriptional activity,” Molecular Endocrinology, vol. 26, no. 5, pp. 762–774, 2012. View at Publisher · View at Google Scholar
- H. A. Abdel-Hafiz and K. B. Horwitz, “Control of progesterone receptor ranscriptional synergy by SUMOylation and deSUMOylation,” BMC Molecular Biology, vol. 22, no. 13, article 10, 2012. View at Publisher · View at Google Scholar
- S. Chen, S. Gulla, C. Cai, and S. P. Balk, “Androgen receptor serine 81 phosphorylation mediates chromatin binding and transcriptional activation,” Journal of Biological Chemistry, vol. 287, no. 11, pp. 8571–8583, 2012. View at Publisher · View at Google Scholar
- M. Anbalagan, B. Huderson, L. Murphy, and B. G. Rowan, “Post-translational modifications of nuclear receptors and human disease,” Nuclear Receptor Signaling, vol. 10, article e001, 2012.
- A. D. Wallace and J. A. Cidlowski, “Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids,” Journal of Biological Chemistry, vol. 276, no. 46, pp. 42714–42721, 2001. View at Publisher · View at Google Scholar · View at Scopus
- A. Ciechanover, A. Orian, and A. L. Schwartz, “Ubiquitin-mediated proteolysis: biological regulation via destruction,” Bioessays, vol. 22, no. 5, pp. 442–451, 2000.
- S. Sengupta and B. Wasylyk, “Ligand-dependent interaction of the glucocorticoid receptor with p53 enhances their degradation by Hdm2,” Genes and Development, vol. 15, no. 18, pp. 2367–2380, 2001. View at Publisher · View at Google Scholar · View at Scopus
- X. Wang and D. B. DeFranco, “Alternative effects of the ubiquitin-proteasome pathway on glucocorticoid receptor down-regulation and transactivation are mediated by CHIP, an E3 ligase,” Molecular Endocrinology, vol. 19, no. 6, pp. 1474–1482, 2005. View at Publisher · View at Google Scholar · View at Scopus
- D. M. Lonard, Z. Nawaz, C. L. Smith, and B. W. O'Malley, “The 26S proteasome is required for estrogen receptor-α and coactivator turnover and for efficient estrogen receptor-α transactivation,” Molecular Cell, vol. 5, no. 6, pp. 939–948, 2000. View at Scopus
- B. J. Deroo, C. Rentsch, S. Sampath, J. Young, D. B. DeFranco, and T. K. Archer, “Proteasomal inhibition enhances glucocorticoid receptor transactivation and alters its subnuclear trafficking,” Molecular and Cellular Biology, vol. 22, no. 12, pp. 4113–4123, 2002. View at Publisher · View at Google Scholar · View at Scopus
- W. B. Pratt, M. D. Galigniana, Y. Morishima, and P. J. M. Murphy, “Role of molecular chaperones in steroid receptor action,” Essays in Biochemistry, vol. 40, pp. 41–58, 2004. View at Scopus
- W. B. Pratt, Y. Morishima, M. Murphy, and M. Harrell, “Chaperoning of glucocorticoid receptors,” Handbook of experimental pharmacology., no. 172, pp. 111–138, 2006. View at Scopus
- L. Li, Z. Li, P. M. Howley, and D. B. Sacks, “E6AP and calmodulin reciprocally regulate estrogen receptor stability,” Journal of Biological Chemistry, vol. 281, no. 4, pp. 1978–1985, 2006. View at Publisher · View at Google Scholar · View at Scopus
- Y. Zhang, Z. Li, D. B. Sacks, and J. B. Ames, “Structural basis for Ca2+-induced activation and dimerization of estrogen receptor a by calmodulin,” Journal of Biological Chemistry, vol. 287, no. 12, pp. 9336–9344, 2012.
- A. Sivanandam, S. Murthy, K. Chinnakannu et al., “Calmodulin protects androgen receptor from calpain-mediated breakdown in prostate cancer cells,” Journal of Cellular Physiology, vol. 226, no. 7, pp. 1889–1896, 2011. View at Publisher · View at Google Scholar · View at Scopus
- P. La Rosa, V. Pesiri, G. Leclercq, M. Marino, and F. Acconcia, “Palmitoylation regulates 17β-estradiol-induced estrogen receptor α degradation and transcriptional activity,” Molecular Endocrinology, vol. 26, no. 5, pp. 762–774, 2012. View at Publisher · View at Google Scholar
- K. Chatterjee, J. K. Lee, A. Rentoumis, and J. L. Jameson, “Negative regulation of the thyroid-stimulating hormone α gene by thyroid hormone: receptor interaction adjacent to the TATA box,” Proceedings of the National Academy of Sciences of the United States of America, vol. 86, no. 23, pp. 9114–9118, 1989. View at Publisher · View at Google Scholar · View at Scopus
- S. Seoane, M. Alonso, C. Segura, and R. Pérez-Fernández, “Localization of a negative vitamin D response sequence in the human growth hormone gene,” Biochemical and Biophysical Research Communications, vol. 292, no. 1, pp. 250–255, 2002. View at Publisher · View at Google Scholar
- A. Weisz, L. Coppola, and F. Bresciani, “Specific binding of estrogen receptor to sites upstream and within the transcribed region of the chicken ovalbumin gene,” Biochemical and Biophysical Research Communications, vol. 139, no. 2, pp. 396–402, 1986. View at Scopus
- J. La Baer and K. R. Yamamoto, “Analysis of the DNA-binding affinity, sequence specificity and context dependence of the glucocorticoid receptor zinc finger region,” Journal of Molecular Biology, vol. 239, no. 5, pp. 664–688, 1994. View at Publisher · View at Google Scholar · View at Scopus
- F. Claessens and D. T. Gewirth, “DNA recognition by nuclear receptors,” Essays in Biochemistry, vol. 40, pp. 59–72, 2004. View at Scopus
- S. Y. Tsai, J. Carlstedt-Duke, N. L. Weigel et al., “Molecular interactions of steroid hormone receptor with its enhancer element: evidence for receptor dimer formation,” Cell, vol. 55, no. 2, pp. 361–369, 1988. View at Scopus
- C. M. Klinge, D. L. Bodenner, D. Desai, R. M. Niles, and A. M. Traish, “Binding of type II nuclear receptors and estrogen receptor to full and half-site estrogen response elements in Vitro,” Nucleic Acids Research, vol. 25, no. 10, pp. 1903–1912, 1997. View at Publisher · View at Google Scholar · View at Scopus
- R. C. J. Ribeiro, W. Feng, R. L. Wagner et al., “Definition of the surface in the thyroid hormone receptor ligand binding domain for association as homodimers and heterodimers with retinoid X receptor,” Journal of Biological Chemistry, vol. 276, no. 18, pp. 14987–14995, 2001. View at Publisher · View at Google Scholar · View at Scopus
- Y. Brelivet, S. Kammerer, N. Rochel, O. Poch, and D. Moras, “Signature of the oligomeric behaviour of nuclear receptors at the sequence and structural level,” EMBO Reports, vol. 5, no. 4, pp. 423–429, 2004. View at Publisher · View at Google Scholar · View at Scopus
- S. Lee and M. L. Privalsky, “Heterodimers of retinoic acid receptors and thyroid hormone receptors display unique combinatorial regulatory properties,” Molecular Endocrinology, vol. 19, no. 4, pp. 863–878, 2005. View at Publisher · View at Google Scholar · View at Scopus
- E. Powell and W. Xu, “Intermolecular interactions identify ligand-selective activity of estrogen receptor α/β dimers,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 48, pp. 19012–19017, 2008. View at Publisher · View at Google Scholar · View at Scopus
