scholarly journals Human TAF(II)135 potentiates transcriptional activation by the AF-2s of the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian cells.

1997 ◽  
Vol 11 (11) ◽  
pp. 1381-1395 ◽  
Author(s):  
G Mengus ◽  
M May ◽  
L Carre ◽  
P Chambon ◽  
I Davidson
Keyword(s):  
Retinoic Acid ◽  
Thyroid Hormone ◽  
Vitamin D3 ◽  
Transcriptional Activation ◽  
Mammalian Cells ◽  
Hormone Receptors ◽  
Thyroid Hormone Receptors

Dual regulatory role for thyroid-hormone receptors allows control of retinoic-acid receptor activity

Nature ◽  
1989 ◽  
Vol 340 (6235) ◽  
pp. 653-656 ◽  
Author(s):  
Gerhart Graupner ◽  
Ken N. Wills ◽  
Maty Tzukerman ◽  
Xiao-kun Zhang ◽  
Magnus Pfahl
Keyword(s):  
Retinoic Acid ◽  
Thyroid Hormone ◽  
Hormone Receptors ◽  
Retinoic Acid Receptor ◽  
Receptor Activity ◽  
Regulatory Role ◽  
Thyroid Hormone Receptors ◽  
Acid Receptor

scholarly journals tau4/tau c/AF-2 of the thyroid hormone receptor relieves silencing of the retinoic acid receptor silencer core independent of both tau4 activation function and full dissociation of corepressors.

1997 ◽  
Vol 17 (8) ◽  
pp. 4259-4271 ◽  
Author(s):  
A Baniahmad ◽  
D Thormeyer ◽  
R Renkawitz
Keyword(s):  
Amino Acids ◽  
Retinoic Acid ◽  
Thyroid Hormone ◽  
Transcriptional Activation ◽  
Hormone Receptors ◽  
Thyroid Hormone Receptor ◽  
Retinoic Acid Receptor ◽  
Activation Function ◽  
Acid Receptor ◽  
C Terminus

Members of the thyroid hormone (TR)-retinoic acid receptor (RAR) subfamily of nuclear hormone receptors silence gene expression in the absence of hormone. Addition of cognate ligands leads to dissociation of corepressors, association of coactivators, and transcriptional activation. Here, we used the hRAR alpha silencer core, which encompasses the ligand binding domain, including receptor regions D and E of RAR alpha without the activation function called tau4/tau c/AF-2 and without the F region, to analyze the mechanisms by which transcriptional silencing is relieved. Although the RAR silencer core is able to bind ligand, it acts as a constitutive transcriptional silencer. We have fused various small activation domains to the C terminus of the silencer core and analyzed hormone-dependent changes in receptor function. We show that nine amino acids derived from the hTRbeta are sufficient to transform the RAR silencer core into a hormone-dependent activator. Lengthening the linker between the silencer core and these nine amino acids is not critical for mediating ligand-induced relief of silencing and activation. In addition, we show that a transactivation function at the C terminus is not required for relief of silencing by the hormone, but it is required for transcriptional activation. Furthermore, we created functional silencer fusions which lose their repressive function upon addition of hormone, although the corepressors SMRT and N-CoR remain attached to the receptor.

Post-transcriptional induction of β1-adrenergic receptor by retinoic acid, but not triiodothyronine, in C6 glioma cells expressing thyroid hormone receptors

1996 ◽  
Vol 135 (6) ◽  
pp. 709-715 ◽  
Author(s):  
Mònica López-Barahona ◽  
Teresa Iglesias ◽  
Irene García-Higuera ◽  
Federico Mayor ◽  
Angel Zaballos ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Thyroid Hormone ◽  
Adrenergic Receptor ◽  
Hormone Receptors ◽  
Glioma Cells ◽  
C6 Glioma ◽  
High Expression ◽  
Thyroid Hormone Receptors ◽  
C6 Glioma Cells ◽  
C6 Cells

López-Barahona M, Iglesias T, García-Higuera I, Mayor Jr F, Zaballos A, Bernal J, Muñoz A. Posttranscriptional induction of β1 -adrenergic receptor by retinoic acid, but not triiodothyronine, in C6 glioma cells expressing thyroid hormone receptors. Eur J Endocrinol 1996:135:709–15. ISSN 0804–4643 Thyroid hormone (triiodothyronine; T3) has been shown to control the expression of β1 -adrenergic receptors (β1-AR) in cardiac myocytes, but not in C6 glioma cells. This cell specificity has been attributed to low expression of T3 receptors and high expression of the c-erbAα2 splice variant that interferes with the action of T3. To check this hypothesis we have expressed the c-erbA/thyroid hormone receptor (TR) α1 gene in C6 glioma cells and investigated their response to thyroid hormone. Cells expressing TRα1, but not wild-type cells, were responsive to T3 as shown by increased expression of mitochrondrial hydroxymethylglutaryl CoA synthase after T3 exposure. However, T3 had no effect on β1-AR gene expression in either set of cells. The β1-AR mRNA concentrations were, however, altered by retinoic acid (RA) treatment. Retinoic acid caused a rapid up-regulation of β1-AR mRNA levels that was blocked by cycloheximide. Retinoic acid did not increase the β1-AR gene transcription rate in run-on experiments. These results indicate an indirect post-transcriptional effect of RA. Control of β1-AR expression in C6 cells is also exerted at the translational level, because there was no correlation between mRNA and protein induction, as determined by radioligand binding studies. We conclude that lack of responsiveness of the β1-AR gene in C6 cells to T3 is not due to high expression of c-erbAα2 but to undefined cell-specific factors. Alberto Muñoz, Instituto Investigaciones Biomedicas, Arturo Duperier 4, 28029 Madrid, Spain

scholarly journals The Book of Opposites: The Role of the Nuclear Receptor Co-regulators in the Suppression of Epidermal Genes by Retinoic Acid and Thyroid Hormone Receptors

2005 ◽  
Vol 124 (5) ◽  
pp. 1034-1043 ◽  
Author(s):  
Sang H. Jho ◽  
Constantinos Vouthounis ◽  
Brian Lee ◽  
Olivera Stojadinovic ◽  
Mark J. Im ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Thyroid Hormone ◽  
Nuclear Receptor ◽  
Hormone Receptors ◽  
Thyroid Hormone Receptors
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