Y. Akiyama, Y. Koda, S. Byeon, S. Shimada, T. Nishikawaji et al., Reduced expression of SET7/9, a histone mono-methyltransferase, is associated with gastric cancer progression, Oncotarget, vol.7, pp.3966-3983, 2015.

W. A. Alaynick, R. P. Kondo, W. Xie, W. He, C. R. Dufour et al., ERR? Directs and Maintains the Transition to Oxidative Metabolism in the Postnatal Heart, Cell Metab, vol.6, pp.13-24, 2007.

A. , C. D. Berger, S. L. Cote, J. Dent, S. Jenuwien et al., New Nomenclature for Chromatin-Modifying Enzymes, vol.131, pp.633-636, 2007.

S. Amente, L. Lania, and B. Majello, The histone LSD1 demethylase in stemness and cancer transcription programs, Biochim. Biophys. Acta BBA-Gene Regul. Mech, vol.1829, pp.981-986, 2013.

E. A. Ariazi, R. J. Kraus, M. L. Farrell, V. C. Jordan, and J. E. Mertz, Estrogen-Related Receptor ?1 Transcriptional Activities Are Regulated in Part via the ErbB2/HER2 Signaling Pathway, Mol. Cancer Res, vol.5, pp.71-85, 2007.

S. F. Arnold, M. Melamed, D. P. Vorojeikina, A. C. Notides, and S. Sasson, Estradiol-Binding Mechanism and Binding Capacity of the Human Estrogen Receptor Is Regulated by Tyrosine Phosphorylation, Mol. Endocrinol, vol.11, pp.48-53, 1997.

A. J. Bannister and T. Kouzarides, Reversing histone methylation, Nature, vol.436, pp.1103-1106, 2005.

P. Bardet, B. Horard, V. Laudet, and J. Vanacker, The ERR? orphan nuclear receptor controls morphogenetic movements during zebrafish gastrulation, Dev. Biol, vol.281, pp.102-111, 2005.

Á. P. Barrios, A. V. Gómez, J. E. Sáez, G. Ciossani, E. Toffolo et al., Differential Properties of Transcriptional Complexes Formed by the CoREST Family, Mol. Cell. Biol, vol.34, pp.2760-2770, 2014.

J. B. Barry, G. , and V. , Epidermal Growth Factor-Induced Signaling in Breast Cancer Cells Results in Selective Target Gene Activation by Orphan Nuclear Receptor Estrogen-Related Receptor ?, Cancer Res, vol.65, pp.6120-6129, 2005.

D. Barsyte-lovejoy, F. Li, M. J. Oudhoff, J. H. Tatlock, A. Dong et al., R)-PFI-2 is a potent and selective inhibitor of SETD7 methyltransferase activity in cells, Proc. Natl. Acad. Sci, vol.111, pp.12853-12858, 2014.

S. B. Baylin and P. A. Jones, A decade of exploring the cancer epigenome-biological and translational implications, Nat. Rev. Cancer, vol.11, pp.726-734, 2011.

C. Benner, S. Konovalov, C. Mackintosh, K. R. Hutt, R. Stunnenberg et al., , 2013.

, Decoding a Signature-Based Model of Transcription Cofactor Recruitment Dictated by Cardinal CisRegulatory Elements in Proximal Promoter Regions, PLOS Genet, vol.9, p.1003906

S. L. Berger, The complex language of chromatin regulation during transcription, p.119, 2007.

S. L. Berger, T. Kouzarides, R. Shiekhattar, and A. Shilatifard, An operational definition of epigenetics, Genes Dev, vol.23, pp.781-783, 2009.

B. E. Bernstein, T. S. Mikkelsen, X. Xie, M. Kamal, D. J. Huebert et al., A Bivalent Chromatin Structure Marks Key Developmental Genes in Embryonic Stem Cells, Cell, vol.125, pp.315-326, 2006.

S. Bhasin, L. Woodhouse, R. Casaburi, A. B. Singh, D. Bhasin et al., Testosterone dose-response relationships in healthy young men, Am. J. Physiol.-Endocrinol. Metab, vol.281, pp.1172-1181, 2001.

S. Bianco, O. Lanvin, V. Tribollet, C. Macari, S. North et al., Modulating Estrogen Receptor-related Receptor-? Activity Inhibits Cell Proliferation, J. Biol. Chem, vol.284, pp.23286-23292, 2009.

S. Bianco, J. Sailland, and J. Vanacker, ERRs and cancers: Effects on metabolism and on proliferation and migration capacities, J. Steroid Biochem. Mol. Biol, vol.130, pp.180-185, 2012.

E. Bonnelye and J. E. Aubin, Estrogen Receptor-Related Receptor ?: A Mediator of Estrogen Response in Bone, J. Clin. Endocrinol. Metab, vol.90, pp.3115-3121, 2005.

E. Bonnelye, J. M. Vanacker, N. Spruyt, S. Alric, B. Fournier et al., Expression of the estrogen-related receptor 1 (ERR-1) orphan receptor during mouse development, Mech. Dev, vol.65, pp.71-85, 1997.

E. Bonnelye, J. M. Vanacker, T. Dittmar, A. Begue, X. Desbiens et al., The ERR-1 Orphan Receptor Is a Transcriptional Activator Expressed During Bone Development, Mol. Endocrinol, vol.11, pp.905-916, 1997.

E. Bonnelye, L. Merdad, V. Kung, and J. E. Aubin, The Orphan Nuclear Estrogen Receptor-related Receptor ? (ERR?) Is Expressed throughout Osteoblast Differentiation and Regulates Bone Formation In Vitro
URL : https://hal.archives-ouvertes.fr/hal-02353236

M. V. Botuyan, J. Lee, I. M. Ward, J. Kim, J. R. Thompson et al., Structural Basis for the Methylation State-Specific Recognition of Histone H4-K20 by 53BP1 and Crb2 in DNA Repair, Cell, vol.127, pp.1361-1373, 2006.

D. Brasacchio, J. Okabe, C. Tikellis, A. Balcerczyk, P. George et al., Hyperglycemia Induces a Dynamic Cooperativity of Histone Methylase and Demethylase Enzymes Associated With Gene-Activating Epigenetic Marks That Coexist on the Lysine Tail, Diabetes, vol.58, pp.1229-1236, 2009.

A. O. Brinkmann and J. Trapman, Prostate cancer schemes for androgen escape, Nat. Med, vol.6, pp.628-629, 2000.

B. B. Busch, . Stevens, C. William, R. Martin, P. Ordentlich et al., Identification of a Selective Inverse Agonist for the Orphan Nuclear Receptor Estrogen-Related Receptor ?, J. Med. Chem, vol.47, pp.5593-5596, 2004.

N. Bushue, W. , and Y. Y. , Retinoid pathway and cancer therapeutics, Adv. Drug Deliv. Rev, vol.62, pp.1285-1298, 2010.

C. Cai, H. H. He, S. Chen, I. Coleman, H. Wang et al., Androgen Receptor Gene Expression in Prostate Cancer Is Directly Suppressed by the Androgen Receptor Through Recruitment of Lysine-Specific Demethylase 1, Cancer Cell, vol.20, pp.457-471, 2011.

S. Campaner, F. Spreafico, T. Burgold, M. Doni, U. Rosato et al., The Methyltransferase Set7/9 (Setd7) Is Dispensable for the p53-Mediated DNA Damage Response In Vivo, Mol. Cell, vol.43, pp.681-688, 2011.

R. A. Campbell, P. Bhat-nakshatri, N. M. Patel, D. Constantinidou, S. Ali et al., , 2001.

, Phosphatidylinositol 3-Kinase/AKT-mediated Activation of Estrogen Receptor ? A NEW MODEL FOR ANTI-ESTROGEN RESISTANCE, J. Biol. Chem, vol.276, pp.9817-9824

E. I. Campos, R. , and D. , Histones: Annotating Chromatin, Annu. Rev. Genet, vol.43, pp.559-599, 2009.

G. Cao, Y. Liang, C. L. Broderick, B. A. Oldham, T. P. Beyer et al., Antidiabetic Action of a Liver X Receptor Agonist Mediated By Inhibition of Hepatic Gluconeogenesis, J. Biol. Chem, vol.278, pp.1131-1136, 2003.

J. Carnesecchi and J. Vanacker, Estrogen-Related Receptors and the control of bone cell fate, Mol. Cell. Endocrinol, vol.432, pp.37-43, 2016.

A. Castet, A. Herledan, S. Bonnet, S. Jalaguier, J. Vanacker et al., ReceptorInteracting Protein 140 Differentially Regulates Estrogen Receptor-Related Receptor Transactivation Depending on Target Genes, Mol. Endocrinol, vol.20, pp.1035-1047, 2006.

S. K. Chakrabarti, J. Francis, S. M. Ziesmann, J. C. Garmey, and R. G. Mirmira, Covalent Histone Modifications Underlie the Developmental Regulation of Insulin Gene Transcription in Pancreatic ? Cells, J. Biol. Chem, vol.278, pp.23617-23623, 2003.

D. Chakravarti, V. J. Lamorte, M. C. Nelson, T. Nakajima, I. G. Schulman et al., Role of CBP/P300 in nuclear receptor signalling, Nature, vol.383, pp.99-103, 1996.

C. Charlot, H. Dubois-pot, T. Serchov, Y. Tourrette, and B. Wasylyk, A review of posttranslational modifications and subcellular localization of Ets transcription factors: possible connection with cancer and involvement in the hypoxic response, Methods Mol. Biol. Clifton NJ, vol.647, pp.3-30, 2010.

T. Chen, Overcoming drug resistance by regulating nuclear receptors, Adv. Drug Deliv. Rev, vol.62, pp.1257-1264, 2010.

D. Chen, P. E. Pace, R. C. Coombes, A. , and S. , Phosphorylation of Human Estrogen Receptor ? by Protein Kinase A Regulates Dimerization, Mol. Cell. Biol, vol.19, pp.1002-1015, 1999.

D. Chen, H. Ma, H. Hong, S. S. Koh, S. Huang et al., Regulation of Transcription by a Protein Methyltransferase, Science, vol.284, pp.2174-2177, 1999.

E. I. Chen, J. Hewel, J. S. Krueger, C. Tiraby, M. R. Weber et al., Adaptation of Energy Metabolism in Breast Cancer Brain Metastases, Cancer Res, vol.67, pp.1472-1486, 2007.

J. Chen, Y. Fu, D. S. Day, Y. Sun, S. Wang et al., VEGF amplifies transcription through ETS1 acetylation to enable angiogenesis, Nat. Commun, vol.8, p.383, 2017.

S. Chen, D. Zhou, C. Yang, T. Okubo, Y. Kinoshita et al., , 2001.

, Modulation of aromatase expression in human breast tissue, J. Steroid Biochem. Mol. Biol, vol.79, pp.35-40

S. Chen, D. Zhou, C. Yang, and M. Sherman, Molecular Basis for the Constitutive Activity of Estrogen-related Receptor ?-1, J. Biol. Chem, vol.276, pp.28465-28470, 2001.

Y. Chen, Y. Yang, F. Wang, K. Wan, K. Yamane et al., Crystal structure of human histone lysine-specific demethylase 1 (LSD1), Proc. Natl. Acad. Sci, vol.103, pp.13956-13961, 2006.

Y. Chen, P. Chi, S. Rockowitz, P. J. Iaquinta, T. Shamu et al., ETS factors reprogram the androgen receptor cistrome and prime prostate tumorigenesis in response to PTEN loss, Nat. Med, vol.19, pp.1023-1029, 2013.

Y. Chen, S. Yang, J. Hu, C. Yu, M. He et al., Increased Expression of SETD7 Promotes Cell Proliferation by Regulating Cell Cycle and Indicates Poor Prognosis in Hepatocellular Carcinoma, PLOS ONE, vol.11, p.154939, 2016.

P. Chi, C. D. Allis, W. , and G. G. , Covalent histone modifications-miswritten, misinterpreted and mis-erased in human cancers, Nat. Rev. Cancer, vol.10, pp.457-469, 2010.

M. J. Chisamore, M. E. Cunningham, O. Flores, H. A. Wilkinson, C. et al., Characterization of a Novel Small Molecule Subtype Specific Estrogen-Related Receptor ? Antagonist in MCF-7, Breast Cancer Cells. PLOS ONE, vol.4, p.5624, 2009.