- T. E. Wilson, T. J. Fahrner, and J. Milbrandt, “The orphan receptors NGFI-B and steroidogenic factor 1 establish monomer binding as a third paradigm of nuclear receptor-DNA interaction,” Molecular and Cellular Biology, vol. 13, no. 9, pp. 5794–5804, 1993. View at Scopus
- D. J. Mangelsdorf, C. Thummel, M. Beato et al., “The nuclear receptor super-family: the second decade,” Cell, vol. 83, no. 6, pp. 835–839, 1995. View at Scopus
- M. Danielsen, L. Hinck, and G. M. Ringold, “Two amino acids within the knuckle of the first zinc finger specify DNA response element activation by the glucocorticoid receptor,” Cell, vol. 57, no. 7, pp. 1131–1138, 1989. View at Scopus
- G. Verrijdt, E. Schoenmakers, A. Haelens et al., “Change of specificity mutations in androgen-selective enhancers. Evidence for a role of differential DNA binding by the androgen receptor,” Journal of Biological Chemistry, vol. 275, no. 16, pp. 12298–12305, 2000. View at Publisher · View at Google Scholar · View at Scopus
- P. L. Shaffer, A. Jivan, D. E. Dollins, F. Claessens, and D. T. Gewirth, “Structural basis of androgen receptor binding to selective androgen response elements,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 14, pp. 4758–4763, 2004. View at Publisher · View at Google Scholar · View at Scopus
- S. Denayer, C. Helsen, L. Thorrez, A. Haelens, and F. Claessens, “The rules of DNA recognition by the androgen receptor,” Molecular Endocrinology, vol. 24, no. 5, pp. 898–913, 2010. View at Publisher · View at Google Scholar · View at Scopus
- F. Aslam, V. Shalhoub, A. J. Van Wijnen et al., “Contributions of distal and proximal promoter elements to glucocorticoid regulation of osteocalcin gene transcription,” Molecular Endocrinology, vol. 9, no. 6, pp. 679–690, 1995. View at Scopus
- X. M. Ou, J. M. Storring, N. Kushwaha, and P. R. Albert, “Heterodimerization of mineralocorticoid and glucocorticoid receptors at a novel negative response element of the 5-HT1A receptor gene,” Journal of Biological Chemistry, vol. 276, no. 17, pp. 14299–14307, 2001. View at Scopus
- M. M. V. Ruiz, T. H. Bugge, P. Hirschmann, and H. G. Stunnenberg, “Functional characterization of a natural retinoic acid responsive element,” EMBO Journal, vol. 10, no. 12, pp. 3829–3838, 1991. View at Scopus
- F. Casas, L. Daury, S. Grandemange et al., “Endocrine regulation of mitochondrial activity: involvement of truncated RXRα and c-Erb aα1 proteins,” FASEB Journal, vol. 17, no. 3, pp. 426–436, 2003. View at Publisher · View at Google Scholar · View at Scopus
- G. R. Williams, A. M. Zavacki, J. W. Harney, and G. A. Brent, “Thyroid hormone receptor binds with unique properties to response elements that contain hexamer domains in an inverted palindrome arrangement,” Endocrinology, vol. 134, no. 4, pp. 1888–1896, 1994. View at Publisher · View at Google Scholar · View at Scopus
- M. Ikeda, M. Rhee, and W. W. Chin, “Thyroid hormone receptor monomer, homodimer, and heterodimer (with retinoid-X receptor) contact different nucleotide sequences in thyroid hormone response elements,” Endocrinology, vol. 135, no. 4, pp. 1628–1638, 1994. View at Publisher · View at Google Scholar · View at Scopus
- M. A. Hirst, L. Hinck, M. Danielsen, and G. M. Ringold, “Discrimination of DNA response elements for thyroid hormone and estrogen is dependent on dimerization of receptor DNA binding domains,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 12, pp. 5527–5531, 1992. View at Publisher · View at Google Scholar · View at Scopus
- T. L. Towers, B. F. Luisi, A. Asianov, and L. P. Freedman, “DNA target selectivity by the vitamin D3 receptor: mechanism of dimer binding to an asymmetric repeat element,” Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 13, pp. 6310–6314, 1993. View at Scopus
- T. Miyamoto, S. Suzuki, and L. J. DeGroot, “High affinity and specificity of dimeric binding of thyroid hormone receptors to DNA and their ligand-dependent dissociation,” Molecular Endocrinology, vol. 7, no. 2, pp. 224–231, 1993. View at Publisher · View at Google Scholar · View at Scopus
- T. Miyamoto, S. Suzuki, and L. J. DeGroot, “Differential binding and activation of thyroid hormone response elements by TR(α1) and RXR(α)-trap heterodimers,” Molecular and Cellular Endocrinology, vol. 102, no. 1-2, pp. 111–117, 1994. View at Publisher · View at Google Scholar · View at Scopus
- C. Carlberg, I. Bendik, A. Wyss et al., “Two nuclear signalling pathways for vitamin D,” Nature, vol. 361, no. 6413, pp. 657–660, 1993. View at Publisher · View at Google Scholar · View at Scopus
- Z. H. Yan, A. Medvedev, T. Hirose, H. Gotoh, and A. M. Jetten, “Characterization of the response element and DNA binding properties of the nuclear orphan receptor germ cell nuclear factor/retinoid receptor- related testis-associated receptor,” Journal of Biological Chemistry, vol. 272, no. 16, pp. 10565–10572, 1997. View at Publisher · View at Google Scholar · View at Scopus
- R. Schule, K. Umesono, D. J. Mangelsdorf, J. Bolado, J. W. Pike, and R. M. Evans, “Jun-Fos and receptors for vitamins A and D recognize a common response element in the human osteocalcin gene,” Cell, vol. 61, no. 3, pp. 497–504, 1990. View at Publisher · View at Google Scholar · View at Scopus
- M. A. Lazar and T. J. Berrodin, “Thyroid hormone receptors form distinct nuclear protein-dependent and independent complexes with a thyroid hormone response element,” Molecular Endocrinology, vol. 4, no. 11, pp. 1627–1635, 1990. View at Scopus
- S. Faisst and S. Meyer, “Compilation of vertebrate-encoded transcription factors,” Nucleic Acids Research, vol. 20, no. 1, pp. 3–26, 1992. View at Scopus
- J. Kirfel, M. Kelter, L. M. Cancela, P. A. Price, and R. Schüle, “Identification of a novel negative retinoic acid responsive element in the promoter of the human matrix Gla protein gene,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 6, pp. 2227–2232, 1997. View at Publisher · View at Google Scholar · View at Scopus
- D. W. Eubank, E. Duplus, S. C. Williams, C. Forest, and E. G. Beale, “Peroxisome proliferator-activated receptor γ and chicken ovalbumin upstream promoter transcription factor II negatively regulate the phosphoenolpyruvate carboxykinase promoter via a common element,” Journal of Biological Chemistry, vol. 276, no. 32, pp. 30561–30569, 2001. View at Publisher · View at Google Scholar · View at Scopus
- M. S. Kim, R. Fujiki, A. Murayama et al., “1β,25(OH)2D3-induced transrepression by vitamin D receptor through E-box-type elements in the human parathyroid hormone gene promoter,” Molecular Endocrinology, vol. 21, no. 2, pp. 334–342, 2007. View at Publisher · View at Google Scholar · View at Scopus
- C. J. Guigon, D. W. Kim, X. Zhu, L. Zhao, and S. Y. Cheng, “Tumor suppressor action of liganded thyroid hormone receptor β by direct repression of β-catenin gene expression,” Endocrinology, vol. 151, no. 11, pp. 5528–5536, 2010. View at Publisher · View at Google Scholar · View at Scopus
