Nuclear receptor superfamily: Principles of signaling

Germain, Pierre; Altucci, Lucia; Bourguet, William; Rochette-Egly, C.; Gronemeyer, Hinrich

doi:10.1351/pac200375111619

Cited by 53Estrogen and related hormone effectsNuclear Receptors and SignalingGenomics and Chromatin Dynamics

Nuclear receptor superfamily: Principles of signaling

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Germain, Pierre, Altucci, Lucia, Bourguet, William, Rochette-Egly, C., Gronemeyer, Hinrich·2003·Pure and Applied Chemistry

DOI 10.1351/pac200375111619

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Abstract

Nuclear receptors (NRs) comprise a family of 49 members that share a common structural organization and act as ligand-inducible transcription factors with major (patho)physiological impact. For some NRs (“orphan receptors”), cognate ligands have not yet been identified or may not exist. The principles of DNA recognition and ligand binding are well understood from both biochemical and crystal structure analyses. The 3D structures of several DNA-binding domains (DBDs),in complexes with a variety of cognate response elements, and multiple ligand-binding domains (LBDs), in the absence (apoLBD)and presence (holoLBD) of agonist, have been established and reveal canonical structural organization. Agonist binding induces a structural transition in the LBD whose most striking feature is the relocation of helix H12, which is required for establishing a coactivator complex, through interaction with members of the p160 family (SRC1, TIF2, AIB1) and/or the TRAP/DRIP complex. The p160-dependent coactivator complex is a multiprotein complex that comprises histone acetyltransferases (HATs), such as CBP,methyltransferases, such as CARM1, and other enzymes (SUMO ligase,etc.). The agonist-dependent recruitment of the HAT complex results in chromatin modification in the environment of the target gene promoters, which is requisite to, or may in some cases be sufficient for, transcription activation. In the absence of ligands, or in the presence of some antagonists, certain NRs are bound to distinct multiprotein complexes through the interaction with corepressors, such as NCoR and SMRT. Corepressor complexes comprise histone deacetylases (HDACs) that have the capacity to condense chromatin over target gene promoters. Ligands have been designed that selectively modulate the interaction between NRs and their coregulators. Both HATs and HDACs can also modify the acetylation status of nonhistone proteins, but the significance in the context of NR signaling is unclear. NRs communicate with other intracellular signaling pathways on a mutual basis, and their functionality may be altered, positively or negatively, by post-translational modification. The majority of NRs act as retinoid X receptor (RXR) heterodimers in which RXR cannot a priori respond autonomously to its cognate ligand to activate target gene transcription. This RXR subordination allows signaling pathway identity for the RXR partner. The corresponding mechanism is understood and reveals cell and NR selectivity, indicating that RXR can, under certain conditions, act autonomously. NRs are regulators of cell life and death,and NR malfunction can be at the basis of both disease and therapy, as is impressively documented in the case of acute promyelocytic leukemia. Recently, several pathways have been uncovered that link NR action with cell proliferation and apoptosis.

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RARs heterodimerized with RXRs bind to specific retinoic acid response elements (RARE) located in the promoters of target genes.
“RARs heterodimerized with RXRs bind to specifi c retinoic acid response elements (RARE) located in the promoters of target genes.”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [77]
Classically, RAREs are composed of two direct repeats (DR) of a core hexameric motif (A/G)G(G/T)TCA separated by 1, 2, or 5 nucleotides and referred as DR1, DR2, and DR5.
“Classically, RAREs are composed of two direct repeats (DR) of a core hexameric motif (A/G) G (G/T) TCA separated by 1, 2, or 5 nucleotides and referred as DR1, DR2, and DR5 ( 26, 76, 77 ) ( Fig. 3B ).”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [77]