M. J. Chisamore, H. A. Wilkinson, O. Flores, C. , and J. D. , Estrogen-related receptor-? antagonist inhibits both estrogen receptor-positive and estrogen receptor-negative breast tumor growth in mouse xenografts, Mol. Cancer Ther, vol.8, pp.672-681, 2009.

H. Cho, T. Suzuki, N. Dohmae, S. Hayami, M. Unoki et al., Demethylation of RB Regulator MYPT1 by Histone Demethylase LSD1 Promotes Cell Cycle Progression in Cancer Cells, Cancer Res, vol.71, pp.655-660, 2011.

S. Chuikov, J. K. Kurash, J. R. Wilson, B. Xiao, N. Justin et al., Regulation of p53 activity through lysine methylation, Nature, vol.432, pp.353-360, 2004.

P. A. Cloos, J. Christensen, K. Agger, and K. Helin, Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease, Genes Dev, vol.22, pp.1115-1140, 2008.

P. Costet, Y. Luo, N. Wang, and A. R. Tall, Sterol-dependent transactivation of the human ABC1 promoter by LXR/RXR, J. Biol. Chem, 2000.

J. Couture, E. Collazo, and R. C. Trievel, Molecular recognition of histone H3 by the WD40 protein WDR5, Nat. Struct. Mol. Biol, vol.13, pp.698-703, 2006.

J. Couture, E. Collazo, G. Hauk, and R. C. Trievel, Structural basis for the methylation site specificity of SET7/9, Nat. Struct. Mol. Biol, vol.13, pp.140-146, 2006.

P. Coward, D. Lee, M. V. Hull, and J. M. Lehmann, 4-Hydroxytamoxifen binds to and deactivates the estrogen-related receptor ?, Proc. Natl. Acad. Sci, vol.98, pp.8880-8884, 2001.

F. Crick, Central Dogma of Molecular Biology, Nature, vol.227, pp.561-563, 1970.

G. Deblois, G. , and V. , Functional and physiological genomics of estrogen-related receptors (ERRs) in health and disease, Biochim. Biophys. Acta BBA-Mol. Basis Dis, vol.1812, pp.1032-1040, 2011.

G. Deblois, G. , and V. , Oestrogen-related receptors in breast cancer: control of cellular metabolism and beyond, Nat. Rev. Cancer, vol.13, pp.27-36, 2013.

G. Deblois, J. A. Hall, M. Perry, J. Laganière, M. Ghahremani et al., , 2009.

, Genome-Wide Identification of Direct Target Genes Implicates Estrogen-Related Receptor ? as a Determinant of Breast Cancer Heterogeneity, Cancer Res, vol.69, pp.6149-6157

G. Deblois, G. Chahrour, M. Perry, G. Sylvain-drolet, W. J. Muller et al., , 2010.

, Transcriptional Control of the ERBB2 Amplicon by ERR? and PGC-1? Promotes Mammary Gland Tumorigenesis, Cancer Res, vol.70, pp.10277-10287

T. G. Deering, T. Ogihara, A. P. Trace, B. Maier, and R. G. Mirmira, , 2009.

, Maintains Transcription and Euchromatin Structure at Islet-Enriched Genes. Diabetes, vol.58, pp.185-193

M. Delmotte, A. Tahayato, P. Formstecher, and P. Lefebvre, Serine 157, a Retinoic Acid Receptor ? Residue Phosphorylated by Protein Kinase C in Vitro, Is Involved in RXR·RAR? Heterodimerization and Transcriptional Activity, J. Biol. Chem, vol.274, pp.38225-38231, 1999.

C. Dhalluin, J. E. Carlson, L. Zeng, C. He, A. K. Aggarwal et al., , 1999.

, Structure and ligand of a histone acetyltransferase bromodomain, Nature, vol.399, pp.491-496

A. Dhayalan, S. Kudithipudi, P. Rathert, J. , and A. , Specificity Analysis-Based Identification of New Methylation Targets of the SET7/9 Protein Lysine Methyltransferase, Chem. Biol, vol.18, pp.111-120, 2011.

S. C. Dillon, X. Zhang, R. C. Trievel, and X. Cheng, The SET-domain protein superfamily: protein lysine methyltransferases, Genome Biol, vol.6, p.227, 2005.

A. Diman, J. Boros, F. Poulain, J. Rodriguez, M. Purnelle et al., Nuclear respiratory factor 1 and endurance exercise promote human telomere transcription, Sci. Adv, vol.2, 2016.

J. Dittmer, The role of the transcription factor Ets1 in carcinoma, Semin. Cancer Biol, vol.35, pp.20-38, 2015.

S. Domcke, A. F. Bardet, A. Ginno, P. Hartl, D. Burger et al., Competition between DNA methylation and transcription factors determines binding of NRF1, Nature, vol.528, pp.575-579, 2015.

D. Duteil, E. Metzger, D. Willmann, P. Karagianni, N. Friedrichs et al., LSD1 promotes oxidative metabolism of white adipose tissue, Nat. Commun, vol.5, issue.123, 2014.

M. A. Dwyer, J. D. Joseph, H. E. Wade, M. L. Eaton, R. S. Kunder et al., WNT11 Expression Is Induced by Estrogen-Related Receptor ? and ?-Catenin and Acts in an Autocrine Manner to Increase Cancer Cell Migration, Cancer Res, vol.70, pp.9298-9308, 2010.

C. Ea and D. Baltimore, Regulation of NF-?B activity through lysine monomethylation of p65, Proc. Natl. Acad. Sci, vol.106, pp.18972-18977, 2009.

K. S. Egorova, O. M. Olenkina, and L. V. Olenina, Lysine methylation of nonhistone proteins is a way to regulate their stability and function, Biochem. Biokhimiia, vol.75, pp.535-548, 2010.

L. J. Eichner, G. , and V. , Estrogen related receptors (ERRs): A new dawn in transcriptional control of mitochondrial gene networks, Mitochondrion, vol.11, pp.544-552, 2011.

L. J. Eichner, M. Perry, C. R. Dufour, N. Bertos, M. Park et al., miR378 * Mediates Metabolic Shift in Breast Cancer Cells via the PGC-1?/ERR? Transcriptional Pathway, Cell Metab, vol.12, pp.352-361, 2010.

P. Estève, H. G. Chin, J. Benner, G. R. Feehery, M. Samaranayake et al., Regulation of DNMT1 stability through SET7-mediated lysine methylation in mammalian cells, Proc. Natl. Acad. Sci, vol.106, pp.5076-5081, 2009.

J. D. Eudy, S. Yao, M. D. Weston, M. Ma-edmonds, C. B. Talmadge et al., Isolation of a Gene Encoding a Novel Member of the Nuclear Receptor Superfamily from the Critical Region of Usher Syndrome Type IIa at 1q41, Genomics, vol.50, pp.382-384, 1998.

M. J. Evans and R. C. Scarpulla, Interaction of nuclear factors with multiple sites in the somatic cytochrome c promoter. Characterization of upstream NRF-1, ATF, and intron Sp1 recognition sequences, J. Biol. Chem, vol.264, pp.14361-14368, 1989.

M. J. Evans and R. C. Scarpulla, NRF-1: a trans-activator of nuclear-encoded respiratory genes in animal cells, Genes Dev, vol.4, pp.1023-1034, 1990.

C. Evans-molina, R. D. Robbins, T. Kono, S. A. Tersey, G. L. Vestermark et al., Peroxisome Proliferator-Activated Receptor ? Activation Restores Islet Function in Diabetic Mice through Reduction of Endoplasmic Reticulum Stress and Maintenance of Euchromatin Structure, Mol. Cell. Biol, vol.29, pp.2053-2067, 2009.

L. Fang, L. Zhang, W. Wei, X. Jin, P. Wang et al., A Methylation-Phosphorylation Switch Determines Sox2 Stability and Function in ESC Maintenance or Differentiation, Mol. Cell, vol.55, pp.537-551, 2014.

V. J. Findlay, A. C. Larue, D. P. Turner, P. M. Watson, and D. K. Watson, Chapter OneUnderstanding the Role of ETS-Mediated Gene Regulation in Complex Biological Processes, Advances in Cancer, pp.1-61, 2013.

F. Forneris, C. Binda, M. A. Vanoni, E. Battaglioli, and A. Mattevi, Human Histone Demethylase LSD1 Reads the Histone Code, J. Biol. Chem, vol.280, pp.41360-41365, 2005.

F. Foeis, C. Bida, A. Dallaglio, M. W. Faaije, E. Battaglioli et al., A Highl Specific Mechanism of Histone H3-K4 Recognition by Histone Demethylase LSD1, J. Biol. Chem, vol.281, pp.35289-35295

M. F. Fraga, E. Ballestar, M. F. Paz, S. Ropero, F. Setien et al., Epigenetic differences arise during the lifetime of monozygotic twins, Proc. Natl. Acad. Sci, vol.102, pp.10604-10609, 2005.

A. Fritah, M. Christian, P. , and M. G. , The metabolic coregulator RIP140: an update, Am. J. Physiol.-Endocrinol. Metab, vol.299, pp.335-340, 2010.

K. Fujimaki, T. Ogihara, D. L. Morris, H. Oda, H. Iida et al., SET7/9 Enzyme Regulates Cytokine-induced Expression of Inducible Nitricoxide Synthase through Methylation of Lysine 4 at Histone 3 in the Islet ? Cell, J. Biol. Chem, vol.290, pp.16607-16618, 2015.

S. Gaillard, M. A. Dwyer, and D. P. Mcdonnell, Definition of the Molecular Basis for Estrogen Receptor-Related Receptor-?-Cofactor Interactions, Mol. Endocrinol, vol.21, pp.62-76, 2007.

M. Gallet, S. Saïdi, E. Haÿ, J. Photsavang, C. Marty et al., Repression of Osteoblast Maturation by ERR? Accounts for Bone Loss Induced by Estrogen Deficiency, PLOS ONE, vol.8, p.54837, 2013.

W. Gao, Androgen receptor as a therapeutic target, Adv. Drug Deliv. Rev, vol.62, pp.1277-1284, 2010.

K. Garber, Energy Boost: The Warburg Effect Returns in a New Theory of Cancer, JNCI J. Natl. Cancer Inst, vol.96, pp.1805-1806, 2004.

I. Garcia-bassets, Y. Kwon, F. Telese, G. G. Prefontaine, K. R. Hutt et al., Histone Methylation-Dependent Mechanisms Impose Ligand Dependency for Gene Activation by Nuclear Receptors, Cell, vol.128, pp.505-518, 2007.

L. A. Garrett-sinha, Review of Ets1 structure, function, and roles in immunity, Cell. Mol. Life Sci, vol.70, pp.3375-3390, 2013.

M. Giaì, A. Baue, E. Gaaattii, P. Chaao, and C. Egl, Phospholatio pMAPK aad euittet of "UG-aae euied fo 'A-idued 'A'? degradation and transactivation, EMBO J, vol.21, pp.3760-3769

V. Giguère, Orphan Nuclear Receptors: From Gene to Function, Endocr. Rev, vol.20, pp.689-725, 1999.

V. Giguère, Transcriptional Control of Energy Homeostasis by the Estrogen-Related Receptors, Endocr. Rev, vol.29, pp.677-696, 2008.

V. Giguère, N. Yang, P. Segui, and R. M. Evans, Identification of a new class of steroid hormone receptors, Nature, vol.331, pp.91-94, 1988.

D. Gkikas, M. Tsampoula, and P. K. Politis, Nuclear receptors in neural stem/progenitor cell homeostasis, Cell. Mol. Life Sci, vol.74, pp.4097-4120, 2017.

E. L. Greer and Y. Shi, Histone methylation: a dynamic mark in health, disease and inheritance, Nat. Rev. Genet, vol.13, pp.343-357, 2012.

S. Gugneja and R. C. Scarpulla, Serine Phosphorylation within a Concise Amino-terminal Domain in Nuclear Respiratory Factor 1 Enhances DNA Binding, J. Biol. Chem, vol.272, pp.18732-18739, 1997.

J. C. Hahne, A. F. Okuducu, T. Fuchs, A. Florin, and N. Wernert, Identification of ETS-1 target genes in human fibroblasts, Int. J. Oncol, vol.38, pp.1645-1652, 2011.

M. Hakimi, D. A. Bochar, J. Chenoweth, W. S. Lane, G. Mandel et al., A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes, Proc. Natl. Acad. Sci, vol.99, pp.7420-7425, 2002.