- H. P. Harding and M. A. Lazar, “The orphan receptor Rev-ErbAα activates transcription via a novel response element,” Molecular and Cellular Biology, vol. 13, no. 5, pp. 3113–3121, 1993. View at Scopus
- V. Giguere, M. Tini, G. Flock, E. Ong, R. M. Evans, and G. Otulakowski, “Isoform-specific amino-terminal domains dictate DNA-binding properties of RORα, a novel family of orphan hormone nuclear receptors,” Genes and Development, vol. 8, no. 5, pp. 538–553, 1994. View at Scopus
- W. B. Pratt and D. O. Toft, “Steroid receptor interactions with heat shock protein and immunophilin chaperones,” Endocrine Reviews, vol. 18, no. 3, pp. 306–360, 1997. View at Publisher · View at Google Scholar · View at Scopus
- K. Graumann and A. Jungbauer, “Quantitative assessment of complex formation of nuclear-receptor accessory proteins,” Biochemical Journal, vol. 345, no. 3, pp. 627–636, 2000. View at Publisher · View at Google Scholar · View at Scopus
- T. Rajapandi, L. E. Greene, and E. Eisenberg, “The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor,” Journal of Biological Chemistry, vol. 275, no. 29, pp. 22597–22604, 2000. View at Publisher · View at Google Scholar · View at Scopus
- N. S. Cintron and D. Toft, “Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway,” Journal of Biological Chemistry, vol. 281, no. 36, pp. 26235–26244, 2006. View at Publisher · View at Google Scholar · View at Scopus
- J. P. Schülke, G. M. Wochnik, I. Lang-Rollin et al., “Differential impact of tetratricopeptide repeat proteins on the steroid hormone receptors,” PloS one, vol. 5, no. 7, article e11717, 2010. View at Publisher · View at Google Scholar · View at Scopus
- M. Nishi and M. Kawata, “Dynamics of glucocorticoid receptor and mineralocorticoid receptor: implications from live cell imaging studies,” Neuroendocrinology, vol. 85, no. 3, pp. 186–192, 2007. View at Publisher · View at Google Scholar · View at Scopus
- M. Kawata, M. Nishi, K. Matsuda et al., “Steroid receptor signalling in the brain—lessons learned from molecular imaging,” Journal of Neuroendocrinology, vol. 20, no. 6, pp. 673–676, 2008. View at Publisher · View at Google Scholar · View at Scopus
- C. Elbi, D. A. Walker, G. Romero et al., “Molecular chaperones function as steroid receptor nuclear mobility factors,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 9, pp. 2876–2881, 2004. View at Publisher · View at Google Scholar · View at Scopus
- T. E. Spencer, G. Jenster, M. M. Burcin et al., “Steroid receptor coactivator-1 is a histone acetyltransferase,” Nature, vol. 389, no. 6647, pp. 194–198, 1997. View at Publisher · View at Google Scholar · View at Scopus
- Z. Liu, J. Wong, S. Y. Tsai, M. J. Tsai, and B. W. O'Malley, “Sequential recruitment of steroid receptor coactivator-1 (SRC-1) and p300 enhances progesterone receptor-dependent initiation and reinitiation of transcription from chromatin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 22, pp. 12426–12431, 2001. View at Publisher · View at Google Scholar · View at Scopus
- M. Y. Kim, S. J. Hsiao, and W. L. Kraus, “A role for coactivators and histone acetylation in estrogen receptor α-mediated transcription initiation,” EMBO Journal, vol. 20, no. 21, pp. 6084–6094, 2001. View at Publisher · View at Google Scholar · View at Scopus
- B. Belandia, R. L. Orford, H. C. Hurst, and M. G. Parker, “Targeting of SWI/SNF chromatin remodelling complexes to estrogen-responsive genes,” EMBO Journal, vol. 21, no. 15, pp. 4094–4103, 2002. View at Publisher · View at Google Scholar · View at Scopus
- Z. Kang, O. A. Jänne, and J. J. Palvimo, “Coregulator recruitment and histone modifications in transcriptional regulation by the androgen receptor,” Molecular Endocrinology, vol. 18, no. 11, pp. 2633–2648, 2004. View at Publisher · View at Google Scholar · View at Scopus
- D. J. van de Wijngaart, H. J. Dubbink, M. E. van Royen, J. Trapman, and G. Jenster, “Androgen receptor coregulators: recruitment via the coactivator binding groove,” Molecular and Cellular Endocrinology, vol. 352, no. 1-2, pp. 57–69, 2012. View at Publisher · View at Google Scholar
- D. Pearce, W. Matsui, J. N. Miner, and K. R. Yamamoto, “Glucocorticoid receptor transcriptional activity determined by spacing of receptor and nonreceptor DNA sites,” Journal of Biological Chemistry, vol. 273, no. 46, pp. 30081–30085, 1998. View at Publisher · View at Google Scholar · View at Scopus
- P. J. Kushner, D. A. Agard, G. L. Greene et al., “Estrogen receptor pathways to AP-1,” Journal of Steroid Biochemistry and Molecular Biology, vol. 74, no. 5, pp. 311–317, 2000. View at Publisher · View at Google Scholar · View at Scopus
- H. Takai, Y. Nakayama, D. S. Kim et al., “Androgen receptor stimulates bone sialoprotein (BSP) gene transcription via cAMP response element and activator protein 1/glucocorticoid response elements,” Journal of Cellular Biochemistry, vol. 102, no. 1, pp. 240–251, 2007. View at Publisher · View at Google Scholar · View at Scopus
- H. Konig, H. Ponta, H. J. Rahmsdorf, and P. Herrlich, “Interference between pathway-specific transcription factors: glucocorticoids antagonize phorbol ester-induced AP-1 activity without altering AP-1 site occupation in vivo,” EMBO Journal, vol. 11, no. 6, pp. 2241–2246, 1992. View at Scopus
- N. Gionet, D. Jansson, S. Mader, and M. A. C. Pratt, “NF-κB and estrogen receptor α interactions: differential function in estrogen receptor-negative and -positive hormone-independent breast cancer cells,” Journal of Cellular Biochemistry, vol. 107, no. 3, pp. 448–459, 2009. View at Publisher · View at Google Scholar · View at Scopus
- N. A. Rao, M. T. McCalman, P. Moulos, et al., “Coactivation of GR and NFKB alters the repertoire of their binding sites and target genes,” Genome Research, vol. 21, no. 9, pp. 1404–1416, 2011. View at Publisher · View at Google Scholar
- J. D. Chen and R. M. Evans, “A transcriptional co-repressor that interacts with nuclear hormone receptors,” Nature, vol. 377, no. 6548, pp. 454–457, 1995. View at Scopus
- A. J. Hörlein, A. M. Näär, T. Heinzel, et al., “Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor,” Nature, vol. 377, no. 6548, pp. 397–404, 1995. View at Publisher · View at Google Scholar
- V. Cavailles, S. Dauvois, F. L'Horset et al., “Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor,” EMBO Journal, vol. 14, no. 15, pp. 3741–3751, 1995. View at Scopus
- I. Fernandes, Y. Bastien, T. Wai et al., “Ligand-dependent nuclear receptor corepressor LCoR functions by histone deacetylase-dependent and -independent mechanisms,” Molecular Cell, vol. 11, no. 1, pp. 139–150, 2003. View at Publisher · View at Google Scholar · View at Scopus
- P. Augereau, E. Badia, S. Carascossa, et al., “The nuclear receptor transcriptional coregulator RIP140,” Nuclear Receptor Signaling, vol. 4, article e024, 2006.
