Abstract

The aryl hydrocarbon (Ah) receptor binds various environmental pollutants, such as polycyclic aromatic hydrocarbons, heterocyclic amines, and polychlorinated aromatic compounds (dioxins, dibenzofurans, and biphenyls), and mediates the carcinogenic effects of these agents. The complementary DNA and part of the gene for an 87-kilodalton human protein that is necessary for Ah receptor function have been cloned. The protein is not the ligand-binding subunit of the receptor but is a factor that is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after binding ligand. The requirement for this factor distinguishes the Ah receptor from the glucocorticoid receptor, to which the Ah receptor has been presumed to be similar. Two portions of the 87-kilodalton protein share sequence similarities with two Drosophila proteins, Per and Sim. Another segment of the protein shows conformity to the consensus sequence for the basic helix-loop-helix motif found in proteins that bind DNA as homodimers or heterodimers.

Keywords

Aryl hydrocarbon receptor nuclear translocatorAryl hydrocarbon receptorReceptorProtein subunitChemistryTranscription factor5-HT5A receptorBiochemistryGamma-aminobutyric acid receptor subunit alpha-1CytosolBiologyG alpha subunitGene

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Publication Info

Year
1991
Type
article
Volume
252
Issue
5008
Pages
954-958
Citations
961
Access
Closed

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Cite This

Emily C. Hoffman, Herminio Reyes, Fong‐Fong Chu et al. (1991). Cloning of a Factor Required for Activity of the Ah (Dioxin) Receptor. Science , 252 (5008) , 954-958. https://doi.org/10.1126/science.1852076

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DOI
10.1126/science.1852076