M. Hakimi, Y. Dong, W. S. Lane, D. W. Speicher, and R. Shiekhattar, A Candidate X-linked Mental Retardation Gene Is a Component of a New Family of Histone Deacetylase-containing Complexes, J. Biol. Chem, vol.278, pp.7234-7239, 2003.

M. R. Hayden, S. M. Clee, A. Brooks-wilson, J. Genest, A. Attie et al., , 2000.

, Cholesterol efflux regulatory protein, Tangier disease and familial high-density lipoprotein deficiency

, Curr. Opin. Lipidol, vol.11, pp.117-122

S. He, D. R. Owen, S. A. Jelinsky, L. , and L. , Lysine Methyltransferase SETD7 (SET7/9) Regulates ROS Signaling through mitochondria and NFE2L2/ARE pathway, Sci. Rep, vol.5, p.14368, 2015.

Y. He, Y. Zhao, L. Wang, L. R. Bohrer, Y. Pan et al., LSD1 promotes Sphase entry and tumorigenesis via chromatin co-occupation with E2F1 and selective H3K9 demethylation, Oncogene, vol.37, pp.534-543, 2018.

P. C. Hollenhorst, A. A. Shah, C. Hopkins, and B. J. Graves, Genome-wide analyses reveal properties of redundant and specific promoter occupancy within the ETS gene family, Genes Dev, vol.21, pp.1882-1894, 2007.

R. Holliday, Epigenetics: An overview, Dev. Genet, vol.15, pp.453-457, 1994.

H. Hong, K. Kohli, A. Trivedi, D. L. Johnson, and M. R. Stallcup, GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors, Proc. Natl. Acad. Sci, vol.93, pp.4948-4952, 1996.

J. Huang, R. Sengupta, A. B. Espejo, M. G. Lee, J. A. Dorsey et al., Nature, vol.449, pp.105-108, 2007.

P. Huang, V. Chandra, R. , and F. , Structural Overview of the Nuclear Receptor Superfamily: Insights into Physiology and Therapeutics, Annu. Rev. Physiol, vol.72, pp.247-272, 2010.

S. Hummasti and P. Tontonoz, Adopting New Orphans into the Family of Metabolic Regulators, Mol. Endocrinol, vol.22, pp.1743-1753, 2008.

J. M. Huss, R. P. Kopp, K. , and D. P. , Peroxisome Proliferator-activated Receptor Coactivator1? (PGC-1?) Coactivates the Cardiac-enriched Nuclear Receptors Estrogen-related Receptor-? and-? IDENTIFICATION OF NOVEL LEUCINE-RICH INTERACTION MOTIF WITHIN PGC-1?, J. Biol. Chem, vol.277, pp.40265-40274, 2002.

J. M. Huss, K. Imahashi, C. R. Dufour, C. J. Weinheimer, M. Courtois et al., The Nuclear Receptor ERR? Is Required for the Bioenergetic and Functional Adaptation to Cardiac Pressure Overload, Cell Metab, vol.6, pp.25-37, 2007.

J. M. Huss, W. G. Garbacz, and W. Xie, Constitutive activities of estrogen-related receptors: Transcriptional regulation of metabolism by the ERR pathways in health and disease, Biochim. Biophys. Acta BBA-Mol. Basis Dis, vol.1852, pp.1912-1927, 2015.

M. Ichida, S. Nemoto, and T. Finkel, Identification of a Specific Molecular Repressor of the Peroxisome Proliferator-activated Receptor ? Coactivator-1 ? (PGC-1?), J. Biol. Chem, vol.277, pp.50991-50995, 2002.

E. Jablonka and E. Lamm, Commentary: The epigenotype-a dynamic network view of development, Int. J. Epidemiol, vol.41, pp.16-20, 2012.

R. H. Jacobson, A. G. Ladurner, D. S. King, and R. Tjian, Structure and Function of a Human TAFII250 Double Bromodomain Module, Science, vol.288, pp.1422-1425, 2000.

R. Jaenisch and A. Bird, Epigenetic regulation of gene expression: how the genome integrates intrinsic and environmental signals, Nat. Genet, vol.33, pp.245-254, 2003.

T. Jenuwein, G. Laible, R. Dorn, and G. Reuter, SET domain proteins modulate chromatin domains in eu-and heterochromatin, Cell. Mol. Life Sci. CMLS, vol.54, pp.80-93, 1998.

L. Jin, L. , and Y. , Structural and functional insights into nuclear receptor signaling, Adv. Drug Deliv. Rev, vol.62, pp.1218-1226, 2010.

Y. Jin, T. Y. Kim, M. S. Kim, M. A. Kim, S. H. Park et al., Nuclear import of human histone lysine-specific demethylase LSD1, J. Biochem. (Tokyo), vol.156, pp.305-313, 2014.

B. A. Jonas and M. L. Privalsky, SMRT and N-CoR Corepressors Are Regulated by Distinct Kinase Signaling Pathways, J. Biol. Chem, vol.279, pp.54676-54686, 2004.

J. Kallen, J. Schlaeppi, F. Bitsch, I. Filipuzzi, A. Schilb et al., Evidence for Ligand-independent Transcriptional Activation of the Human Estrogen-related Receptor ? (ERR?) CRYSTAL STRUCTURE OF ERR? LIGAND BINDING DOMAIN IN COMPLEX WITH PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR COACTIVATOR-1?, J. Biol. Chem, vol.279, pp.49330-49337, 2004.

Y. Kamei, H. Ohizumi, Y. Fujitani, T. Nemoto, T. Tanaka et al., PPAR? coactivator 1?/ERR ligand 1 is an ERR protein ligand, whose expression induces a high-energy expenditure and antagonizes obesity, Proc. Natl. Acad. Sci, vol.100, pp.12378-12383, 2003.

A. Kar and A. Gutierrez-hartmann, Molecular mechanisms of ETS transcription factormediated tumorigenesis, Crit. Rev. Biochem. Mol. Biol, vol.48, pp.522-543, 2013.

M. D. Kaas, Ö. D. I?ei, and U. Güdüz, Dug esistaat east cancer cells overexpress ETS1 gene, Biomed. Pharmacother, vol.64, pp.458-462

S. Kato, A. Yokoyama, and R. Fujiki, Nuclear receptor coregulators merge transcriptional coregulation with epigenetic regulation, Trends Biochem. Sci, vol.36, pp.272-281, 2011.

S. T. Keating, M. Ziemann, J. Okabe, A. W. Khan, A. Balcerczyk et al., Deep sequencing reveals novel Set7 networks, Cell. Mol. Life Sci, vol.71, pp.4471-4486, 2014.

E. T. Keller, W. B. Ershler, C. , and C. , The androgen receptor: a mediator of diverse responses, Front. Biosci. J. Virtual Libr, vol.1, pp.59-71, 1996.

D. P. Kelly and R. C. Scarpulla, Transcriptional regulatory circuits controlling mitochondrial biogenesis and function, Genes Dev, vol.18, pp.357-368, 2004.
DOI : 10.1101/gad.1177604
URL : http://genesdev.cshlp.org/content/18/4/357.full.pdf

E. Kim, W. Günther, K. Yoshizato, H. Meissner, S. Zapf et al., Tumor suppressor p53 inhibits transcriptional activation of invasion gene thromboxane synthase mediated by the proto-oncogenic factor ets-1, Oncogene, vol.22, pp.7716-7727, 2003.

S. Kim, H. Lee, K. Han, S. C. Kim, Y. Choi et al.,

, SET7/9 Methylation of the Pluripotency Factor LIN28A Is a Nucleolar Localization Mechanism that Blocks let-7 Biogenesis in Human ESCs, vol.15, pp.735-749

Y. Kim, H. J. Nam, J. Lee, D. Y. Park, C. Kim et al., Methylation-dependent regulation of HIF-1? stability restricts retinal and tumour angiogenesis, Nat. Commun, vol.7, p.10347, 2016.

S. Ko, J. Ahn, C. S. Song, S. Kim, K. Knapczyk-stwora et al., Lysine Methylation and Functional Modulation of Androgen Receptor by Set9 Methyltransferase, Mol. Endocrinol, vol.25, pp.433-444, 2011.

S. Kong, K. Kim, J. Kim, M. K. Kim, K. H. Lee et al., The ELK3-GATA3 axis orchestrates invasion and metastasis of breast cancer cells in vitro and in vivo, Oncotarget, vol.7, pp.65137-65146, 2016.

H. Kontaki and I. Talianidis, Lysine Methylation Regulates E2F1-Induced Cell Death, Mol. Cell, vol.39, pp.152-160, 2010.
DOI : 10.1016/j.molcel.2010.06.006
URL : https://doi.org/10.1016/j.molcel.2010.06.006

A. Kouskouti, E. Scheer, A. Staub, L. Tora, and I. Talianidis, Gene-Specific Modulation of TAF10 Function by SET9-Mediated Methylation, Mol. Cell, vol.14, pp.175-182, 2004.

P. Kunderfranco, M. Mello-grand, R. Cangemi, S. Pellini, A. Mensah et al., ETS Transcription Factors Control Transcription of EZH2 and Epigenetic Silencing of the Tumor Suppressor Gene Nkx3.1 in Prostate Cancer, PLOS ONE, vol.5, 2010.

J. K. Kurash, H. Lei, Q. Shen, W. L. Marston, B. W. Granda et al., Methylation of p53 by Set7/9 Mediates p53 Acetylation and Activity In Vivo, vol.29, pp.392-400, 2008.

T. Kwon, J. H. Chang, E. Kwak, C. W. Lee, A. Joachimiak et al., , 2003.

, EMBO J, vol.22, pp.292-303

M. Laahe, D. Ocaaoll, &. 'ea, K. Mehtle, and T. Jeuei, Methlatio of histoe H lysine 9 creates a binding site for HP1 proteins, Nature, vol.410, pp.116-120

B. A. Laffitte, L. C. Chao, J. Li, R. Walczak, S. Hummasti et al., adipose tissue. Proc. Natl. Acad. Sci, vol.100, pp.5419-5424, 2003.

R. B. Lanz, N. J. Mckenna, S. A. Onate, U. Albrecht, J. Wong et al., A Steroid Receptor Coactivator, SRA, Functions as an RNA and Is Present in an SRC-1 Complex, Cell, vol.97, pp.17-27, 1999.

G. M. Lee, L. W. Donaldson, M. A. Pufall, H. Kang, I. Pot et al., , 2005.

, The Structural and Dynamic Basis of Ets-1 DNA Binding Autoinhibition, J. Biol. Chem, vol.280, pp.7088-7099

J. Lee, J. Park, H. Choi, H. Won, H. -. Joo et al., LSD1 demethylates HIF1? to inhibit hydroxylation and ubiquitin-mediated degradation in tumor angiogenesis, Oncogene, vol.36, pp.5512-5521, 2017.

M. G. Lee, C. Wynder, N. Cooch, and R. Shiekhattar, An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation, Nature, vol.437, pp.432-435, 2005.

D. Leprince, A. Gegonne, J. Coll, C. De-taisne, A. Schneeberger et al., , 1983.

, A putative second cell-derived oncogene of the avian leukaemia retrovirus E26, Nature, vol.306, pp.395-397

E. Li, Chromatin modification and epigenetic reprogramming in mammalian development, Nat. Rev. Genet, vol.3, pp.662-673, 2002.

H. Li, P. J. Gomes, C. , and J. D. , RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2, Proc. Natl. Acad. Sci, vol.94, pp.8479-8484, 1997.
DOI : 10.1073/pnas.94.16.8479
URL : http://www.pnas.org/content/94/16/8479.full.pdf

H. Lin, S. Yeh, H. Kang, C. , and C. , Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor, Proc. Natl. Acad. Sci, vol.98, pp.7200-7205, 2001.
DOI : 10.1073/pnas.121173298
URL : http://europepmc.org/articles/pmc34646?pdf=render

T. Lin, A. Ponn, X. Hu, B. K. Law, L. et al., Requirement of the histone demethylase LSD1 in Snai1-mediated transcriptional repression during epithelial-mesenchymal transition, Oncogene, vol.29, p.4896, 2010.

M. D. Litt, M. Simpson, M. Gaszner, C. D. Allis, F. et al., Correlation Between Histone Lysine Methylation and Developmental Changes at the Chicken ?-Globin Locus, Science, vol.293, pp.2453-2455, 2001.