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The Nuclear Corepressors NCoR and SMRT Are Key Regulators of Both Ligand- and 8-Bromo-Cyclic AMP-Dependent Transcriptional Activity of the Human Progesterone Receptor
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The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full‐length receptors to direct repeats.
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The SMRT Corepressor Is Regulated by a MEK-1 Kinase Pathway: Inhibition of Corepressor Function Is Associated with SMRT Phosphorylation and Nuclear Export
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Functional Interactions of the AF-2 Activation Domain Core Region of the Human Androgen Receptor with the Amino-Terminal Domain and with the Transcriptional Coactivator TIF2 (Transcriptional Intermediary Factor 2)
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AF-2 Activity and Recruitment of Steroid Receptor Coactivator 1 to the Estrogen Receptor Depend on a Lysine Residue Conserved in Nuclear Receptors
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Dimerization interfaces formed between the DNA binding domains determine the cooperative binding of RXR/RAR and RXR/TR heterodimers to DR5 and DR4 elements.
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The inducible Iac operator-repressor system is functional in mammalian cells
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Transcriptional Hyperactivity of Human Progesterone Receptors Is Coupled to Their Ligand-Dependent Down-Regulation by Mitogen-Activated Protein Kinase-Dependent Phosphorylation of Serine 294
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A base mutation of the C-erbA beta thyroid hormone receptor in a kindred with generalized thyroid hormone resistance. Molecular heterogeneity in two other kindreds.
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Regulation of the Transcriptional Activity of the Peroxisome Proliferator-activated Receptor α by Phosphorylation of a Ligand-independent trans-Activating Domain
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Retinoic acid receptors: From molecular mechanisms to cancer therapy
di Masi, A., Leboffe, L., De Marinis, E., Pagano, F., Cicconi, L., Rochette-Egly, C., Lo-Coco, F., Ascenzi, P., & Nervi, C. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2014.12.003 · Cited by 403 · see citing works
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Vitamin A and retinoid signaling: genomic and nongenomic effects
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Dynamic and combinatorial control of gene expression by nuclear retinoic acid receptors (RARs)
Rochette‐Egly, C., & Germain, P. (2009) · Nuclear Receptor Signaling · doi:10.1621/nrs.07005 · Cited by 244 · see citing works
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The molecular physiology of nuclear retinoic acid receptors. From health to disease
Duong, V., & Rochette‐Egly, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.10.007 · Cited by 137 · see citing works
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Glucocorticoids and the innate immune system: crosstalk with the toll-like receptor signaling network
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Conformational Dynamics of the Estrogen Receptor α: Molecular Dynamics Simulations of the Influence of Binding Site Structure on Protein Dynamics
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Transient expression of thyroid hormone nuclear receptor TRβ2 sets S opsin patterning during cone photoreceptor genesis
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Exploring Interactions of Endocrine-Disrupting Compounds with Different Conformations of the Human Estrogen Receptor α Ligand Binding Domain: A Molecular Docking Study
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Protein kinases and the proteasome join in the combinatorial control of transcription by nuclear retinoic acid receptors
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Freshwater mudsnail (Potamopyrgus antipodarum) estrogen receptor: Identification and expression analysis under exposure to (xeno-)hormones
Stange, D., Sieratowicz, A., Horres, R., & Oehlmann, J. (2011) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2011.09.003 · Cited by 58 · see citing works
Definition of the Molecular Basis for Estrogen Receptor-Related Receptor-α-Cofactor Interactions
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Sex steroid levels and expression patterns of estrogen receptor gene in the oyster Crassostrea angulata during reproductive cycle
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Vinexin β Interacts with the Non-phosphorylated AF-1 Domain of Retinoid Receptor γ (RARγ) and Represses RARγ-mediated Transcription
