Identification of the Ah Receptor Nuclear Translocator Protein (Arnt) as a Component of the DNA Binding Form of the Ah Receptor

@article{Reyes1992IdentificationOT,
  title={Identification of the Ah Receptor Nuclear Translocator Protein (Arnt) as a Component of the DNA Binding Form of the Ah Receptor},
  author={H Reyes and Suzanne Reisz-Porszasz and Oliver Hankinson},
  journal={Science},
  year={1992},
  volume={256},
  pages={1193 - 1195}
}
The Ah (dioxin) receptor binds a number of widely disseminated environmental pollutants, including 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and polycyclic aromatic hydrocarbons, and mediates their carcinogenic effects. The ligand-bound receptor activates Cyp1a1 gene transcription through interaction with specific DNA sequences, termed xenobiotic responsive elements (XREs). The Ah receptor nuclear translocator protein (Arnt) is required for Ah receptor function. Arnt is now shown to be a… 
Interaction of the regulatory domains of the murine Cyp1a1 gene with two DNA-binding proteins in addition to the Ah receptor and the Ah receptor nuclear translocator (ARNT).
TLDR
Evidence from in vivo methylation protection indicated that two G residues flanking AhRE3, one of which is required for binding of the 95-kDa protein, may be protected from methylation in uninduced cells and become exposed upon dioxin treatment, suggesting that the 95s may be constitutively bound to AhRE2, and be displaced by binding ofThe Ah receptor complex.
Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT).
TLDR
Both the PAS A and PAS B segments apparently fulfill additional, unknown functions required for biological activity of ARNT, which possesses multiple domains required for maximal heterodimerization.
Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT)
The activated aryl hydrocarbon receptor (AHR) and the AHR nuclear translocator (ARNT) bind DNA as a heterodimer. Both proteins represent a novel class of basic helix-loop-helix (bHLH)-containing
Investigation on the potential role of the Ah receptor nuclear translocator protein in vitamin D receptor action.
TLDR
Two lines of evidence demonstrate that ARNT is not required for vitamin D receptor activity, and therefore does not correspond to the vitamin D receptors accessory protein.
A factor binding to the xenobiotic responsive element (XRE) of P-4501A1 gene consists of at least two helix-loop-helix proteins, Ah receptor and Arnt.
TLDR
The results indicate that Ah receptor and Arnt proteins are components of the XRE-binding factor and suggest that Arnt as well as the Ah receptor are localized in the cytosol of nontreated cells.
Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor
The intracellular basic region/helix-loop-helix (bHLH) dioxin receptor mediates signal transduction by dioxin (2,3,7,8-tetrachlorodibenzo-p-dioxin) and functions as a ligand-activated DNA binding
Mapping the Protein/DNA Contact Sites of the Ah Receptor and Ah Receptor Nuclear Translocator*
TLDR
These experiments indicate that while the structural features of the ARNTGTG complex may closely resemble that deduced for proteins such as Max, E47, and USF, the AHRTNGC complex may represent a unique DNA binding form of basic/helix-loop-helix proteins.
Transcriptional Activation by the Mouse Ah Receptor.
TLDR
Analyses of deletion mutants indicate that the carboxyl half of AhR contains several types of transactivation domain, which function independently of domains that mediate TCDD recognition, DNA binding, and heterodimerization with the Ah receptor nuclear translocator (Arnt) protein.
Mechanisms of Ligand-Induced Aryl Hydrocarbon Receptor-Mediated Biochemical and Toxic Responses
TLDR
Molecular mechanistic studies of TCDD action have contributed significantly to an improved understanding of the role of at least 2 bHLH/PAS proteins, as well as organ- and tissue-specific biochemical and toxic responses to this class of environmental toxins.
Aryl hydrocarbon receptor-mediated signal transduction.
TLDR
A review of recent molecular studies of AhR-mediated gene regulation reveals that expression of the AhR is a requirement for proper embryonal development, which appears to be a common function shared by many other bHLH proteins.
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TLDR
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TLDR
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