X. Liu, D. Wang, Y. Zhao, B. Tu, Z. Zheng et al.,

, Methyltransferase Set7/9 regulates p53 activity by interacting with Sirtuin 1 (SIRT1). Proc. Natl. Acad. Sci, vol.108, 1925.

X. Liu, Z. Chen, C. Xu, X. Leng, H. Cao et al., Repression of hypoxiainducible factor ? signaling by Set7-mediated methylation, Nucleic Acids Res, vol.43, pp.5081-5098, 2015.

D. M. Loaad and B. W. Omalle, Nuleaa 'eepto Coegulatos: Judges, Juies, aad Executioners of Cellular Regulation, Mol. Cell, vol.27, pp.691-700

G. Lu, Q. Zhang, Y. Huang, J. Song, R. Tomaino et al., Phosphorylation of ETS1 by Src Family Kinases Prevents Its Recognition by the COP1 Tumor Suppressor, Cancer Cell, vol.26, pp.222-234, 2014.

J. Luo, R. Sladek, J. Bader, A. Matthyssen, J. Rossant et al., Placental abnormalities in mouse embryos lacking the orphan nuclear receptor ERR-?, Nature, vol.388, pp.778-782, 1997.

A. V. Maganti, B. Maier, S. A. Tersey, M. L. Sampley, A. L. Mosley et al., Transcriptional Activity of the Islet ? Cell Factor Pdx1 Is Augmented by Lysine Methylation Catalyzed by the Methyltransferase Set7/9, J. Biol. Chem, vol.290, pp.9812-9822, 2015.

A. Maiques-diaz and T. C. Somervaille, LSD1: biologic roles and therapeutic targeting, Epigenomics, vol.8, pp.1103-1116, 2016.
DOI : 10.2217/epi-2016-0009
URL : http://europepmc.org/articles/pmc5066116?pdf=render

M. A. Majérus, F. Bibollet-ruche, J. B. Telliez, B. Wasylyk, and B. Bailleul, Serum, AP-1 and Ets-1 stimulate the human ets-1 promoter, Nucleic Acids Res, vol.20, pp.2699-2703, 1992.

H. Makkonen, T. Jääskeläinen, T. Pitkänen-arsiola, M. Rytinki, K. K. Waltering et al., Identification of ETS-like transcription factor 4 as a novel androgen receptor target in prostate cancer cells, Oncogene, vol.27, pp.4865-4876, 2008.

C. Marabelli, B. Marrocco, and A. Mattevi, The growing structural and functional complexity of the LSD1/KDM1A histone demethylase, Curr. Opin. Struct. Biol, vol.41, pp.135-144, 2016.

C. E. Massie, B. Adaa, N. L. Baaosa-moais, A. G. Lh, M. G. Taa et al., New androgen receptor genomic targets show an interaction with the ETS1 transcription factor, EMBO Rep, vol.8, pp.871-878, 2007.

F. E. May, Novel drugs that target the estrogen-related receptor alpha: their therapeutic potential in breast cancer, 2014.

I. J. Mcewan, Molecular mechanisms of androgen receptor-mediated gene regulation: structure-function analysis of the AF-1 domain, Endocr. Relat. Cancer, vol.11, pp.281-293, 2004.

N. J. Mkea and B. W. Omalle,

, Coiatoial Cottol of Gee Epessio Nulea Receptors and Coregulators. Cell, vol.108, pp.465-474

E. Metzger, M. Wissmann, N. Yin, J. M. Müller, R. Schneider et al., LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription, Nature, vol.437, p.436, 2005.

E. Metzger, A. Imhof, D. Patel, P. Kahl, K. Hoffmeyer et al., Phosphorylation of histone H3T6 by PKC? I controls demethylation at histone H3K4, Nature, vol.464, pp.792-796, 2010.

M. Meyer, H. Gronemeyer, B. Turcotte, M. Bocquel, D. Tasset et al., , 1989.

, Steroid hormone receptors compete for factors that mediate their enhancer function, Cell, vol.57, pp.433-442

N. Mosammaparast and Y. Shi, Reversal of Histone Methylation: Biochemical and Molecular Mechanisms of Histone Demethylases, Annu. Rev. Biochem, vol.79, pp.155-179, 2010.

S. Munro, N. Khaire, A. Inche, S. Carr, L. Thangue et al., Lysine methylation regulates the pRb tumour suppressor protein, Oncogene, vol.29, pp.2357-2367, 2010.

M. M. Musri, M. C. Carmona, F. A. Hanzu, P. Kaliman, R. Gomis et al., Histone Demethylase LSD1 Regulates Adipogenesis, J. Biol. Chem, vol.285, pp.30034-30041, 2010.

S. S. Nair, B. C. Nair, V. Cortez, D. Chakravarty, E. Metzger et al., PELP1 is a reader of histone H3 methylation that facilitates oestrogen eepto-? target gene activation by regulating lysine demethylase 1 specificity, EMBO Rep, vol.11, pp.438-444, 2010.

Z. Nawaz, D. M. Lonard, C. L. Smith, E. Lev-lehman, S. Y. Tsai et al.,

, The Angelman Syndrome-Associated Protein, E6-AP, Is a Coactivator for the Nuclear Hormone Receptor Superfamily, Mol. Cell. Biol, vol.19, pp.1182-1189

T. B. Nicholson, C. , and T. , LSD1 demethylates histone and non-histone proteins, Epigenetics, vol.4, pp.129-132, 2009.

K. Nishioka, S. Chuikov, K. Sarma, H. Erdjument-bromage, C. D. Allis et al., Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation, Genes Dev, vol.16, pp.479-489, 2002.

M. F. Nunn, P. H. Seeburg, C. Moscovici, and P. H. Duesberg, Tripartite structure of the avian erythroblastosis virus E26 transforming gene, Nature, vol.306, pp.391-395, 1983.

T. Oikawa and T. Yamada, Molecular biology of the Ets family of transcription factors, Gene, vol.303, pp.11-34, 2003.

B. Omalle, MINI'EVIEW: The "teoid 'eepto "upefaail: Moe Eiteet Pedicted for the Future, Mol. Endocrinol, vol.4, pp.363-369

S. A. Oñate, S. Y. Tsai, M. Tsai, and B. W. Omalle, euee aad Chaaaateizatio of a Coactivator for the Steroid Hormone Receptor Superfamily, Science, vol.270, pp.1354-1357

M. J. Oudhoff, S. A. Freeman, A. L. Couzens, F. Antignano, E. Kuznetsova et al., Control of the Hippo Pathway by Set7Dependent Methylation of Yap, Dev. Cell, vol.26, pp.188-194, 2013.

R. Pallai, A. Bhaskar, V. Sodi, R. , and L. M. , Ets1 and Elk1 transcription factors regulate cancerous inhibitor of protein phosphatase 2A expression in cervical and endometrial carcinoma cells, Transcription, vol.3, pp.323-335, 2012.

M. T. Pedersen and K. Helin, Histone demethylases in development and disease, Trends Cell Biol, vol.20, pp.662-671, 2010.

J. Pérez-schindler, S. Summermatter, S. Salatino, F. Zorzato, M. Beer et al., The Corepressor NCoR1 Antagonizes PGC-1? and Estrogen-Related Receptor ? in the Regulation of Skeletal Muscle Function and Oxidative Metabolism, Mol. Cell. Biol, vol.32, pp.4913-4924, 2012.

S. Pilotto, V. Speranzini, M. Tortorici, D. Durand, A. Fish et al., Interplay among nucleosomal DNA, histone tails, and corepressor CoREST underlies LSD1-mediated H3 demethylation, Proc. Natl. Acad. Sci, vol.112, pp.2752-2757, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01448118

S. Pradhan, H. G. Chin, P. Estève, and S. E. Jacobsen, SET7/9 mediated methylation of nonhistone proteins in mammalian cells, Epigenetics Off. J. DNA Methylation Soc, vol.4, pp.383-387, 2009.

M. G. Pray-grant, J. A. Daniel, D. Schieltz, J. R. Yates-iii, and P. A. Grant, Chd1 chromodomain links histone H3 methylation with SAGA-and SLIK-dependent acetylation, Nature, vol.433, pp.434-438, 2005.

B. N. Radde, M. M. Ivanova, H. X. Mai, N. Alizadeh-rad, K. Piell et al., Nuclear respiratory factor-1 and bioenergetics in tamoxifen-resistant breast cancer cells, Exp. Cell Res, vol.347, pp.593-599, 2000.

G. Reute and P. Spierer, Position effect variegation and chromatin proteins, BioEssays, vol.14, pp.605-612, 1992.

M. Robinson-rechavi, H. E. Garcia, and V. Laudet, The nuclear receptor superfamily, J. Cell Sci, vol.116, pp.585-586, 2003.

C. Rochette-egly, Nuclear receptors: integration of multiple signalling pathways through phosphorylation, Cell. Signal, vol.15, pp.355-366, 2003.

C. Rochette-egly, M. Oulad-abdelghani, A. Staub, V. Pfister, I. Scheuer et al., Phosphorylation of the retinoic acid receptor-alpha by protein kinase A, Mol. Endocrinol, vol.9, pp.860-871, 1995.

M. G. Rosenfeld, V. V. Lunyak, and C. K. Glass, Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response, Genes Dev, vol.20, pp.1405-1428, 2006.

A. J. Ruthenburg, W. Wang, D. M. Graybosch, H. Li, C. D. Allis et al., , 2006.

, Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex, Nat. Struct. Mol. Biol, vol.13, pp.704-712

J. Sailland, V. Tribollet, C. Forcet, C. Billon, B. Barenton et al., Estrogen-related receptor ? decreases RHOA stability to induce orientated cell migration, Proc. Natl. Acad. Sci, vol.111, pp.15108-15113, 2014.

H. Santos-rosa, R. Schneider, B. E. Bernstein, N. Karabetsou, A. Morillon et al., Methylation of Histone H3 K4 Mediates Association of the Isw1p ATPase with Chromatin, Mol. Cell, vol.12, pp.1325-1332, 2003.

R. C. Scarpulla, Nuclear control of respiratory gene expression in mammalian cells, J. Cell. Biochem, vol.97, pp.673-683, 2006.

R. C. Scarpulla, Transcriptional Paradigms in Mammalian Mitochondrial Biogenesis and Function, Physiol. Rev, vol.88, pp.611-638, 2008.

R. C. Scarpulla, Nuclear Control of Respiratory Chain Expression by Nuclear Respiratory Factors and PGC-1-Related Coactivator, Ann. N. Y. Acad. Sci, vol.1147, pp.321-334, 2008.

R. C. Scarpulla, Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network, Biochim. Biophys. Acta BBA-Mol. Cell Res, vol.1813, pp.1269-1278, 2011.

S. N. Schreiber, D. Knutti, K. Brogli, T. Uhlmann, and A. Kralli, The Transcriptional Coactivator PGC-1 Regulates the Expression and Activity of the Orphan Nuclear Receptor EstrogenRelated Receptor ? (ERR?), J. Biol. Chem, vol.278, pp.9013-9018, 2003.

I. G. Schulman, Nuclear receptors as drug targets for metabolic disease, Adv. Drug Deliv. Rev, vol.62, pp.1307-1315, 2010.

J. J. Seidel and B. J. Graves, An ERK2 docking site in the Pointed domain distinguishes a subset of ETS transcription factors, Genes Dev, vol.16, pp.127-137, 2002.

N. Serce, A. Gnatzy, S. Steiner, H. Lorenzen, J. Kirfel et al., Elevated expression of LSD1 (Lysine-specific demethylase 1) during tumour progression from pre-invasive to invasive ductal carcinoma of the breast, BMC Clin. Pathol, vol.12, p.13, 2012.

A. D. Sharrocks, The ETS-domain transcription factor family, Nat. Rev. Mol. Cell Biol, vol.2, pp.827-837, 2001.

C. Shen, D. Wang, X. Liu, B. Gu, Y. Du et al., , 2015.

, SET7/9 regulates cancer cell proliferation by influencing ?-catenin stability, FASEB J, vol.29, pp.4313-4323

X. Shi, T. Hong, K. L. Walter, M. Ewalt, E. Michishita et al., ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression, Nature, vol.442, pp.96-99, 2006.
URL : https://hal.archives-ouvertes.fr/hal-02154247

Y. Shi, F. Lan, C. Matson, P. Mulligan, J. R. Whetstine et al., , 2004.

, Histone Demethylation Mediated by the Nuclear Amine Oxidase Homolog LSD1, Cell, vol.119, pp.941-953

Y. Shi, C. Matson, F. Lan, S. Iwase, T. Baba et al., Regulation of LSD1 Histone Demethylase Activity by Its Associated Factors, Mol. Cell, vol.19, pp.857-864, 2005.