Bour, G., Plassat, J., Bauer, A., Lalevée, S., & Rochette‐Egly, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501344200 · Cited by 50 · see citing works
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Estrogen activity as a preventive and therapeutic target in thyroid cancer
Rajoria, S., Suriano, R., George, A. L., Shanmugam, A., Jussim, C., Shin, E. J., Moscatello, A. L., Geliebter, J., Carpi, A., & Tiwari, R. K. (2011) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2011.11.010 · Cited by 46 · see citing works
Dynamics of Nuclear Receptor Helix-12 Switch of Transcription Activation by Modeling Time-Resolved Fluorescence Anisotropy Decays
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Combination therapy for treating breast cancer using antiestrogen, ERA-923, and the mammalian target of rapamycin inhibitor, temsirolimus
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Progesterone Receptor Isoforms in Normal and Malignant Breast
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Protein structure based rational design of ecdysone agonists
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Nuclear and Extra-Nuclear Effects of Retinoid Acid Receptors: How They Are Interconnected
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Activation helix orientation of the estrogen receptor is mediated by receptor dimerization: evidence from molecular dynamics simulations.
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The retinoic acid receptor (RAR) in molluscs: Function, evolution and endocrine disruption insights
André, A., Ruivo, R., Fonseca, E. S. S., Froufe, E., Castro, L. F. C., & Santos, M. M. (2019) · Aquatic Toxicology · doi:10.1016/j.aquatox.2019.01.002 · Cited by 30 · see citing works
Retinoic Acid Receptor Subtype-Specific Transcriptotypes in the Early Zebrafish Embryo
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Nuclear receptor and target gene mRNA abundance in duodenum and colon of dogs with chronic enteropathies
Greger, D. L., Gropp, F., Morel, C., Sauter, S. N., & Blum, J. W. (2005) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2005.12.002 · Cited by 20 · see citing works
Tackling exosome and nuclear receptor interaction: an emerging paradigm in the treatment of chronic diseases
Aswani, B. S., Hegde, M., Vishwa, R., Alqahtani, M. S., Abbas, M., Almubarak, H. A., Sethi, G., & Kunnumakkara, A. B. (2024) · Military Medical Research · doi:10.1186/s40779-024-00564-1 · Cited by 16 · see citing works
Cloning and functional characterization of a retinoid X receptor orthologue in Platynereis dumerilii: An evolutionary and toxicological perspective
André, A., Ruivo, R., Capitão, A., Froufe, E., Páscoa, I., Castro, L. F. C., & Santos, M. M. (2017) · Chemosphere · doi:10.1016/j.chemosphere.2017.05.064 · Cited by 16 · see citing works
Mouse embryocarcinoma F9 cells and retinoic acid: A model to study the molecular mechanisms of endodermal differentiation
Bour, G., Taneja, R., & Rochette‐Egly, C. (2006) · Advances in developmental biology · doi:10.1016/s1574-3349(06)16007-x · Cited by 12 · see citing works
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An Orthologue of the Retinoic Acid Receptor (RAR) Is Present in the Ecdysozoa Phylum Priapulida
Fonseca, E. S. S., Hiromori, Y., Kaite, Y., Ruivo, R., Franco, J. N., Nakanishi, T., Santos, M. M., & Castro, L. F. C. (2019) · Genes · doi:10.3390/genes10120985 · Cited by 12 · see citing works
Highly twisted adamantyl arotinoids: Synthesis, antiproliferative effects and RXR transactivation profiles
Pérez-Rodríguez, S., Ortiz, M. A., Pereira, R., Rodríguez‐Barrios, F., de Lera, Á. R., & Piedrafita, F. J. (2009) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2009.01.011 · Cited by 11 · see citing works
MSK1 and Nuclear Receptors Signaling
Piskunov, A., & Rochette‐Egly, C. (2013) · Cited by 9 · see citing works
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Protein Conformational Transitions from All-atom Adaptively Biased Path Optimization (ABPO)
Wu, H., & Post, C. (2018) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.8b00147 · Cited by 9 · see citing works
Expression variations of two retinoid signaling pathway receptors in the rotifer Brachionus calyciflorus exposed to three endocrine disruptors
Joaquim‐Justo, C., & Gismondi, É. (2021) · Ecotoxicology · doi:10.1007/s10646-020-02339-5 · Cited by 6 · see citing works
Molecular docking for screening chemicals of environmental health concern: insight from a case study on bisphenols
Norouzi, S., Nahmiach, N., Perez, G. R., Zhu, Y., Peslherbe, G. H., Muir, D. C. G., & Zhang, X. (2025) · Environmental Science Processes & Impacts · doi:10.1039/d5em00084j · Cited by 5 · see citing works