- N. Subramaniam, W. Cairns, and S. Okret, “Glucocorticoids repress transcription from a negative glucocorticoid response element recognized by two homeodomain-containing proteins, Pbx and Oct-1,” Journal of Biological Chemistry, vol. 273, no. 36, pp. 23567–23574, 1998. View at Publisher · View at Google Scholar · View at Scopus
- M. A. Wilson and S. A. Chrysogelos, “Identification and characterization of a negative regulatory element within the epidermal growth factor receptor gene first intron in hormone-dependent breast cancer cells,” Journal of Cellular Biochemistry, vol. 85, no. 3, pp. 601–614, 2002. View at Publisher · View at Google Scholar · View at Scopus
- M. V. Govindan, “Recruitment of cAMP-response element-binding protein and histone deacetylase has opposite effects on glucocorticoid receptor gene transcription,” Journal of Biological Chemistry, vol. 285, no. 7, pp. 4489–4510, 2010. View at Publisher · View at Google Scholar · View at Scopus
- K. Prüfer and J. Barsony, “Retinoid X Receptor dominates the nuclear import and export of the unliganded vitamin D receptor,” Molecular Endocrinology, vol. 16, no. 8, pp. 1738–1751, 2002. View at Publisher · View at Google Scholar · View at Scopus
- X. Cao, W. Liu, F. Lin, et al., “Retinoid X receptor regulates Nur77/TR3-dependent apoptosis by modulating its nuclear export and mitochondrial targeting,” Molecular and Cellular Biology, vol. 24, no. 22, pp. 9705–9725, 2004. View at Publisher · View at Google Scholar
- V. C. Yu, C. Delsert, B. Andersen et al., “RXRβ: a coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elements,” Cell, vol. 67, no. 6, pp. 1251–1266, 1991. View at Scopus
- M. Puzianowska-Kuznicka, S. Damjanovski, and Y. B. Shi, “Both thyroid hormone and 9-cis retinoic acid receptors are required to efficiently mediate the effects of thyroid hormone on embryonic development and specific gene regulation in Xenopus laevis,” Molecular and Cellular Biology, vol. 17, no. 8, pp. 4738–4749, 1997. View at Scopus
- L. Laflamme, G. Hamann, N. Messier, S. Maltais, and M. F. Langlois, “RXR acts as a coregulator in the regulation of genes of the hypothalamo-pituitary axis by thyroid hormone receptors,” Journal of Molecular Endocrinology, vol. 29, no. 1, pp. 61–72, 2002. View at Publisher · View at Google Scholar · View at Scopus
- P. Lefebvre, Y. Benomar, and B. Staels, “Retinoid X receptors: common heterodimerization partners with distinct functions,” Trends in Endocrinology and Metabolism, vol. 21, no. 11, pp. 676–683, 2010. View at Publisher · View at Google Scholar · View at Scopus
- S. Mader, J. Y. Chen, Z. Chen, J. White, P. Chambon, and H. Gronemeyer, “The patterns of binding of RAR, RXR and TR homo- and heterodimers to direct repeats are dictated by the binding specificities of the DNA binding domains,” EMBO Journal, vol. 12, no. 13, pp. 5029–5041, 1993. View at Scopus
- W. R. Force, J. B. Tillman, C. N. Sprung, and S. R. Spindler, “Homodimer and heterodimer DNA binding and transcriptional responsiveness to triiodothyronine (T3) and 9-cis-retinoic acid are determined by the number and order of high affinity half-sites in a T3 response element,” Journal of Biological Chemistry, vol. 269, no. 12, pp. 8863–8871, 1994. View at Scopus
- B. Morin, L. A. Nichols, and L. J. Holland, “Flanking sequence composition differentially affects the binding and functional characteristics of glucocorticoid receptor homo- and heterodimers,” Biochemistry, vol. 45, no. 23, pp. 7299–7306, 2006. View at Publisher · View at Google Scholar · View at Scopus
- T. Perlmann, P. N. Rangarajan, K. Umesono, and R. M. Evans, “Determinants for selective RAR and TR recognition of direct repeat HREs,” Genes and Development, vol. 7, no. 7, pp. 1411–1422, 1993. View at Scopus
- R. Kurokawa, V. C. Yu, A. Naar et al., “Differential orientations of the DNA-binding domain and carboxy-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers,” Genes and Development B, vol. 7, no. 7, pp. 1423–1435, 1993. View at Scopus
- R. Kurokawa, J. DiRenzo, M. Boehm et al., “Regulation of retinoid signalling by receptor polarity and allosteric control of ligand binding,” Nature, vol. 371, no. 6497, pp. 528–531, 1994. View at Publisher · View at Google Scholar · View at Scopus
- A. IJpenberg, E. Jeannin, W. Wahli, and B. Desvergne, “Polarity and specific sequence requirements of peroxisome proliferator- activated receptor (PPAR)/retinoid X receptor heterodimer binding to DNA. A functional analysis of the malic enzyme gene PPAR response element,” Journal of Biological Chemistry, vol. 272, no. 32, pp. 20108–20117, 1997. View at Publisher · View at Google Scholar · View at Scopus
- J. Ferrara, K. McCuaig, G. N. Hendy, M. Uskokovic, and J. H. White, “Highly potent transcriptional activation by 16-ene derivatives of 1,25- dihydroxyvitamin D3. Lack of modulation by 9-cis-retinoic acid of response to 1,25-dihydroxyvitamin D3 or its derivatives,” Journal of Biological Chemistry, vol. 269, no. 4, pp. 2971–2981, 1994. View at Scopus
- B. M. Forman, K. Umesono, J. Chen, and R. M. Evans, “Unique response pathways are established by allosteric interactions among nuclear hormone receptors,” Cell, vol. 81, no. 4, pp. 541–550, 1995. View at Scopus
- D. Li, T. Yamada, F. Wang, A. I. Vulin, and H. H. Samuels, “Novel roles of retinoid X receptor (RXR) anal RXR ligand in dynamically modulating the activity of the thyroid hormone receptor/RXR heterodimer,” Journal of Biological Chemistry, vol. 279, no. 9, pp. 7427–7437, 2004. View at Publisher · View at Google Scholar · View at Scopus
- J. Y. Chen, J. Clifford, C. Zusi et al., “Two distinct actions of retinoid-receptor ligands,” Nature, vol. 382, no. 6594, pp. 819–822, 1996. View at Publisher · View at Google Scholar · View at Scopus
- S. A. Kliewer, K. Umesono, D. J. Noonan, R. A. Heyman, and R. M. Evans, “Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors,” Nature, vol. 358, no. 6389, pp. 771–774, 1992. View at Publisher · View at Google Scholar · View at Scopus
- V. Antonio, B. Janvier, A. Brouillet, M. Andreani, and M. Raymondjean, “Oxysterol and 9-cis-retinoic acid stimulate the group IIA secretory phospholipase A2 gene in rat smooth-muscle cells,” Biochemical Journal, vol. 376, no. 2, pp. 351–360, 2003. View at Publisher · View at Google Scholar · View at Scopus
- I. Zamir, J. Dawson, R. M. Lavinsky, C. K. Glass, M. G. Rosenfeld, and M. A. Lazar, “Cloning and characterization of a corepressor and potential component of the nuclear hormone receptor repression complex,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 26, pp. 14400–14405, 1997. View at Publisher · View at Google Scholar · View at Scopus