R. J. Sims, K. Nishioka, R. , and D. , Histone lysine methylation: a signature for chromatin function, Trends Genet, vol.19, pp.629-639, 2003.

R. J. Sims, C. Chen, H. Santos-rosa, T. Kouzarides, S. S. Patel et al., Human but Not Yeast CHD1 Binds Directly and Selectively to Histone H3 Methylated at Lysine 4 via Its Tandem Chromodomains, J. Biol. Chem, vol.280, pp.41789-41792, 2005.

A. K. Singh, M. Swarnalatha, and V. Kumar, c-ETS1 Facilitates G1/S-phase Transition by Upregulating Cyclin E and CDK2 Genes and Cooperates with Hepatitis B Virus X Protein for Their Deregulation, J. Biol. Chem, vol.286, pp.21961-21970, 2011.

M. J. Son, W. K. Kim, A. Park, K. Oh, J. Kim et al., Set7/9, a methyltransferase, regulates the thermogenic program during brown adipocyte differentiation through the modulation of p53 acetylation, Mol. Cell. Endocrinol, vol.431, pp.46-53, 2016.

J. Sonoda, J. Laganière, I. R. Mehl, G. D. Barish, L. Chong et al., Nuclear receptor ERR? and coactivator PGC-1? are effectors of IFN-?-induced host defense, Genes Dev, vol.21, 1909.

P. Stavropoulos, G. Blobel, and A. Hoelz, Crystal structure and mechanism of human lysinespecific demethylase-1, Nat. Struct. Mol. Biol, vol.13, p.626, 2006.

R. A. Stein and D. P. Mcdonnell, Estrogen-related receptor ? as a therapeutic target in cancer, 2006.

, Endocr. Relat. Cancer, vol.13, pp.25-32

M. M. Steward, J. Lee, A. Odooaa, M. Watt, B. E. Bestei et al.,

, Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes, Nat. Struct. Mol. Biol, vol.13, pp.852-854

B. D. Strahl, A. , and C. D. , The language of covalent histone modifications, Nature, vol.403, pp.41-45, 2000.

K. Subramanian, D. Jia, P. Kapoor-vazirani, D. R. Powell, R. E. Collins et al., Regulation of Estrogen Receptor ? by the SET7 Lysine Methyltransferase, 2008.

, Mol. Cell, vol.30, pp.336-347

G. Sun and Y. Shi, Nuclear receptors in stem cells and their therapeutic potential, Adv. Drug Deliv. Rev, vol.62, pp.1299-1306, 2010.

I. S. Tam, G. , and V. , There and back again: The journey of the estrogen-related receptors in the cancer realm, J. Steroid Biochem. Mol. Biol, vol.157, pp.13-19, 2016.

Y. Tao, R. L. Neppl, Z. Huang, J. Chen, R. Tang et al., The histone methyltransferase Set7/9 promotes myoblast differentiation and myofibril assembly, J. Cell Biol, vol.194, pp.551-565, 2011.

S. D. Taverna, H. Li, A. J. Ruthenburg, C. D. Allis, P. et al., How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers, Nat. Struct. Mol. Biol, vol.14, pp.1025-1040, 2007.

A. C. Tecalco-cruz, Molecular pathways involved in the transport of nuclear receptors from the nucleus to cytoplasm, J. Steroid Biochem. Mol. Biol, vol.178, pp.36-44, 2018.

R. Teperino, K. Schoonjans, A. , and J. , Histone Methyl Transferases and Demethylases, 2010.

, Can They Link Metabolism and Transcription?, Cell Metab, vol.12, pp.321-327

C. Teyssier, S. Bianco, O. Lanvin, and J. Vanacker, The orphan receptor ERR? interferes with steroid signaling, Nucleic Acids Res, vol.36, pp.5350-5361, 2008.

C. Teyssier, M. Gallet, B. Rabier, L. Monfoulet, J. Dine et al., Absence of ERR? in Female Mice Confers Resistance to Bone Loss Induced by Age or Estrogen-Deficiency. PLOS ONE 4, e7942, Mol. Biol. Cell, vol.17, pp.1643-1651, 2006.

F. H. Van-tienen, P. J. Lindsey, C. J. Van-der-kallen, and H. J. Smeets, Prolonged Nrf1 overexpression triggers adipocyte inflammation and insulin resistance, J. Cell. Biochem, vol.111, pp.1575-1585, 2010.

S. Tomar, J. P. Plotnik, J. Haley, J. Scantland, S. Dasari et al., ETS1 induction by the microenvironment promotes ovarian cancer metastasis through focal adhesion kinase, Cancer Lett, vol.414, pp.190-204, 2018.

G. B. Tremblay, T. Kunath, D. Bergeron, L. Lapointe, C. Champigny et al., Diethylstilbestrol regulates trophoblast stem cell differentiation as a ligand of orphan nuclear receptor ERR?, Genes Dev, vol.15, pp.833-838, 2001.

V. Tribollet, B. Barenton, A. Kroiss, S. Vincent, L. Zhang et al., miR-135a Inhibits the Invasion of Cancer Cells via Suppression of ERR?, PLOS ONE, vol.11, 2016.

N. K. Tuano, J. Okabe, M. Ziemann, M. E. Cooper, and A. El-osta, Set7 mediated interactions regulate transcriptional networks in embryonic stem cells, Nucleic Acids Res, vol.44, pp.9206-9217, 2016.

A. Urfer-buchwalder and R. Urfer, Identification of a Nuclear Respiratory Factor 1, 2017.

, Recognition Motif in the Apolipopotei E Vaaiaat APOE liked to Alzheies Disease, p.40668

J. M. Vanacker, C. Delmarre, X. Guo, and V. Laudet, Activation of the osteopontin promoter by the orphan nuclear receptor estrogen receptor related alpha, Cell Growth Differ, vol.9, p.1007, 1998.

J. Vanacker, K. Pettersson, J. Gustafsson, and V. Laudet, Transcriptional targets shaed estoge eepto-elated eeptos E''s aad estoge eepto E' ?, 1999.

, EMBO J, vol.18, pp.4270-4279

J. Vanacker, E. Bonnelye, S. Chopin-delannoy, C. Delmarre, V. Cavaillès et al., , 1999.

, Transcriptional Activities of the Orphan Nuclear Receptor ERR? (Estrogen Receptor-Related Receptor-?), Mol. Endocrinol, vol.13, pp.764-773

R. A. Varier and H. T. Timmers, Histone lysine methylation and demethylation pathways in cancer, Biochim. Biophys. Acta BBA-Rev. Cancer, vol.1815, pp.75-89, 2011.

J. A. Villena and A. Kralli, ERR?: a metabolic function for the oldest orphan, Trends Endocrinol. Metab, vol.19, pp.269-276, 2008.

J. A. Villena, M. B. Hock, W. Y. Chang, J. E. Barcas, V. Giguère et al., Orphan nuclear receptor estrogen-related receptor ? is essential for adaptive thermogenesis, Proc. Natl. Acad. Sci, vol.104, pp.1418-1423, 2007.

C. A. Virbasius, J. V. Virbasius, and R. C. Scarpulla, NRF-1, an activator involved in nuclearmitochondrial interactions, utilizes a new DNA-binding domain conserved in a family of developmental regulators, Genes Dev, vol.7, pp.2431-2445, 1993.

E. H. Vu, R. J. Kraus, and J. E. Mertz, Phosphorylation-Dependent Sumoylation of EstrogenRelated Receptor ?1, Biochemistry (Mosc.), vol.46, pp.9795-9804, 2007.

B. L. Wagner, A. F. Valledor, G. Shao, C. L. Daige, E. D. Bischoff et al., Promoter-Specific Roles for Liver X Receptor/Corepressor Complexes in the Regulation of ABCA1 and SREBP1 Gene Expression, Mol. Cell. Biol, vol.23, pp.5780-5789, 2003.

D. Wang, J. Zhou, X. Liu, D. Lu, C. Shen et al., , 2013.

, Methylation of SUV39H1 by SET7/9 results in heterochromatin relaxation and genome instability, Proc. Natl. Acad. Sci, vol.110, pp.5516-5521

H. Wang, R. Cao, L. Xia, H. Erdjument-bromage, C. Borchers et al., Purification and Functional Characterization of a Histone H3-Lysine 4-Specific Methyltransferase, Mol. Cell, vol.8, pp.1207-1217, 2001.

J. Wang, S. Hevi, J. K. Kurash, H. Lei, F. Gay et al., The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation, Nat. Genet, vol.41, p.125, 2009.

J. Wang, S. Hevi, J. K. Kurash, H. Lei, F. Gay et al., The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation, Nat. Genet, vol.41, pp.125-129, 2009.

Y. Wang, H. Zhang, Y. Chen, Y. Sun, F. Yang et al., , 2009.

, Is a Subunit of the NuRD Complex and Targets the Metastasis Programs in Breast Cancer, Cell, vol.138, pp.660-672

P. Webb, C. M. Anderson, C. Valentine, P. Nguyen, A. Marimuthu et al., The Nuclear Receptor Corepressor (N-CoR) Contains Three Isoleucine Motifs (I/LXXII) That Serve as Receptor Interaction Domains (IDs), Mol. Endocrinol, vol.14, pp.1976-1985, 2000.

A. L. Webster, M. S. Yan, and P. A. Marsden, Epigenetics and Cardiovascular Disease, 2013.

, J. Cardiol, vol.29, pp.46-57

M. Wiench, T. B. Miranda, and G. L. Hager, Control of nuclear receptor function by local chromatin structure, FEBS J, vol.278, pp.2211-2230, 2011.

P. J. Willy, I. R. Murray, J. Qian, B. B. Busch, W. C. Stevens et al., Regulation of PPAR? coactivator 1? (PGC-1?) signaling by an estrogenrelated receptor ? (ERR?) ligand, Proc. Natl. Acad. Sci, vol.101, pp.8912-8917, 2004.

B. J. Wilson, A. M. Tremblay, G. Deblois, G. Sylvain-drolet, G. et al., An Acetylation Switch Modulates the Transcriptional Activity of Estrogen-Related Receptor ?, Mol. Endocrinol, vol.24, pp.1349-1358, 2010.

J. R. Wilson, C. Jing, P. A. Walker, S. R. Martin, S. A. Howell et al., Crystal Structure and Functional Analysis of the Histone Methyltransferase SET7/9, vol.111, pp.105-115, 2002.

M. Wissmann, N. Yin, J. M. Müller, H. Greschik, B. D. Fodor et al., Cooperative demethylation by JMJD2C and LSD1 promotes androgen receptor-dependent gene expression, Nat. Cell Biol, vol.9, p.347, 2007.

A. P. Wolffe, H. , and J. J. , Chromatin disruption and modification, Nucleic Acids Res, vol.27, pp.711-720, 1999.

F. Wu, J. Wang, Y. Wang, T. Kwok, S. Kong et al., Estrogen-related receptor ? (ERR?) inverse agonist XCT-790 induces cell death in chemotherapeutic resistant cancer cells, Chem. Biol. Interact, vol.181, pp.236-242, 2009.

R. Wu, Q. Feng, D. M. Lonard, and B. W. Omalle, C-3 Coactivator Functional Lifetime Is Regulated by a Phospho-Dependent Ubiquitin Time Clock, Cell, vol.129, pp.1125-1140

Y. Wu, Y. Wang, X. H. Yang, T. Kang, Y. Zhao et al., The Deubiquitinase USP28 Stabilizes LSD1 and Confers Stem-Cell-like Traits to, Breast Cancer Cells. Cell Rep, vol.5, pp.224-236, 2013.

J. Wysocka, T. Swigut, H. Xiao, T. A. Milne, S. Y. Kwon et al., A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling, Nature, vol.442, pp.86-90, 2006.

B. Xiao, C. Jing, J. R. Wilson, P. A. Walker, N. Vasisht et al., Structure and catalytic mechanism of the human histone methyltransferase SET7/9, Nature, vol.421, pp.652-656, 2003.