Structural insight to human Retinoid X receptor alpha-Thyroid hormone receptor beta heterodimer by molecular modelling and MD-simulation studies: role of conserved water molecules
Mukherjee, S., Dasgupta, S., Panja, S. S., & Adhikari, U. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2147097 · Cited by 5 · see citing works
Investigation of Interactions between DNA and Nuclear Receptors: A Review of the Most Used Methods
Fattori, J., Indolfo, N. D. C., Campos, J. C. L. D. O., Videira, N. B., Bridi, A. V., Doratioto, T. R., de Assis, M. A., & Figueira, A. C. M. (2014) · Nuclear Receptor Research · doi:10.11131/2014/101090 · Cited by 5 · see citing works
Production and characterization of a retinoic acid receptor RARγ construction encompassing the DNA binding domain and the disordered N-terminal proline rich domain
Martinez-Zapien, D., Delsuc, M., Travé, G., Lutzing, R., Rochette‐Egly, C., & Kieffer, B. (2013) · Protein Expression and Purification · doi:10.1016/j.pep.2013.12.001 · Cited by 4 · see citing works
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Chapter 1 Supported Lipid Bilayers for the Detection of Hormone-Receptor Interactions
Sacks, V., & Rishpon, J. (2006) · Elsevier eBooks · doi:10.1016/s1554-4516(05)03001-2 · Cited by 4 · see citing works
Cloning and comparative analysis of the retinoid X receptor in two marine gastropods with varying sensitivity to imposex under tributyltin contamination
Giulianelli, S., Ruivo, R., Neuparth, T., Castro, L. F. C., Bigatti, G., & Santos, M. M. (2025) · Environmental Science and Pollution Research · doi:10.1007/s11356-025-36278-7 · Cited by 3 · see citing works
Purification and crystallization of the heterodimeric complex of RARβ and RXRα ligand-binding domains in the active conformation
Pogenberg, V., Guichou, J., & Bourguet, W. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904009928 · Cited by 3 · see citing works
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Synthesis and preliminary evaluation of affinity to retinoic acid receptors for new organosilicon-based retinoids
Nantogmah, S., Desai, S., Bhandare, R. R., Gabriel, J. L., Soprano, D. R., & Canney, D. J. (2012) · Pharmaceutical Chemistry Journal · doi:10.1007/s11094-012-0692-5 · Cited by 3 · see citing works
Measuring binding kinetics of ligands with tethered receptors by fluorescence polarization complemented with total internal reflection fluorescence microscopy
Kwok, K. C. (2010) · HKBU Institutional Repository (Hong Kong Baptist University) · Cited by 3 · see citing works
Identification of Nuclear Receptors and Its Family Using Wavelet Variance Features
Gupta, R., Mittal, A., Singh, K., Sharma, P., & Sharma, A. (2007) · doi:10.1109/icit.2007.55 · Cited by 3 · see citing works
Metadichol® A Novel Inverse Agonist of Thyroid Receptor and its Applications in Thyroid Diseases
Pr, R. (2019) · Biology and Medicine · doi:10.35248/0974-8369.19.11.458 · Cited by 2 · see citing works
Design and Simulation of Parallel Algorithms for Motion Estimation
Bhattacharyya, D., Chakrabarti, A., & Misra, S. (2007) · doi:10.1109/icit.2007.44 · Cited by 2 · see citing works
La vitamina D regula la expresión del factor neurotrófico GDNF en cultivos neuronales estriatales y en ratas normales y hemiparkinsonianas
Rey, B. (2014) · Tesis Doctorals en Xarxa (Consorci de Serveis Universitaris de Catalunya)
Retinoid-induced apoptosis and proliferation of hepatocytes are mediated by distinct nuclear receptors
Bu, P. (2009) · KU ScholarWorks (The University of Kansas)
Mechanisms of transcriptional activation of estrogen responsive genes in breast cancer cells
Chen, C.-C. (2009) · OakTrust (Texas A&M University Libraries)
Nuclear Receptors
Chai, S. C., & Chen, T. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00113-4
Regulação do promotor SMyHC3 pelos receptores nucleares GR e COUP-TFII
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Histone désacétylases, signalisation œstrogénique et cancer du sein : établissement d’outils bioluminescents pour la détection d’inhibiteurs sélectifs de HDAC : expression et rôle de HDAC9 dans les lignées cellulaires de cancer du sein
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Effet de la pollution urbaine et industrielle sur le système endocrinien : évaluation des conséquences sur la reproduction de "Ruditapes decusatus" issue du golfe de Gabès (Tunisie)
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Mécanisme moléculaires du rôle protumorigénique de PPARgamma et RXRalpha dans les cancers de vessie
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Yu, Y. E. (2011)
Analysis of genetic variants in the 5’ regulatory region of the ALAS1 gene in South African patients with Variegate Porphyria (VP)
du Plessis, N. (2007) · SUNScholar (Stellenbosch University)

