The c-erb-A protein is a high-affinity receptor for thyroid hormone

@article{Sap1986TheCP,
  title={The c-erb-A protein is a high-affinity receptor for thyroid hormone},
  author={Jan Sap and Alberto Mu{\~n}oz and Klaus Damm and Yves Goldberg and Jacques Ghysdael and Achim Leutz and Hartmut Beug and Björn Vennström},
  journal={Nature},
  year={1986},
  volume={324},
  pages={635-640}
}
Hormone binding and localization of the c-erb-A protein suggest that it is a receptor for thyroid hormone, a nuclear protein that binds to DNA and activates transcription. In contrast, the product of the viral oncogene v-erb-A is defective in binding the hormone but is still located in the nucleus. 
Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist
TLDR
The oncogenic derivative of the thyroid-hormone receptor, v-erbA, acts as a constitutive represser and, when coexpressed with the receptor, blocks activation by thyroid hormone.
The v‐erbA oncogene is a thyroid hormone receptor antagonist
  • R. Evans
  • Biology
    International journal of cancer. Supplement = Journal international du cancer. Supplement
  • 1989
TLDR
Surprisingly, v-erbA does not act as an activator but rather as a constitutive repressor of hormone-responsive genes, and is demonstrated to negatively regulates the expression of a T 3 -responsive reporter gene in the absence of hormone.
DNA Binding Properties of the Thyroid Hormone Receptor/c-erbA Protein and Its Viral Homologue P75gag-v-erbA
TLDR
The experiments demonstrate that the two proteins can recognize the same regulatory elements in erythroblasts but with distinct effects on transcription, and that other TREs bind to only one of the proteins, suggesting that mutations in the primary structure of the viral protein has altered its specificity.
The Thyroid Hormone Receptor/c-erbA Protein and its Viral Homologue P75gag-v-erbA
TLDR
The experiments demonstrate that the two proteins can recognize the same regulatory elements in erythroblasts but with distinct effects on transcription, and that other TREs bind to only one of the proteins, suggesting that mutations in the primary structure of the viral protein has altered its specificity.
A c-erb-A binding site in rat growth hormone gene mediates trans-activation by thyroid hormone
TLDR
An avidin–biotin complex DNA-binding assay is described which can detect specific, high-affinity binding of rat pituitary cell T3 receptors to the sequence 5'CAGGGACGTGACCGCA3', located 164 base pairs 5' to the transcriptional start site of the rat growth hormone gene.
Sequence-specific DNA binding by the v-erbA oncogene protein of avian erythroblastosis virus
TLDR
The v-erbA protein bound at high affinity to a set of DNA fragments recognized by the rat thyroid hormone receptor, but the relative affinity of the v- DerbA protein for the different binding sites was distinct from that previously reported for the thyroid hormone receptors.
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References

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The c-erb-A gene encodes a thyroid hormone receptor
TLDR
The cDNA sequence of human c-erb-A indicates that the protein encoded by the gene is related to the steroid hormone receptors, and binding studies show it to be a receptor for thyroid hormones.
Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A
TLDR
Cloned and sequenced the complete complementary DNA of the oestrogen receptor (ER) present in the breast cancer cell line MCF-7 and found extensive homology between the ER and the erb-A protein of the oncogenic avian erythroblastosis virus.
Thyroid Hormone Action: In vitro Demonstration of Putative Receptors in Isolated Nuclei and Soluble Nuclear Extracts
Saturable binding activities for triiodothyronine were demonstrated in vitro with isolated nuclei and soluble nuclear extracts of rat liver, kidney, and cultured GH1 cells. The binding activity can
Domain structure of human glucocorticoid receptor and its relationship to the v-erb-A oncogene product
TLDR
It is reported here that both forms of the receptor are related, with respect to their domain structure, to the v-erb-A oncogene product of avian erythroblastosis virus (AEV), which suggests that steroid receptor genes and the c-erb -A proto-oncogene are derived from a common primordial regulatory gene.
The binding of thyroid hormone receptors to DNA.
Chromatin receptors for thyroid hormones. Interactions of the solubilized proteins with DNA.
TLDR
The finding that receptors bind extensively and tightly to DNA suggests that receptors in chromatin may randomly bind to any available DNA, resulting in some of the receptors being at physiologically unimportant sites.
The chicken oestrogen receptor sequence: homology with v‐erbA and the human oestrogen and glucocorticoid receptors.
TLDR
A chicken oviduct cDNA clone containing the complete open reading frame of the oestrogen receptor (ER) has been isolated and sequenced, indicating that c‐erbA, the cellular counterpart of v‐erbB, belongs to a multigene family of transcriptional regulatory proteins which bind steroid‐related ligands.
Localisation of the oestradiol‐binding and putative DNA‐binding domains of the human oestrogen receptor.
TLDR
Site‐directed mutagenesis was used to prepare a series of human oestrogen receptor (hER) deletion mutants and results indicate that a region which is highly conserved between the human and chicken ERs (region E) contains all of the sequence necessary to bind oestradiol with high affinity.
Dose-dependent depletion of nuclear receptors by L-triiodothyronine: evidence for a role in induction of growth hormone synthesis in cultured GH1 cells.
TLDR
The relationship between the binding of T3 to nuclear receptors and the induction of growth hormone synthesis was examined in cultured GH1 cells, a rat pituitary cell line and the biologic dose-response curve was shifted to the left of the receptor occupancy curve.
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