W. Xie, Development of novel therapeutic strategy by regulating the nuclear hormone receptors, Adv. Drug Deliv. Rev, vol.62, p.1217, 2010.

M. Yang, C. B. Gocke, X. Luo, D. Borek, D. R. Tomchick et al., Structural Basis for CoREST-Dependent Demethylation of Nucleosomes by the Human LSD1, 2006.

, Histone Demethylase. Mol. Cell, vol.23, pp.377-387

Y. Yarden and M. X. Sliwkowski, Untangling the ErbB signalling network, Nat. Rev. Mol. Cell Biol, vol.2, pp.127-137, 2001.

H. Yoon, D. W. Chan, Z. Huang, J. Li, J. D. Fondell et al., Purification and futioal haateizatio of the huaa N-Co' ople: the oles of HDAC, TBL aad TBL, EMBO J, vol.22, pp.1336-1346, 2003.

S. K. Yoshinaga, C. L. Peterson, I. Herskowitz, and K. R. Yamamoto, Roles of SWI1, SWI2, and SWI3 proteins for transcriptional enhancement by steroid receptors, Science, vol.258, pp.1598-1604, 1992.

A. You, J. K. Tong, C. M. Grozinger, and S. L. Schreiber, CoREST is an integral component of the CoREST-human histone deacetylase complex, Proc. Natl. Acad. Sci, vol.98, pp.1454-1458, 2001.

P. Zegerman, B. Canas, D. Pappin, and T. Kouzarides, Histone H3 Lysine 4 Methylation Disrupts Binding of Nucleosome Remodeling and Deacetylase (NuRD) Repressor Complex, J. Biol. Chem, vol.277, pp.11621-11624, 2002.

Z. Zhang and C. T. Teng, Estrogen Receptor-related Receptor ?1 Interacts with Coactivator and Constitutively Activates the Estrogen Response Elements of the Human Lactoferrin Gene, J. Biol. Chem, vol.275, pp.20837-20846, 2000.

J. Zhang, C. Wang, X. Chen, M. Takada, C. Fan et al.,

, EglN assoiates ith the N'F-PGC? complex and controls mitochondrial function in breast cancer, EMBO J, vol.34, pp.2953-2970

L. Zhang, Q. Ding, W. , and Z. , Nuclear Respiratory Factor 1 Mediates the Transcription Initiation of Insulin-Degrading Enzyme in a TATA Box-Binding Protein-Independent Manner, PLOS ONE, vol.7, 2012.

X. Zhang, H. Wen, and X. Shi, Lysine methylation: beyond histones, Acta Biochim. Biophys. Sin, vol.44, pp.14-27, 2012.
DOI : 10.1093/abbs/gmr100
URL : https://academic.oup.com/abbs/article-pdf/44/1/14/4228/gmr100.pdf

Y. Zhang, J. Liu, J. Lin, L. Zhou, Y. Song et al., The transcription factor GATA1 and the histone methyltransferase SET7 interact to promote VEGFmediated angiogenesis and tumor growth and predict clinical outcome of breast cancer, Oncotarget, vol.7, pp.9859-9875, 2016.

L. Zhao, M. Tang, Z. Hu, B. Yan, W. Pi et al., miR504 mediated down-regulation of nuclear respiratory factor 1 leads to radio-resistance in nasopharyngeal carcinoma, Oncotarget, vol.6, pp.15995-16018, 2015.

Y. Zheng, J. Ma, Z. Wang, J. Li, B. Jiang et al., A Systematic Review of Histone Lysine-Specific Demethylase 1 and Its Inhibitors, Med. Res. Rev, vol.35, pp.1032-1071, 2015.

L. Zhang, C. Cerutti, E. Lambert, B. Barenton, C. Forcet et al., The lysine methyltransferase SET7/9 regulates cell invasion capacity by modulating ERR?s transcriptional activity

L. Zhang, S. Vincent, C. Cerutti, C. Forcet, V. Tribollet et al., LSD1-ERR? complex requires NRF1 to positively regulate transcription and cell invasion, Scientific Report, vol.8, p.10041, 2018.
DOI : 10.1038/s41598-018-27676-8
URL : https://www.nature.com/articles/s41598-018-27676-8.pdf

J. Carnesecchia, *. , C. Forcet, *. , L. Zhang et al., ERR? drives H3K9 demethylation by LSD1 to promote cell invasion, Proceedings of the National Academy of Sciences, vol.114, p.3909, 2017.

*. Co,

L. Zhang, J. Wong, and J. Vanacker, The Estrogen-related receptors (ERRs): potential targets against bone loss, Cell. Mol. Life Sci, vol.73, pp.3781-3787, 2016.
DOI : 10.1007/s00018-016-2328-5

V. Tribollet, B. Barenton, A. Kroiss, S. Vincent, L. Zhang et al., Séverine Périan, Nathalie Allioli1, Jacques Samarut

, PLOS ONE, vol.11, issue.5, p.156445

L. Fang, J. Zhang, H. Zhang, X. Yang, X. Jin et al., , pp.565-580, 2016.

L. Fang, L. Zhang, W. Wei, X. Jin, P. Wang et al., A methylation-phosphorylation switch determines sox2 stability and function in ESC maintenance or differentiation, Conference: 2015:5th Meeting on Nuclear Receptor, vol.55, pp.537-551, 2014.
DOI : 10.1016/j.molcel.2014.06.018
URL : https://doi.org/10.1016/j.molcel.2014.06.018

, For luciferase assays, cells were cotransfected with CMV-?Gal plasmid. Luciferase activity was normalized to that of ?-galactosidase. Cells were harvested 48 h after transfection. SiRNA sequences are shown in Table S2.E R R ? deletion mut a n t sa sw e l la sE R R E-L u c i f e r a s ep l a s mids have been described elsewhere (55). Detailed materials and methods are provided in SI Materials and Methods. ACKNOWLEDGMENTS. This work was funded by, MDA-MB231 and HEK293T cells were cultured in DMEM supplemented with 10% FCS, 10 U/mL penicillin, and 10 ?g/mL streptomycin

J. , is funded by Association pour la Recherche sur le Cancer (ARC). L.Z. is funded by the Chinese Scolarship Council (CSC) and Région

B. Li, M. Carey, and J. L. Workman, The role of chromatin during transcription, Cell, vol.128, issue.4, pp.707-719, 2007.

T. Jenuwein and C. D. Allis, Translating the histone code, Science, vol.293, issue.5532, pp.1074-1080, 2001.

M. G. Rosenfeld, V. V. Lunyak, and C. K. Glass, Sensors and signals: A coactivator/ corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response, Genes Dev, vol.20, issue.11, pp.1405-1428, 2006.

T. Kouzarides, Chromatin modifications and their function, Cell, vol.128, issue.4, pp.693-705, 2007.

Y. Shi and J. R. Whetstine, Dynamic regulation of histone lysine methylation by demethylases, Mol Cell, vol.25, issue.1, pp.1-14, 2007.

P. A. Cloos, J. Christensen, K. Agger, and K. Helin, Erasing the methyl mark: Histone demethylases at the center of cellular differentiation and disease, Genes Dev, vol.22, issue.9, pp.1115-1140, 2008.

S. C. Kampranis and P. N. Tsichlis, Histone demethylases and cancer, Adv Cancer Res, vol.102, pp.103-169, 2009.

S. Lim, E. Metzger, R. Schüle, J. Kirfel, and R. Buettner, Epigenetic regulation of cancer growth by histone demethylases, Int J Cancer, vol.127, issue.9, pp.1991-1998, 2010.

E. L. Greer and Y. Shi, Histone methylation: A dynamic mark in health, disease and inheritance, Nat Rev Genet, vol.13, issue.5, pp.343-357, 2012.

Y. Shi, Histone demethylation mediated by the nuclear amine oxidase homolog LSD1, Cell, vol.119, issue.7, pp.941-953, 2004.

Y. J. Shi, Regulation of LSD1 histone demethylase activity by its associated factors, Mol Cell, vol.19, issue.6, pp.857-864, 2005.

Y. Wang, LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer, Cell, vol.138, issue.4, pp.660-672, 2009.

E. Metzger, LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription, Nature, vol.437, issue.7057, pp.436-439, 2005.

E. Metzger, Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4, Nature, vol.464, issue.7289, pp.792-796, 2010.

C. Cai, Lysine-specific demethylase 1 has dual functions as a major regulator of androgen receptor transcriptional activity, Cell Reports, vol.9, issue.5, pp.1618-1627, 2014.

C. Benner, Decoding a signature-based model of transcription cofactor recruitment dictated by cardinal cis-regulatory elements in proximal promoter regions, PLoS Genet, vol.9, issue.11, p.1003906, 2013.

D. Duteil, LSD1 promotes oxidative metabolism of white adipose tissue, Nat Commun, vol.5, p.4093, 2014.

A. Adamo, LSD1 regulates the balance between self-renewal and differentiation in human embryonic stem cells, Nat Cell Biol, vol.13, issue.6, pp.652-659, 2011.

W. A. Whyte, Enhancer decommissioning by LSD1 during embryonic stem cell differentiation, Nature, vol.482, issue.7384, pp.221-225, 2012.

M. M. Musri, Histone demethylase LSD1 regulates adipogenesis, J Biol Chem, vol.285, issue.39, pp.30034-30041, 2010.

P. Kahl, Androgen receptor coactivators lysine-specific histone demethylase 1 and four and a half LIM domain protein 2 predict risk of prostate cancer recurrence, Cancer Res, vol.66, issue.23, pp.11341-11347, 2006.

J. H. Schulte, Lysine-specific demethylase 1 is strongly expressed in poorly differentiated neuroblastoma: Implications for therapy, Cancer Res, vol.69, issue.5, pp.2065-2071, 2009.

S. Lim, Lysine-specific demethylase 1 (LSD1) is highly expressed in ERnegative breast cancers and a biomarker predicting aggressive biology, Carcinogenesis, vol.31, issue.3, pp.512-520, 2010.

T. Lin, A. Ponn, X. Hu, B. K. Law, and J. Lu, Requirement of the histone demethylase LSD1 in Snai1-mediated transcriptional repression during epithelial-mesenchymal transition, Oncogene, vol.29, issue.35, pp.4896-4904, 2010.

S. Hayami, Overexpression of LSD1 contributes to human carcinogenesis through chromatin regulation in various cancers, Int J Cancer, vol.128, issue.3, pp.574-586, 2011.

V. Laudet and H. Gronemeyer, The Nuclear Receptor Factbook (Academic, 2002.

V. Perissi, K. Jepsen, C. K. Glass, and M. G. Rosenfeld, Deconstructing repression: Evolving models of co-repressor action, Nat Rev Genet, vol.11, issue.2, pp.109-123, 2010.

S. Kato, A. Yokoyama, and R. Fujiki, Nuclear receptor coregulators merge transcriptional coregulation with epigenetic regulation, Trends Biochem Sci, vol.36, issue.5, pp.272-281, 2011.

V. Giguère, Orphan nuclear receptors: From gene to function, Endocr Rev, vol.20, issue.5, pp.689-725, 1999.

B. Horard and J. M. Vanacker, Estrogen receptor-related receptors: Orphan receptors desperately seeking a ligand, J Mol Endocrinol, vol.31, issue.3, pp.349-357, 2003.

V. Giguère, Transcriptional control of energy homeostasis by the estrogenrelated receptors, Endocr Rev, vol.29, issue.6, pp.677-696, 2008.

J. A. Villena and A. Kralli, ERRalpha: A metabolic function for the oldest orphan, Trends Endocrinol Metab, vol.19, issue.8, pp.269-276, 2008.

A. Charest-marcotte, The homeobox protein Prox1 is a negative modulator of ERR?/PGC-1? bioenergetic functions, Genes Dev, vol.24, issue.6, pp.537-542, 2010.

J. Pérez-schindler, The corepressor NCoR1 antagonizes PGC-1? and estrogen-related receptor ? in the regulation of skeletal muscle function and oxidative metabolism, Mol Cell Biol, vol.32, issue.24, pp.4913-4924, 2012.

E. A. Ariazi and V. C. Jordan, Estrogen-related receptors as emerging targets in cancer and metabolic disorders, Curr Top Med Chem, vol.6, issue.3, pp.203-215, 2006.