Topic 1.1 Nuclear receptor superfamily: Principles of signaling*
Germain, P., Altucci, L., Bourguet, W., Rochette‐Egly, C., & Gronemeyer, H. (2014)
Self-citation
Nuclear Receptor Coactivators
Stender, J. D., & Glass, C. K. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00244-8
Transcriptional coregulators of the nuclear receptor superfamily: coactivators and corepressors
Lee*, J. W., Lee, Y. C., Na, S.-Y., Jung, D.-J., & Lee, S.-K. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000856 · Cited by 139 · see citing works
Nuclear receptor: Structure and function
Sar, P. (2022) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2022.07.014 · Cited by 16 · see citing works
Nuclear receptor cofactors as chromatin remodelers
Lemon, B. D., & Freedman, L. P. (1999) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)00010-6 · Cited by 103 · see citing works

Authors: Germain, P., Altucci, L., Bourguet, W., Rochette-Egly, C., & Gronemeyer, H.
Affiliations: Institut de génétique et de biologie moléculaire et cellulaire (FR)
University of Campania "Luigi Vanvitelli" (IT)
Centre National de la Recherche Scientifique (FR)
1IGBMC -B.P.10142, F-67404 Illkirch Cedex, C.U.de Strasbourg, France
ORCID: Altucci, Lucia
Bourguet, William
Gronemeyer, Hinrich
Venue: Pure and Applied Chemistry
Publisher: Walter de Gruyter GmbH
Published: 2003-01-01
Volume: 75
Issue: 11-12
Pages: 1619-1664
ISSN: 0033-4545 (ISSN-L)
1365-3075
DOI: 10.1351/pac200375111619
OpenAlex: W2134246871
Cited by: 53
References: 321
Citations by year: 2025: 2 · 2024: 1 · 2022: 1 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 1 · 2017: 2 · 2015: 1 · 2014: 5 · 2013: 4 · 2012: 2
FWCI: 1.25
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Pure and Applied Chemistry (publishedVersion)
HAL (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: nuclear receptors, orphan receptors, ligand binding, DNA-binding domain, ligand-binding domain, p160 coactivators, histone acetyltransferase, histone deacetylase, corepressors, chromatin modification, nuclear receptor signaling

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Nuclear receptor superfamily: Principles of signaling

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