This Article Full Text Full Text (PDF) All Versions of this Article: 21/2/321    most recent Author Manuscript (PDF) Purchase Article View Shopping Cart Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager NURSA Molecule Pages Link Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Flamant, F. Articles by Samarut, J. Search for Related Content PubMed PubMed Citation Articles by Flamant, F. Articles by Samarut, J.

Thyroid Hormones Signaling Is Getting More Complex: STORMs Are Coming

Laboratory of Molecular Cell Biology (F.F., K.G., J.S.), Unité Mixte de Recherche, Centre National de la Recherche Scientifique 5161, Institut National de la Recherche Agronomique 1237, Ecole Normale Supérieure de Lyon, Institut Fédératif de Recherche 128 Biosciences Lyon Gerland, and Université Claude Bernard Lyon 1 (J.S.), 69364 Lyon Cedex 07, France

Address all correspondence and requests for reprints to: Frederic Flamant, Laboratory of Molecular Cell Biology, Unité Mixte de Recherche, Centre National de la Recherche Scientifique 5161, Institut National de la Recherche Agronomique 1237, Ecole Normale Supérieure de Lyon, Institut Fédératif de Recherche 128 Biosciences Lyon Gerland, 46 allée d’Italie, 69364 Lyon Cedex 07, France. E-mail: Frederic.Flamant{at}ens-lyon.fr.

T₃ regulates many physiological and developmental processes by binding to thyroid hormone receptors (TRs). This induces a conformational change of DNA-bound TRs that releases corepressors in favor of coactivators. The associated chromatin modifications induce polymerase II recruitment. Mouse genetic studies clarified the respective contribution of each receptor isoform and revealed the important activity of unliganded TRs. They also confirm the paradoxical negative regulation of some promoters by liganded TRs. Recent advances place these molecular events in a broader context of extra- and intracellular regulation: control of ligand availability, changes in the cell sensitivity to T₃, nongenomic effects, and cross talks with other signaling pathways contribute to increase the diversity and complexity of thyroid hormones signaling. A promising novel class of TRs synthetic ligands, called STORMs (selective TR modulators), might allow for tissue- and promoter-specific interventions.

NURSA Molecule Pages Link:

Nuclear Receptors:   TRα  |  TRβ  |  PPARα  |  LXRβ

Coregulators:   P/CAF  |  PGC-1  |  SRA  |  TBLR1  |  Alien  |  CARM1  |  Cyclin D1  |  hr  |  PRMT1  |  SRC-1  |  GRIP1

Ligands:   9-cis-Retinoic acid  |  Thyroid hormone

This article has been cited by other articles:

				S. Garapaty, M. A. Mahajan, and H. H. Samuels Components of the CCR4-NOT Complex Function as Nuclear Hormone Receptor Coactivators via Association with the NRC-interacting Factor NIF-1 J. Biol. Chem., March 14, 2008; 283(11): 6806 - 6816. [Abstract] [Full Text] [PDF]

				E. Kress, A. Rezza, J. Nadjar, J. Samarut, and M. Plateroti The Thyroid Hormone Receptor-{alpha} (TR{alpha}) Gene Encoding TR{alpha}1 Controls Deoxyribonucleic Acid Damage-Induced Tissue Repair Mol. Endocrinol., January 1, 2008; 22(1): 47 - 55. [Abstract] [Full Text] [PDF]

				L. Quignodon, S. Vincent, H. Winter, J. Samarut, and F. Flamant A Point Mutation in the Activation Function 2 Domain of Thyroid Hormone Receptor {alpha}1 Expressed after CRE-Mediated Recombination Partially Recapitulates Hypothyroidism Mol. Endocrinol., October 1, 2007; 21(10): 2350 - 2360. [Abstract] [Full Text] [PDF]

				L. Quignodon, C. Grijota-Martinez, E. Compe, R. Guyot, N. Allioli, D. Laperriere, R. Walker, P. Meltzer, S. Mader, J. Samarut, et al. A combined approach identifies a limited number of new thyroid hormone target genes in post-natal mouse cerebellum J. Mol. Endocrinol., July 1, 2007; 39(1): 17 - 28. [Abstract] [Full Text] [PDF]

				S. Suzuki, N. Suzuki, J.-i. Mori, A. Oshima, S. Usami, and K. Hashizume {micro}-Crystallin as an Intracellular 3,5,3'-Triiodothyronine Holder in Vivo Mol. Endocrinol., April 1, 2007; 21(4): 885 - 894. [Abstract] [Full Text] [PDF]