A. Fradet, Dual function of ERR? in breast cancer and bone metastasis formation: Implication of VEGF and osteoprotegerin, Cancer Res, vol.71, issue.17, pp.5728-5738, 2011.

M. A. Dwyer, WNT11 expression is induced by estrogen-related receptor alpha and beta-catenin and acts in an autocrine manner to increase cancer cell migration, Cancer Res, vol.70, issue.22, pp.9298-9308, 2010.

J. Sailland, Estrogen-related receptor ? decreases RHOA stability to induce orientated cell migration, Proc Natl Acad Sci, vol.111, issue.42, pp.15108-15113, 2014.

V. Tribollet, miR-135a inhibits the invasion of cancer cells via suppression of ERR?, PLoS One, vol.11, issue.5, p.156445, 2016.

S. Bianco, J. Sailland, and J. M. Vanacker, ERRs and cancers: Effects on metabolism and on proliferation and migration capacities, J Steroid Biochem Mol Biol, vol.130, issue.3-5, pp.180-185, 2012.

G. Deblois and V. Giguère, Oestrogen-related receptors in breast cancer: Control of cellular metabolism and beyond, Nat Rev Cancer, vol.13, issue.1, pp.27-36, 2013.

C. Chaveroux, Molecular and genetic crosstalks between mTOR and ERR? are key determinants of rapamycin-induced nonalcoholic fatty liver, Cell Metab, vol.17, issue.4, pp.586-598, 2013.

G. Ferrari-amorotti, Inhibiting interactions of lysine demethylase LSD1 with snail/slug blocks cancer cell invasion, Cancer Res, vol.73, issue.1, pp.235-245, 2013.

G. Shao, Lysine-specific demethylase 1 mediates epidermal growth factor signaling to promote cell migration in ovarian cancer cells, Sci Rep, vol.5, p.15344, 2015.

A. Page-mccaw, A. J. Ewald, and Z. Werb, Matrix metalloproteinases and the regulation of tissue remodelling, Nat Rev Mol Cell Biol, vol.8, issue.3, pp.221-233, 2007.

I. Garcia-bassets, Histone methylation-dependent mechanisms impose ligand dependency for gene activation by nuclear receptors, Cell, vol.128, issue.3, pp.505-518, 2007.
DOI : 10.1016/j.cell.2006.12.038
URL : https://doi.org/10.1016/j.cell.2006.12.038

M. Wissmann, Cooperative demethylation by JMJD2C and LSD1 promotes androgen receptor-dependent gene expression, Nat Cell Biol, vol.9, issue.3, pp.347-353, 2007.
DOI : 10.1038/ncb1546

B. Perillo, DNA oxidation as triggered by H3K9me2 demethylation drives estrogen-induced gene expression, Science, vol.319, issue.5860, pp.202-206, 2008.
DOI : 10.1126/science.1147674

E. Metzger, Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation, Nat Cell Biol, vol.10, issue.1, pp.53-60, 2008.

S. S. Nair, PELP1 is a reader of histone H3 methylation that facilitates oestrogen receptor-alpha target gene activation by regulating lysine demethylase 1 specificity, EMBO Rep, vol.11, issue.6, pp.438-444, 2010.

Y. Chen, Crystal structure of human histone lysine-specific demethylase 1 (LSD1), Proc Natl Acad Sci, vol.103, issue.38, pp.13956-13961, 2006.
DOI : 10.1073/pnas.0606381103
URL : http://www.pnas.org/content/103/38/13956.full.pdf

N. Serce, Elevated expression of LSD1 (Lysine-specific demethylase 1) during tumour progression from pre-invasive to invasive ductal carcinoma of the breast, BMC Clin Pathol, vol.12, p.13, 2012.

R. S. Derr, High nuclear expression levels of histone-modifying enzymes LSD1, HDAC2 and SIRT1 in tumor cells correlate with decreased survival and increased relapse in breast cancer patients, BMC Cancer, vol.14, p.604, 2014.

S. Nagasawa, LSD1 overexpression is associated with poor prognosis in basal-like breast cancer, and sensitivity to PARP inhibition, PLoS One, vol.10, issue.2, p.118002, 2015.
DOI : 10.1371/journal.pone.0118002
URL : https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0118002&type=printable

J. M. Vanacker, Transcriptional activities of the orphan nuclear receptor ERR alpha (estrogen receptor-related receptor-alpha), Mol Endocrinol, vol.13, issue.5, pp.764-773, 1999.

M. V. Petoukhov, Reconstruction of quaternary structure from X-ray scattering by equilibrium mixtures of biological macromolecules, Biochemistry, vol.52, issue.39, pp.6844-6855, 2013.

,

. Carnesecchi,

, Supporting Information Carnesecchi et al

, For proliferation assays, 10 4 siRNAtransfected cells were seeded in 96-well plates. Cell viability was determined 48 h after transfection using CellTiterGlo kit (Promega) under the manufacturer's recommendations. For invasion assays, 5×10 4 cells were suspended in 200 ?L DMEM/2% FCS and seeded on top of matrigel invasion chambers (Corning), SI Materials and Methods Cell Culture and Transfection

, Beads were then added to the extract and incubated for 1 h, washed 5 times with Nonidet P-40 buffer, and finally resuspended in Laemmli buffer for immunoblotting analysis. We analyzed 50 ?g of wholecell lysate as input fraction. For GST pull-down assays, GST-tagged proteins were produced from BL-21 (DE3) bacterial strain, purified on Gluthatione-Agarose beads (Sigma), and quantified by Coomassie staining, Interaction Assays. For coimmunoprecipitation assays, cells were harvested in PBS, and pellets were resuspended in Nonidet P-40 buffer (20 mM Tris, pH 7.5, 150 mM NaCl, 2 mM EDTA, 1% Nonidet P-40) supplemented with protease inhibitor mixture

;. Triton and D. Pmsf, HeLa nuclear extracts or ERR? produced in vitro with rabbit reticulocyte lysate (Promega) were subfraction. For proximity ligation assays, cells cultured on coverslips were fixed with 4% paraformaldehyde (Merck) for 10 min at room temperature, mM EDTA) supplemented with NaCl, vol.2

, Bioscience) according to the recommendations provided by the manufacturer using anti-LSD1 or anti-ERR? antibodies. Samples were Dapi-counterstained. Images were acquired using a Zeiss AxioImager microscope

, For production in insect cells, full-length ERR? (2-422) was cloned into pDEST8 vector containing a C-terminal hexahistidine tag and expressed in Sf9 or Sf21 insect cells using the baculovirus technology. For production in bacteria, full-length ERR? was cloned into pnEAvHX vector containing an N-terminal hexahistidine tag as well as a TrxA fusion moiety and expressed in BL21 Escherichia coli. For purification, harvested cells were resuspended in lysis buffer (20 mM Tris·HCl, pH 8, 400 mM NaCl, 10% glycerol, 2 mM CHAPS, 5 mM imidazole, cOmplete EDTA-free protease inhibitor mixture tablet; Roche Applied Science), sonicated, and centrifuged. The supernatant was loaded on 5 mL HisTrapp FF crude column (GE Healthcare). The protein was eluted at 250 mM imidazole and further purified by SEC on Superdex S200 (16/60 and 10/300, GE Healthcare) column. Purity and homogeneity of the protein were assessed by SDS/PAGE, and complex formation was monitored by native PAGE. For the demethylation assays, bulk histones were incubated with purified LSD1 and/or ERR? and NRF1 in the demethylase activity assay buffer (50 mM Tris, pH8.8, 50 mM KCl, 5 mM MgCl2, 0.5% BSA, 5% glycerol) for 18 h at 30 °C, Vitro Demethylation Assay. In vitro demethylation assays were performed on bulk histones (Sigma-Aldrich), using purified LSD1 (Enzo-Lifesciences; cat. no. BML-SE544) with or without ERR? translated in vitro using the reticulocyte lysate system (Promega) or recombinant ERR? produced as described (56)

, Proteins (25-50 ?g) were resolved on 8-15% SDS/PAGE, blotted onto PVDF membrane (GE-Healthcare), and probed with specific antibodies after saturation. The antibodies (and their dilution) used in this study were as follows: ERR? (GTX108166, Genetex, 1/5,000), Western Blot Analysis. For Western blot analysis, cells were lysed in Nonidet P-40 or RIPA buffer supplemented with Protease Inhibitor Mixture

, Real-time PCR was performed in a 96-well plate using the IQ SYBR Green Supermix (Biorad). Data were quantified by the ??-Ct method and normalized to 36b4 expression

, Illumina. Sequences were aligned on the human genome (hg19, GRCh37 version) using TopHat. Read counts were determined using HT-seq. Differentially expressed genes were identified with DESeq2 R package, using an adjusted P value (padj) < 0.05. Genes showing significantly modified expression in at least one siRNA experiment were gathered together for hierarchical clustering (Cluster 3.0) and heatmap representation (Java TreeView 1.1.6r4). Clustering used the euclidian distance and the average linkage method applied to log twofold changes, RNA Sequencing and Bioinformatic Analysis. RNAs were extracted from two independent replicates from MDA-MB231 cells (transfected with siRNAs) using Qiagen RNA extraction kit. RNA quality was assessed using BioAnalyzer 2100TM (Agilent Technologies), 2000.

C. , Lysates from 5 × 10 6 cells were incubated with 5 ?g of antibody overnight at 4 °C on rotation and then for 1 h with 40 ?L of Dynabead-protein G (Life Technology), We cross-linked 10 × 10 6 cells with 1% formaldehyde and quenched them for 5 min in 0.125 M Glycine

. Carnesecchi,

. Fig and . S1, RT-qPCR results are presented relative to control conditions with bars representing mean ± SEM of three independent experiments performed in triplicate. hsp90 and actin were used as a loading control in Western blots. (C) Cell viability was determined 48 h after transfection with the indicated siRNAs. Data are expressed relative to control-transfected cells. Bars represent mean ± SEM of two independent experiments in triplicate. (D) Expression of the indicated genes after siERR? or siLSD1 transfection analyzed by RT-qPCR and presented relative to control conditions. Bars represent mean ± SEM of three independent experiments performed in triplicate. (E) Cells were transfected with siLSD1 or siERR?, alone or in combination. Expression of the indicated genes was analyzed by RT-qPCR and is presented relative to control conditions. Bars represent mean ± SEM is shown for individual siRNA (siLSD1 or siERR?) relative to combined siRNA (siLSD1 + siERR?). (F) Binding of ERR? on the ERREs of the indicated genes analyzed by ChIP followed by qPCR. Percent enrichment relative to input is shown using antiERR? or IgG as a control. Bindings of ERR? on a proximal (but not distal) element of its own promoter were used as positive and negative controls, respectively. (G) Binding of ERR? on the TSSs of the indicated genes analyzed by ChIP followed by qPCR. Percent enrichment relative to input is shown using anti-ERR? or, Common transcriptional targets of ERR? and LSD1. (A and B) Cells transfected with siRNAs directed against LSD1 (A) or ERR? (B) were analyzed for expression of the indicated genes by RT-qPCR (Left) or Western blots (Right)

. Fig and . S2, Expression of the indicated genes in HEK293T cells after siERR? or siLSD1 treatment analyzed by RT-qPCR and expressed relative to 36b4. Note that all studied genes respond to ERR? and LSD1 in a similar manner in HEK293T and MDAMB231 cells with the exception of LEF1 (not regulated by either factor) and TMEM198, the expression of which was not

*. ,

*. **p-&lt;-0,

. Carnesecchi,

. Fig and . S3, Cells inactivated for LSD1 (siLSD1#1 and #2) or not (siC) were transfected with ERRE-luciferase plasmid together with increasing amounts of ERR?-encoding plasmid. Results were normalized to samples transfected by ERRE-luciferase only. Bars show the mean ± SEM of three independent experiments performed in triplicate. (B) Detection of H3K4me2 and H3K9me2 at the TSSs of the indicated genes analyzed by ChIP. IgG was used as a control. Enrichments are presented relative to total H3 with bars representing mean ± SEM of three independent experiments performed in duplicate. (C) Detection of H3K9me2 at the ERREs of the indicated gene after siRNA-mediated inactivation of ERR? or LSD1. Results are expressed relative to control conditions with bars showing the mean of two independent experiments performed in triplicate, ERR? transcriptional activity depends on LSD1 and controls for ChIP assays. (A)