- U. Dressel, D. Thormeyer, B. Altincicek et al., “Alien, a highly conserved protein with characteristics of a corepressor for members of the nuclear hormone receptor superfamily,” Molecular and Cellular Biology, vol. 19, no. 5, pp. 3383–3394, 1999. View at Scopus
- P. J. Watson, L. Fairall, and J. W. Schwabe, “Nuclear hormone receptor co-repressors: structure and function,” Molecular and Cellular Endocrinology, vol. 348, no. 2, pp. 440–449, 2012. View at Publisher · View at Google Scholar
- R. P. S. Kwok, J. R. Lundblad, J. C. Chrivia et al., “Nuclear protein CBP is a coactivator for the transcription factor CREB,” Nature, vol. 370, no. 6486, pp. 223–226, 1994. View at Publisher · View at Google Scholar · View at Scopus
- J. R. Lundblad, R. P. S. Kwok, M. E. Laurance, M. L. Harter, and R. H. Goodman, “Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP,” Nature, vol. 374, no. 6517, pp. 85–88, 1995. View at Scopus
- S. A. Onate, S. Y. Tsai, M. J. Tsai, and B. W. O'Malley, “Sequence and characterization of a coactivator for the steroid hormone receptor superfamily,” Science, vol. 270, no. 5240, pp. 1354–1357, 1995. View at Scopus
- J. J. Voegel, M. J. S. Heine, C. Zechel, P. Chambon, and H. Gronemeyer, “TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors,” EMBO Journal, vol. 15, no. 14, pp. 3667–3675, 1996. View at Scopus
- J. D. Fondell, H. Ge, and R. G. Roeder, “Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 16, pp. 8329–8333, 1996. View at Publisher · View at Google Scholar · View at Scopus
- X. J. Yang, V. V. Ogryzko, J. I. Nishikawa, B. H. Howard, and Y. Nakatani, “A p300/CPB-associated factor that competes with the adenoviral oncoprotein E1A,” Nature, vol. 382, no. 6589, pp. 319–324, 1996. View at Publisher · View at Google Scholar · View at Scopus
- A. Takeshita, G. R. Cardona, N. Koibuchi, C. S. Suen, and W. W. Chin, “TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1,” Journal of Biological Chemistry, vol. 272, no. 44, pp. 27629–27634, 1997. View at Publisher · View at Google Scholar · View at Scopus
- P. Puigserver, Z. Wu, C. W. Park, R. Graves, M. Wright, and B. M. Spiegelman, “A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis,” Cell, vol. 92, no. 6, pp. 829–839, 1998. View at Publisher · View at Google Scholar · View at Scopus
- C. Rachez, Z. Suldan, J. Ward et al., “A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system,” Genes and Development, vol. 12, no. 12, pp. 1787–1800, 1998. View at Scopus
- H. J. Kim, J. Y. Yi, H. S. Sung et al., “Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation,” Molecular and Cellular Biology, vol. 19, no. 9, pp. 6323–6332, 1999. View at Scopus
- S. K. Lee, S. L. Anzick, J. E. Choi et al., “A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo,” Journal of Biological Chemistry, vol. 274, no. 48, pp. 34283–34293, 1999. View at Publisher · View at Google Scholar · View at Scopus
- Y. Wu, P. Delerive, W. W. Chin, and T. P. Burris, “Requirement of helix 1 and the AF-2 domain of the thyroid hormone receptor for coactivation by PGC-1,” Journal of Biological Chemistry, vol. 277, no. 11, pp. 8898–8905, 2002. View at Publisher · View at Google Scholar · View at Scopus
- B. York and B. W. O'Malley, “Steroid Receptor Coactivator (SRC) family: masters of systems biology,” Journal of Biological Chemistry, vol. 285, no. 50, pp. 38743–38750, 2010. View at Publisher · View at Google Scholar · View at Scopus
- G. Salbert, A. Fanjul, F. J. Piedrafita et al., “Retinoic acid receptors and retinoid X receptor-α down-regulate the transforming growth factor-β1 promoter by antagonizing AP-1 activity,” Molecular Endocrinology, vol. 7, no. 10, pp. 1347–1356, 1993. View at Publisher · View at Google Scholar · View at Scopus
- H. Harant, P. J. Andrew, G. S. Reddy, E. Foglar, and I. J. D. Lindley, “1α,25-dihydroxyvitamin D3 and a variety of its natural metabolites transcriptionally repress nuclear-factor-κB-mediated interleukin-8 gene expression,” European Journal of Biochemistry, vol. 250, no. 1, pp. 63–71, 1997. View at Scopus
- G. Barrera-Hernandez, Q. Zhan, R. Wong, and S. Y. Cheng, “Thyroid hormone receptor is a negative regulator in p53-mediated signaling pathways,” DNA and Cell Biology, vol. 17, no. 9, pp. 743–750, 1998. View at Scopus
- J. Xu, K. L. Thompson, L. B. Shephard, L. G. Hudson, and G. N. Gill, “T3 receptor suppression of Sp1-dependent transcription from the epidermal growth factor receptor promoter via overlapping DNA-binding sites,” Journal of Biological Chemistry, vol. 268, no. 21, pp. 16065–16073, 1993. View at Scopus
- D. D'Ambrosio, M. Cippitelli, M. G. Cocciolo et al., “Inhibition of IL-12 production by 1,25-dihydroxyvitamin D3. Involvement of NF-κB downregulation in transcriptional repression of the p40 gene,” Journal of Clinical Investigation, vol. 101, no. 1, pp. 252–262, 1998. View at Scopus
- G. B. Potter, G. M. J. Beaudoin III, C. L. DeRenzo, J. M. Zarach, S. H. Chen, and C. C. Thompson, “The hairless gene mutated in congenital hair loss disorders encodes a novel nuclear receptor corepressor,” Genes and Development, vol. 15, no. 20, pp. 2687–2701, 2001. View at Publisher · View at Google Scholar · View at Scopus
- A. N. Moraitis, V. Giguère, and C. C. Thompson, “Novel mechanism of nuclear receptor corepressor interaction dictated by activation function 2 helix determinants,” Molecular and Cellular Biology, vol. 22, no. 19, pp. 6831–6841, 2002. View at Publisher · View at Google Scholar · View at Scopus
- J. C. Hsieh, J. M. Sisk, P. W. Jurutka et al., “Physical and functional interaction between the vitamin D receptor and hairless corepressor, two proteins required for hair cycling,” Journal of Biological Chemistry, vol. 278, no. 40, pp. 38665–38674, 2003. View at Publisher · View at Google Scholar · View at Scopus
- M. T. Epping, L. Wang, M. J. Edel, L. Carlée, M. Hernandez, and R. Bernards, “The human tumor antigen PRAME is a dominant repressor of retinoic acid receptor signaling,” Cell, vol. 122, no. 6, pp. 835–847, 2005. View at Publisher · View at Google Scholar · View at Scopus
- K. Hashimoto, M. Yamada, S. Matsumoto, T. Monden, T. Satoh, and M. Mori, “Mouse sterol response element binding protein-1c gene expression is negatively regulated by thyroid hormone,” Endocrinology, vol. 147, no. 9, pp. 4292–4302, 2006. View at Publisher · View at Google Scholar · View at Scopus
- J. C. G. Blanco, I. M. Wang, S. Y. Tsai et al., “Transcription factor TFIIB and the vitamin D receptor cooperatively activate ligand-dependent transcription,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 5, pp. 1535–1539, 1995. View at Publisher · View at Google Scholar · View at Scopus
- J. D. Fondell, F. Brunel, K. Hisatake, and R. G. Roeder, “Unliganded thyroid hormone receptor α can target TATA-binding protein for transcriptional repression,” Molecular and Cellular Biology, vol. 16, no. 1, pp. 281–287, 1996. View at Scopus
