Posttranslational Modification of Thyroid Hormone Nuclear Receptor by Phosphorylation

2018 ◽  
pp. 39-46 ◽  
Author(s):  
Yan-Yun Liu ◽  
Gregory A. Brent
Keyword(s):  
Thyroid Hormone ◽  
Nuclear Receptor ◽  
Posttranslational Modification

scholarly journals A novel orphan receptor specific for a subset of thyroid hormone-responsive elements and its interaction with the retinoid/thyroid hormone receptor subfamily.

1994 ◽  
Vol 14 (10) ◽  
pp. 7025-7035 ◽  
Author(s):  
R Apfel ◽  
D Benbrook ◽  
E Lernhardt ◽  
M A Ortiz ◽  
G Salbert ◽  
...  
Keyword(s):  
Amino Acid ◽  
Thyroid Hormone ◽  
Dna Binding ◽  
Nuclear Receptors ◽  
Nuclear Receptor ◽  
Dna Sequences ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Orphan Receptor ◽  
Retinoid Receptor

The steroid/hormone nuclear receptor superfamily comprises several subfamilies of receptors that interact with overlapping DNA sequences and/or related ligands. The thyroid/retinoid hormone receptor subfamily has recently attracted much interest because of the complex network of its receptor interactions. The retinoid X receptors (RXRs), for instance, play a very central role in this subfamily, forming heterodimers with several receptors. Here we describe a novel member of this subfamily that interacts with RXR. Using a v-erbA probe, we obtained a cDNA which encodes a novel 445-amino-acid protein, RLD-1, that contains the characteristic domains of nuclear receptors. Northern (RNA) blot analysis showed that in mature rats, the receptor is highly expressed in spleen, pituitary, lung, liver, and fat. In addition, weaker expression is observed in several other tissues. Amino acid sequence alignment and DNA-binding data revealed that the DNA-binding domain of the new receptor is related to that of the thyroid/retinoid subgroup of nuclear receptors. RLD-1 preferentially binds as a heterodimer with RXR to a direct repeat of the half-site sequence 5'-G/AGGTCA-3', separated by four nucleotides (DR-4). Surprisingly, this binding is dependent to a high degree on the nature of the spacing nucleotides. None of the known nuclear receptor ligands activated RLD-1. In contrast, a DR-4-dependent constitutive transcriptional activation of a chloramphenicol acetyltransferase reporter gene by the RLD-1/RXR alpha heterodimer was observed. Our data suggest a highly specific role for this novel receptor within the network of gene regulation by the thyroid/retinoid receptor subfamily.

scholarly journals The Nuclear Receptor Corepressor (NCoR) Controls Thyroid Hormone Sensitivity and the Set Point of the Hypothalamic-Pituitary-Thyroid Axis

2011 ◽  
Vol 96 (2) ◽  
pp. 557-557
Author(s):  
Inna Astapova ◽  
Kristen R. Vella ◽  
Preeti Ramadoss ◽  
Kaila A. Holtz ◽  
Benjamin A. Rodwin ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Nuclear Receptor ◽  
Hormone Sensitivity ◽  
Set Point ◽  
Nuclear Receptor Corepressor ◽  
Pituitary Thyroid Axis ◽  
Thyroid Axis

scholarly journals The Nuclear Receptor Corepressor (NCoR) Controls Thyroid Hormone Sensitivity and the Set Point of the Hypothalamic-Pituitary-Thyroid Axis

2011 ◽  
Vol 25 (2) ◽  
pp. 212-224 ◽  
Author(s):  
Inna Astapova ◽  
Kristen R. Vella ◽  
Preeti Ramadoss ◽  
Kaila A. Holtz ◽  
Benjamin A. Rodwin ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Nuclear Receptor ◽  
Hormone Sensitivity ◽  
Set Point ◽  
Nuclear Receptor Corepressor ◽  
Pituitary Thyroid Axis ◽  
Thyroid Axis

scholarly journals Activation of the thyroid hormone receptor α gene promoter by the orphan nuclear receptor ERRα

Oncogene ◽  
1998 ◽  
Vol 17 (19) ◽  
pp. 2429-2435 ◽  
Author(s):  
Jean-Marc Vanacker ◽  
Edith Bonnelye ◽  
Cateline Delmarre ◽  
Vincent Laudet
Keyword(s):  
Thyroid Hormone ◽  
Nuclear Receptor ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Gene Promoter ◽  
Orphan Nuclear Receptor ◽  
Thyroid Hormone Receptor Α
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