*. **p-&lt;-0, 005; ns, nonsignificant. Carnesecchi et al

. Fig and . S4, ERR? mutants were detected in Western blot using flagM2 antibody. (B) In vitro demethylation assay with the same representation as Fig. 3A with supplementation by in vitro translated NRF1. (C) Control of the purity of recombinant ERR? (recERR?) used in Fig. 3B. Shown is a Coomassie blue staining of a gel loaded with the indicated amounts of recombinant ERR? or BSA used as a control. (D) Demethylation assay detecting H3K9me2 similar to Fig. 3A (for Left) and Fig. 3B (for Right) with supplementation of tranylcypromine (TCP), an LSD1 inhibitor. (E) Demethylation assay detecting H3K4me2 and H3K9me2, using recombinant LSD1 and ERR? (recHis6x-Trx-ERR?) purified from bacteria. Right shows a Coomassie blue staining of a gel loaded with the indicated amounts of recombinant ERR? and BSA used as a control. (F) Proximity ligation assays using anti-LSD1, Controls for demethylation and interaction assays. (A) Demethylation assay detecting H3K9me2 similar to Fig

. Carnesecchi,

, Significance is shown as P values above the bars. (C)S i m i l a rt oF i g .4 E using cells treated with the indicated siRNAs. (D)S i m i l a rt oF i g .4 B, analyzing the expression of MMP11 and MMP14 after treatment with the indicated siRNA. No variation (relative to control siRNA) was found significant.( E) Binding of ERR? or LSD1 on the indicated MMP1 promoter regions analyzed by ChIP. Percent enrichment is shown relative to input with IgG used as a control. Bars representmean± SEM of three independent experiments performed in duplicate. (F) Detection of H3K4me2 and H3K9me2 on the TSS of MMP1 gene. Conditions and representation are similar to Fig. S3B.(G) Expression of the indicated genes in MDA-MB231 or HEK293T cells determined by RT-qPCR is shown relative to that of the housekeeping gene 36b4, Fig. S5. ERR? and LSD1 induce cell migration in an MMP1-dependent manner. (A) Extended list of enriched GO terms in ERR?-LSD1 common targets. Numbers correspond to the representation in Fig. 4A.-log10(P value) is indicated as enrichment level

*. **p-&lt;-0,

. Scientific-reports-|, , vol.8, p.10041, 2018.

, resulting in transcriptional activation of a set of common target genes. However, how are the LSD1-TF and, in particular LSD1-ERR?, complexes determined to act at TSSs is not understood. Here we show that promoter-bound nuclear respiratory factor 1 (NRF1), but not ERR?, is essential to LSD1 recruitment at the TSSs of positive LSD1-ERR? targets. In contrast to ERR?, NRF1 does of gene expression is achieved by transcription factors (TFs) that bind to promoters and/or to discrete genomic sites (enhancers) located more or less distal, upstream or downstream, from the transcriptional start sites (TSSs) of the genes they regulate 1-3. hese TFs recruit, amongst others, co-activator proteins that modify histone tails. he latter activities are oten exerted at the TSSs of the targeted genes, and eventually lead to the induction of consistent transcriptional programs that regulate distinct physiopathological traits. How are enhancer-promoter dialogs inely regulated and, in particular, what are the determinants at the TSSs that instruct TF-Co-A complexes where to act are unclear. Lysine Speciic Demethylase 1 (LSD1; KDM1A) is an enzyme that demethylates histone and non-histone substrates and exerts dual activities on histone H3 (H3) 4-11. By demethylating mono-and dimethyl Lys4 on histone H3 (H3K4), LSD1 induces transcriptional repression. In contrast, when demethylating mono-and dimethyl H3K9, LSD1 acts as a transcriptional co-activator, promoting the expression of its target genes. LSD1 can be recruited by various TFs at their cognate response element, including in enhancer regions, and can exert its activities at enhancers and/or TSSs 12-16. he Nuclear Respiratory Factor 1 (NRF1) TF has been suggested as a key factor to tether LSD1 to TSSs and, together with LSD1, induces the expression of genes involved in oxidative phosphorylation in white adipose tissue 17,18. However, the relationships of the LSD1-NRF1 complex with upstream bound TFs are not understood. he Estrogen-Related Receptor ? (ERR?) is an orphan member of the nuclear receptor TF family 19 that regulates various physiopathological features, Lysine-speciic demethylase 1 (LSD1) exerts dual efects on histone H3, promoting transcriptional repression via Lys4 (H3K4) demethylation or transcriptional activation through Lys9 (H3K9) demethylation. These activities are often exerted at transcriptional start sites (TSSs) and depend on the type of enhancer-bound transcription factor (TFs) with which LSD1 interacts

, Correspondence and requests for materials should be addressed to

. Scientific-reports-|, For siRNA transfection, 3.10 ?5 cells per ml were seeded in 6-well plate and 25 pmol/ml of total siRNA were transfected with INTERFERin (Polyplus Transfection) according to the manufacturer's recommendations. Plasmid transfections were performed with JetPrime (Polyplus Transfection). siRNAs were from Invitrogen (ERR?, LSD1) or Eurogentec (NRF1) and sequences are shown on Supplementary Table 1. For invasion assays, 5.10 4 cells were suspended in 200 µl DMEM/2% FCS and seeded on top of matrigel invasion chambers (Corning). Cells were allowed to migrate toward the lower chamber containing DMEM/10% FCS for 48 h. Matrigel was removed using cotton buds and cells were ixed 1 h with 4% formaldehyde, coloured with 0.1% crystal violet, and microphotographed. Cell-covered surfaces were quantiied using ImageJ, | DOI:./sMethods Cells. MDA-MB231 and HEK293T cells were cultured in DMEM supplemented with 10% FCS, 10 U/ml penicillin and 10 µg/ml streptomycin, vol.8, p.10041, 2018.

, GE-Healthcare) and probed with speciic antibodies ater saturation. he antibodies (and their dilution) used in this study were: hsp90 (API-SPA-830, Protease Inhibitor Cocktail (Sigma-Aldrich). Proteins (25-50 µg) were resolved on 8 to 15% SDS-PAGE, blotted onto PVDF membrane

, centrifugation, cell pellets were resuspended in lysis bufer (1% SDS, 50 mM Tris-HCl pH8, 10 mM EDTA). used: Histone H3 (ab1791, Abcam), H3K4me2 (07-030, Millipore) and H3K9me2 (39753, ActiveMotif)

S. Heinz, C. E. Romanoski, C. Benner, and C. K. Glass, he selection and function of cell type-speciic enhancers, Nat Rev Mol Cell Biol, vol.16, pp.144-154, 2015.

M. A. Zabidi and A. Stark, Regulatory enhancer-core-promoter communication via transcription factors and cofactors, Trends Genet, vol.32, pp.801-814, 2016.

F. Reiter, S. Wienerroither, and A. Stark, Combinatorial function of transcription factors and cofactors, Curr Opin Genet Dev, vol.43, pp.73-81, 2017.

Y. Shi, Histone demethylation mediated by the nuclear amine oxidase homolog LSD1, Cell, vol.119, pp.941-953, 2004.

Y. J. Shi, Regulation of LSD1 histone demethylase activity by its associated factors, Mol Cell, vol.19, pp.857-864, 2005.

E. Metzger, LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription, Nature, vol.437, pp.436-439, 2005.

C. Cai, Lysine-speciic demethylase 1 has dual functions as a major regulator of androgen receptor transcriptional activity, Cell Rep, vol.9, pp.1618-1627, 2014.

I. Garcia-bassets, Histone methylation-dependent mechanisms impose ligand dependency for gene activation by nuclear receptors, Cell, vol.128, pp.505-518, 2007.

J. Huang, p53 is regulated by the lysine demethylase LSD1, Nature, vol.449, pp.105-108, 2007.

J. Wang, he lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation, Nat Genet, vol.41, pp.125-129, 2009.

H. Kontaki and I. Talianidis, Lysine methylation regulates E2F1-induced cell death, Mol Cell, vol.39, pp.152-160, 2010.

I. Scionti, LSD1 controls timely MyoD expression via MyoD core enhancer transcription. Cell Rep, vol.18, 1996.

. Scientific-reports-|, , vol.8, p.10041, 2018.

A. Sambeat, LSD1 interacts with Zfp516 to promote UCP1 transcription and brown fat program, Cell Rep, vol.15, pp.2536-2549, 2016.

D. Duteil, Lsd1 ablation triggers metabolic reprogramming of brown adipose tissue, Cell Rep, vol.17, pp.1008-1021, 2016.

J. Carnesecchi, ERR? induces H3K9 demethylation by LSD1 to promote cell invasion, Proc Natl Acad Sci, vol.114, pp.3909-3914, 2017.

T. Boulding, LSD1 activation promotes inducible EMT programs and modulates the tumour microenvironment in breast cancer, Sci Rep, vol.8, 2018.

C. Benner, Decoding a signature-based model of transcription cofactor recruitment dictated by cardinal cis-regulatory elements in proximal promoter regions, PLoS Genet, vol.9, 2013.

D. Duteil, LSD1 promotes oxidative metabolism of white adipose tissue, Nat Commun, vol.5, 2014.

B. Horard and J. M. Vanacker, Estrogen receptor-related receptors: orphan receptors desperately seeking a ligand, J Mol Endocrinol, vol.31, pp.349-357, 2003.

J. A. Villena and A. Kralli, ERRalpha: a metabolic function for the oldest orphan, Trends Endocrinol Metab, vol.19, pp.269-276, 2008.

V. Giguère, Transcriptional control of energy homeostasis by the estrogen-related receptors, Endocr Rev, vol.29, pp.677-696, 2008.

L. J. Eichner, miR-378( * ) mediates metabolic shit in breast cancer cells via the PGC-1?/ERR? transcriptional pathway, Cell Metab, vol.12, pp.352-361, 2010.

M. A. Dwyer, WNT11 expression is induced by estrogen-related receptor alpha and beta-catenin and acts in an autocrine manner to increase cancer cell migration, Cancer Res, vol.70, pp.9298-9308, 2010.

A. Fradet, Dual function of ERR? in breast cancer and bone metastasis formation: implication of VEGF and osteoprotegerin, Cancer Res, vol.71, pp.5728-5738, 2011.

C. Zou, ERR? augments HIF-1 signalling by directly interacting with HIF-1? in normoxic and hypoxic prostate cancer cells, J Pathol, vol.233, pp.61-73, 2014.

J. Sailland, Estrogen-related receptor ? decreases RHOA stability to induce orientated cell migration, Proc Natl Acad Sci, vol.111, pp.15108-15013, 2014.

V. Tribollet, miR-135a inhibits the invasion of cancer cells via suppression of ERR?, PLoS One, vol.11, 2016.

S. Bianco, J. Sailland, and J. M. Vanacker, ERRs and cancers: efects on metabolism and on proliferation and migration capacities, J Steroid Biochem Mol Biol, vol.130, pp.180-185, 2012.

G. Deblois and V. Giguère, Oestrogen-related receptors in breast cancer: control of cellular metabolism and beyond, Nat Rev Cancer, vol.13, pp.27-36, 2013.

R. S. Derr, High nuclear expression levels of histone-modifying enzymes LSD1, HDAC2 and SIRT1 in tumor cells correlate with decreased survival and increased relapse in breast cancer patients, BMC Cancer, vol.14, p.604, 2014.

S. Nagasawa, LSD1 overexpression is associated with poor prognosis in basal-like breast cancer, and sensitivity to PARP inhibition, PLoS One, vol.10, p.118002, 2015.

K. Kim, ROR?2 requires LSD1 to enhance tumor progression in breast cancer, Sci Rep, vol.7, p.11994, 2017.

J. Carnesecchi, C. Cerutti, J. M. Vanacker, and C. Forcet, ERR? protein is stabilized by LSD1 in a demethylation-independent manner, PLoS One, vol.12, 2017.

W. Gao, Increased expression of mitochondrial transcription factor A and nuclear respiratory factor-1 predicts a poor clinical outcome of breast cancer, Oncol Lett, vol.15, pp.1449-1458, 2018.

R. C. Scarpulla, R. B. Vega, and D. P. Kelly, Transcriptional integration of mitochondrial biogenesis, Trends Endocrinol Metab, vol.23, pp.459-466, 2012.

J. Zhang, EglN2 associates with the NRF1-PGC1? complex and controls mitochondrial function in breast cancer, EMBO J, vol.34, pp.2953-2970, 2015.