- I. J. Mcewan and J. Gustafsson, “Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 16, pp. 8485–8490, 1997. View at Publisher · View at Google Scholar · View at Scopus
- A. Wärnmark, A. Wikström, A. P. H. Wright, J. Å. Gustafsson, and T. Härd, “The N-terminal Regions of Estrogen Receptor α and β are Unstructured in Vitro and Show Different TBP Binding Properties,” Journal of Biological Chemistry, vol. 276, no. 49, pp. 45939–45944, 2001. View at Publisher · View at Google Scholar · View at Scopus
- J. Reid, I. Murray, K. Watt, R. Betney, and I. J. McEwan, “The androgen receptor interacts with multiple regions of the large subunit of general transcription factor TFIIF,” Journal of Biological Chemistry, vol. 277, no. 43, pp. 41247–41253, 2002. View at Publisher · View at Google Scholar · View at Scopus
- S. H. Khan, J. Ling, and R. Kumar, “TBP binding-induced folding of the Glucocorticoid receptor AF1 domain facilitates its interaction with Steroid Receptor Coactivator-1,” PLoS ONE, vol. 6, no. 7, article e21939, Article ID e21939, 2011. View at Publisher · View at Google Scholar · View at Scopus
- D. M. Heery, E. Kalkhoven, S. Hoare, and M. G. Parker, “A signature motif in transcriptional co-activators mediates binding to nuclear receptors,” Nature, vol. 387, no. 6634, pp. 733–736, 1997. View at Publisher · View at Google Scholar · View at Scopus
- A. J. Bannister and T. Kouzarides, “The CBP co-activator is a histone acetyltransferase,” Nature, vol. 384, no. 6610, pp. 641–643, 1996. View at Publisher · View at Google Scholar · View at Scopus
- V. V. Ogryzko, R. L. Schiltz, V. Russanova, B. H. Howard, and Y. Nakatani, “The transcriptional coactivators p300 and CBP are histone acetyltransferases,” Cell, vol. 87, no. 5, pp. 953–959, 1996. View at Publisher · View at Google Scholar · View at Scopus
- W. Shao, A. Rosenauer, K. Mann et al., “Ligand-inducible interaction of the DRIP/TRAP coactivator complex with retinoid receptors in retinoic acid-sensitive and -resistant acute promyelocytic leukemia cells,” Blood, vol. 96, no. 6, pp. 2233–2239, 2000. View at Scopus
- V. Perissi, L. M. Staszewski, E. M. McInerney et al., “Molecular determinants of nuclear receptor-corepressor interaction,” Genes and Development, vol. 13, no. 24, pp. 3198–3208, 1999. View at Publisher · View at Google Scholar · View at Scopus
- P. Webb, C. M. Anderson, C. Valentine et al., “The nuclear receptor corepressor (N-CoR) contains three isoleucine motifs (I/LXXII) that serve as receptor interaction domains (IDs),” Molecular Endocrinology, vol. 14, no. 12, pp. 1976–1985, 2000. View at Publisher · View at Google Scholar · View at Scopus
- M. G. Guenther, O. Barak, and M. A. Lazar, “The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3,” Molecular and Cellular Biology, vol. 21, no. 18, pp. 6091–6101, 2001. View at Publisher · View at Google Scholar · View at Scopus
- A. Codina, J. D. Love, Y. Li, M. A. Lazar, D. Neuhaus, and J. W. R. Schwabe, “Structural insights into the interaction and activation of histone deacetylase 3 by nuclear receptor corepressors,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 17, pp. 6009–6014, 2005. View at Publisher · View at Google Scholar · View at Scopus
- M. M. Montano, K. Ekena, R. Delage-Mourroux, W. Chang, P. Martini, and B. S. Katzenellenbogen, “An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 12, pp. 6947–6952, 1999. View at Publisher · View at Google Scholar · View at Scopus
- A. Mazumdar, R. A. Wang, S. K. Mishra et al., “Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor,” Nature Cell Biology, vol. 3, no. 1, pp. 30–37, 2001. View at Publisher · View at Google Scholar · View at Scopus
- N. Huang, E. Vom Baur, J. M. Garnier et al., “Two distinct nuclear receptor interaction domains in NSD1, a novel SET protein that exhibits characteristics of both corepressors and coactivators,” EMBO Journal, vol. 17, no. 12, pp. 3398–3412, 1998. View at Publisher · View at Google Scholar · View at Scopus
- R. I. Scheinman, A. Gualberto, C. M. Jewell, J. A. Cidlowski, and A. S. Baldwin, “Characterization of mechanisms involved in transrepression of NF-κB by activated glucocorticoid receptors,” Molecular and Cellular Biology, vol. 15, no. 2, pp. 943–953, 1995. View at Scopus
- N. Yap, C. L. Yu, and S. Y. Cheng, “Modulation of the transcriptional activity of thyroid hormone receptors by the tumor suppressor p53,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 9, pp. 4273–4277, 1996. View at Publisher · View at Google Scholar · View at Scopus
- G. G. Préfontaine, R. Walther, W. Giffin, M. E. Lemieux, L. Pope, and R. J. G. Haché, “Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter,” Journal of Biological Chemistry, vol. 274, no. 38, pp. 26713–26719, 1999. View at Publisher · View at Google Scholar · View at Scopus
- P. Delerive, K. De Bosscher, S. Besnard et al., “Peroxisome proliferator-activated receptor α negatively regulates the vascular inflammatory gene response by negative cross-talk with transcription factors NF-κB and AP-1,” Journal of Biological Chemistry, vol. 274, no. 45, pp. 32048–32054, 1999. View at Publisher · View at Google Scholar · View at Scopus
- L. H. Wang, X. Y. Yang, X. Zhang, et al., “Transcriptional inactivation of STAT3 by PPARg suppresses IL-6-responsive multiple myeloma cells,” Immunity, vol. 20, no. 2, pp. 205–218, 2004. View at Publisher · View at Google Scholar
- H. P. Kim, J. Y. Lee, J. K. Jeong, S. W. Bae, H. K. Lee, and I. Jo, “Nongenomic stimulation of nitric oxide release by estrogen is mediated by estrogen receptor α localized in caveolae,” Biochemical and Biophysical Research Communications, vol. 263, no. 1, pp. 257–262, 1999. View at Publisher · View at Google Scholar · View at Scopus
- M. L. Lu, M. C. Schneider, Y. Zheng, X. Zhang, and J. P. Richie, “Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation,” Journal of Biological Chemistry, vol. 276, no. 16, pp. 13442–13451, 2001. View at Publisher · View at Google Scholar · View at Scopus
- J. A. Huhtakangas, C. J. Olivera, J. E. Bishop, L. P. Zanello, and A. W. Norman, “The vitamin D receptor is present in caveolae-enriched plasma membranes and binds 1α,25(OH)2-vitamin D3in vivo and in Vitro,” Molecular Endocrinology, vol. 18, no. 11, pp. 2660–2671, 2004. View at Publisher · View at Google Scholar · View at Scopus
- L. Matthews, A. Berry, V. Ohanian, J. Ohanian, H. Garside, and D. Ray, “Caveolin mediates rapid glucocorticoid effects and couples glucocorticoid action to the antiproliferative program,” Molecular Endocrinology, vol. 22, no. 6, pp. 1320–1330, 2008. View at Publisher · View at Google Scholar · View at Scopus
- S. A. Mousa, L. J. O'Connor, J. J. Bergh, F. B. Davis, T. S. Scanlan, and P. J. Davis, “The proangiogenic action of thyroid hormone analogue GC-1 is initiated at an integrin,” Journal of Cardiovascular Pharmacology, vol. 46, no. 3, pp. 356–360, 2005. View at Publisher · View at Google Scholar · View at Scopus
- E. Karteris, S. Zervou, Y. Pang et al., “Progesterone signaling in human myometrium through two novel membrane G protein-coupled receptors: potential role in functional progesterone withdrawal at term,” Molecular Endocrinology, vol. 20, no. 7, pp. 1519–1534, 2006. View at Publisher · View at Google Scholar · View at Scopus
- J. L. Smith, B. R. Kupchak, I. Garitaonandia, et al., “Heterologous expression of human mPRα, mPRβ and mPRγ in yeast confirms their ability to function as membrane progesterone receptors,” Steroids, vol. 73, no. 11, pp. 1160–1173, 2008. View at Publisher · View at Google Scholar
- A. M. Nakhla, M. S. Khan, and W. Rosner, “Biologically active steroids activate receptor-bound human sex hormone-binding globulin to cause LNCaP cells to accumulate adenosine 3',5'-monophosphate,” Journal of Clinical Endocrinology and Metabolism, vol. 71, no. 2, pp. 398–404, 1990. View at Scopus
- A. M. Nakhla, J. Leonard, D. J. Hryb, and W. Rosner, “Sex hormone-binding globulin receptor signal transduction proceeds via a G protein,” Steroids, vol. 64, no. 3, pp. 213–216, 1999. View at Publisher · View at Google Scholar · View at Scopus
- E. A. Mitchell, M. B. Herd, B. G. Gunn, J. J. Lambert, and D. Belelli, “Neurosteroid modulation of GABAA receptors: molecular determinants and significance in health and disease,” Neurochemistry International, vol. 52, no. 4-5, pp. 588–595, 2008. View at Publisher · View at Google Scholar · View at Scopus
- F. Acconcia, P. Ascenzi, A. Bocedi et al., “Palmitoylation-dependent estrogen receptor α membrane localization: regulation by 17β-estradiol,” Molecular Biology of the Cell, vol. 16, no. 1, pp. 231–237, 2005. View at Publisher · View at Google Scholar · View at Scopus
- L. Li, M. P. Haynes, and J. R. Bender, “Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 8, pp. 4807–4812, 2003. View at Publisher · View at Google Scholar · View at Scopus
- G. A. Figtree, D. McDonald, H. Watkins, and K. M. Channon, “Truncated estrogen receptor α 46-kDa isoform in human endothelial cells: relationship to acute activation of nitric oxide synthase,” Circulation, vol. 107, no. 1, pp. 120–126, 2003. View at Publisher · View at Google Scholar · View at Scopus
- Z. Wang, X. Zhang, P. Shen, B. W. Loggie, Y. Chang, and T. F. Deuel, “A variant of estrogen receptor-α, hER-α36: transduction of estrogen- and antiestrogen-dependent membrane-initiated mitogenic signaling,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 24, pp. 9063–9068, 2006. View at Publisher · View at Google Scholar · View at Scopus
- M. Razandi, A. Pedram, and E. R. Levin, “Heat shock protein 27 is required for sex steroid receptor trafficking to and functioning at the plasma membrane,” Molecular and Cellular Biology, vol. 30, no. 13, pp. 3249–3261, 2010. View at Publisher · View at Google Scholar · View at Scopus
- A. Pedram, M. Razandi, R. J. Deschenes, and E. R. Levin, “DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors,” Molecular Biology of the Cell, vol. 23, no. 1, pp. 188–199, 2012. View at Publisher · View at Google Scholar
- A. Pedram, M. Razandi, R. C. A. Sainson, J. K. Kim, C. C. Hughes, and E. R. Levin, “A conserved mechanism for steroid receptor translocation to the plasma membrane,” Journal of Biological Chemistry, vol. 282, no. 31, pp. 22278–22288, 2007. View at Publisher · View at Google Scholar · View at Scopus
- G. Bondar, J. Kuo, N. Hamid, and P. Micevych, “Estradiol-induced estrogen receptor-α trafficking,” Journal of Neuroscience, vol. 29, no. 48, pp. 15323–15330, 2009. View at Publisher · View at Google Scholar · View at Scopus
- C. Buitrago and R. Boland, “Caveolae and caveolin-1 are implicated in 1α,25(OH)2-vitamin D3-dependent modulation of Src, MAPK cascades and VDR localization in skeletal muscle cells,” Journal of Steroid Biochemistry and Molecular Biology, vol. 121, no. 1-2, pp. 169–175, 2010. View at Publisher · View at Google Scholar · View at Scopus
- N. Bennett, J. D. Hooper, C. S. Lee, and G. C. Gobe, “Androgen receptor and caveolin-1 in prostate cancer,” IUBMB Life, vol. 61, no. 10, pp. 961–970, 2009. View at Publisher · View at Google Scholar · View at Scopus
- G. Zhao and R. U. Simpson, “Membrane localization, Caveolin-3 association and rapid actions of vitamin D receptor in cardiac myocytes,” Steroids, vol. 75, no. 8-9, pp. 555–559, 2010. View at Publisher · View at Google Scholar · View at Scopus
- Z. Schwartz, H. Ehland, V. L. Sylvia et al., “1α,25-dihydroxyvitamin D3 and 24R,25-dihydroxyvitamin D3 modulate growth plate chondrocyte physiology via protein kinase C-dependent phosphorylation of extracellular signal-regulated kinase 1/2 mitogen-activated protein kinase,” Endocrinology, vol. 143, no. 7, pp. 2775–2786, 2002. View at Publisher · View at Google Scholar · View at Scopus
- J. M. Vicencio, C. Ibarra, M. Estrada et al., “Testosterone induces an intracellular calcium increase by a nongenomic mechanism in cultured rat cardiac myocytes,” Endocrinology, vol. 147, no. 3, pp. 1386–1395, 2006. View at Publisher · View at Google Scholar · View at Scopus
- N. M. Storey, S. Gentile, H. Ullah et al., “Rapid signaling at the plasma membrane by a nuclear receptor for thyroid hormone,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 13, pp. 5197–5201, 2006. View at Publisher · View at Google Scholar · View at Scopus
- A. Zamoner, L. Heimfarth, S. O. Loureiro, C. Royer, F. R. M. B. Silva, and R. Pessoa-Pureur, “Nongenomic actions of thyroxine modulate intermediate filament phosphorylation in cerebral cortex of rats,” Neuroscience, vol. 156, no. 3, pp. 640–652, 2008. View at Publisher · View at Google Scholar · View at Scopus
- K. Elbaradie, Y. Wang, B. D. Boyan, and Z. Schwartz, “Rapid membrane responses to dihydrotestosterone are sex dependent in growth plate chondrocytes,” Journal of Steroid Biochemistry and Molecular Biology, vol. 132, no. 1-2, pp. 15–23, 2012. View at Publisher · View at Google Scholar
- D. Menegaz, A. Barrientos-Duran, A. Kline et al., “1α,25(OH)2-Vitamin D3 stimulation of secretion via chloride channel activation in Sertoli cells,” Journal of Steroid Biochemistry and Molecular Biology, vol. 119, no. 3–5, pp. 127–134, 2010. View at Publisher · View at Google Scholar · View at Scopus
- M. Druzin, E. Malinina, O. Grimsholm, and S. Johansson, “Mechanism of estradiol-induced block of voltage-gated K+ currents in rat medial preoptic neurons,” PLoS ONE, vol. 6, no. 5, article e20213, Article ID e20213, 2011. View at Publisher · View at Google Scholar · View at Scopus
- T. Simoncini, A. Hafezi-Moghadam, D. P. Brazil, K. Ley, W. W. Chin, and J. K. Llao, “Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase,” Nature, vol. 407, no. 6803, pp. 538–541, 2000. View at Publisher · View at Google Scholar · View at Scopus
- M. Pietrzak and M. Puzianowska-Kuznicka, “Triiodothyronine utilizes phosphatidylinositol 3-kinase pathway to activate anti-apoptotic myeloid cell leukemia-1,” Journal of Molecular Endocrinology, vol. 41, no. 3-4, pp. 177–186, 2008. View at Publisher · View at Google Scholar · View at Scopus
- T. D. Yan, H. Wu, H. P. Zhang, et al., “Oncogenic potential of retinoic acid receptor g in hepatocellular carcinoma,” Cancer Research, vol. 70, no. 6, pp. 2285–2295, 2010. View at Publisher · View at Google Scholar
- V. Boonyaratanakornkit, M. P. Scott, V. Ribon et al., “Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases,” Molecular Cell, vol. 8, no. 2, pp. 269–280, 2001. View at Publisher · View at Google Scholar · View at Scopus
- A. Migliaccio, L. Varricchio, A. De Falco et al., “Inhibition of the SH3 domain-mediated binding of Src to the androgen receptor and its effect on tumor growth,” Oncogene, vol. 26, no. 46, pp. 6619–6629, 2007. View at Publisher · View at Google Scholar · View at Scopus
- B. J. Cheskis, J. Greger, N. Cooch et al., “MNAR plays an important role in ERa activation of Src/MAPK and PI3K/Akt signaling pathways,” Steroids, vol. 73, no. 9-10, pp. 901–905, 2008. View at Publisher · View at Google Scholar · View at Scopus
- J. M. García-Pedrero, B. D. Rio, C. Martínez-Campa, M. Muramatsu, P. S. Lazo, and S. Ramos, “Calmodulin is a selective modulator of estrogen receptors,” Molecular Endocrinology, vol. 16, no. 5, pp. 947–960, 2002. View at Publisher · View at Google Scholar · View at Scopus
- L. Li, Z. Li, and D. B. Sacks, “The transcriptional activity of estrogen receptor-α is dependent on Ca2+/calmodulin,” Journal of Biological Chemistry, vol. 280, no. 13, pp. 13097–13104, 2005. View at Publisher · View at Google Scholar · View at Scopus
- M. Hentschke, C. Schulze, U. Süsens, and U. Borgmeyer, “Characterization of calmodulin binding to the orphan nuclear receptor ERRγ,” Biological Chemistry, vol. 384, no. 3, pp. 473–482, 2003. View at Publisher · View at Google Scholar · View at Scopus
- E. Cifuentes, J. M. Mataraza, B. A. Yoshida et al., “Physical and functional interaction of androgen receptor with calmodulin in prostate cancer cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 2, pp. 464–469, 2004. View at Publisher · View at Google Scholar · View at Scopus
- R. Alzamora, L. R. Brown, and B. J. Harvey, “Direct binding and activation of protein kinase C isoforms by aldosterone and 17β-estradiol,” Molecular Endocrinology, vol. 21, no. 11, pp. 2637–2650, 2007. View at Publisher · View at Google Scholar · View at Scopus
- R. Alzamora and B. J. Harvey, “Direct binding and activation of protein kinase C isoforms by steroid hormones,” Steroids, vol. 73, no. 9-10, pp. 885–888, 2008. View at Publisher · View at Google Scholar · View at Scopus
- C. Demonacos, N. C. Tsawdaroglou, R. Djordjevic-Markovic et al., “Import of the glucocorticoid receptor into rat liver mitochondria in vivo and in Vitro,” Journal of Steroid Biochemistry and Molecular Biology, vol. 46, no. 3, pp. 401–413, 1993. View at Publisher · View at Google Scholar · View at Scopus
- C. Wrutniak, I. Cassar-Malek, S. Marchal et al., “A 43-kDa protein related to c-Erb A α1 is located in the mitochondrial matrix of rat liver,” Journal of Biological Chemistry, vol. 270, no. 27, pp. 16347–16354, 1995. View at Publisher · View at Google Scholar · View at Scopus
- F. Casas, L. Domenjoud, P. Rochard et al., “A 45 kDa protein related to PPARγ2, induced by peroxisome proliferators, is located in the mitochondrial matrix,” FEBS Letters, vol. 478, no. 1-2, pp. 4–8, 2000. View at Publisher · View at Google Scholar · View at Scopus
- J. Q. Chen, M. Eshete, W. L. Alworth, and J. D. Yager, “Binding of MCF-7 cell mitochondrial proteins and recombinant human estrogen receptors α and β to human mitochondrial DNA estrogen response elements,” Journal of Cellular Biochemistry, vol. 93, no. 2, pp. 358–373, 2004. View at Publisher · View at Google Scholar · View at Scopus
- S. Arnold, F. Goglia, and B. Kadenbach, “3,5-Diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP,” European Journal of Biochemistry, vol. 252, no. 2, pp. 325–330, 1998. View at Scopus
- B. Notario, M. Zamora, O. Viñas, and T. Mampel, “All-trans-retinoic acid binds to and inhibits adenine nucleotide translocase and induces mitochondrial permeability transition,” Molecular Pharmacology, vol. 63, no. 1, pp. 224–231, 2003. View at Publisher · View at Google Scholar · View at Scopus
- K. Sterling and M. A. Brenner, “Thyroid hormone action: effect of triiodothyronine on mitochondrial adenine nucleotide translocase in vivo and in Vitro,” Metabolism, vol. 44, no. 2, pp. 193–199, 1995. View at Scopus
- B. Lin, S. K. Kolluri, F. Lin et al., “Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3,” Cell, vol. 116, no. 4, pp. 527–540, 2004. View at Publisher · View at Google Scholar · View at Scopus
- A. Horvat, S. Petrović, N. Nedeljković, J. V. Martinović, and G. Nikezić, “Estradiol affect Na-dependent Ca2+ efflux from synaptosomal mitochondria,” General Physiology and Biophysics, vol. 19, no. 1, pp. 59–71, 2000.
- N. Saelim, L. M. John, J. Wu et al., “Nontranscriptional modulation of intracellular Ca2+ siqnaling by ligand stimulated thyroid hormone receptor,” Journal of Cell Biology, vol. 167, no. 5, pp. 915–924, 2004. View at Publisher · View at Google Scholar · View at Scopus
- L. Zhang, R. Zhou, X. Li, R. J. Ursano, and H. Li, “Stress-induced change of mitochondria membrane potential regulated by genomic and non-genomic GR signaling: a possible mechanism for hippocampus atrophy in PTSD,” Medical Hypotheses, vol. 66, no. 6, pp. 1205–1208, 2006. View at Publisher · View at Google Scholar · View at Scopus
- M. M. Poon and L. Chen, “Retinoic acid-gated sequence-specific translational control by RARα,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 51, pp. 20303–20308, 2008. View at Publisher · View at Google Scholar · View at Scopus
- F. Buttgereit and A. Scheffold, “Rapid glucocorticoid effects on immune cells,” Steroids, vol. 67, no. 6, pp. 529–534, 2002. View at Publisher · View at Google Scholar · View at Scopus
- L. E. Panin, P. V. Mokrushnikov, V. G. Kunitsyn, and B. N. Zaitsev, “Interaction mechanism of cortisol and catecholamines with structural components of erythrocyte membranes,” Journal of Physical Chemistry B, vol. 114, no. 29, pp. 9462–9473, 2010. View at Publisher · View at Google Scholar · View at Scopus