Ah receptor, a novel ligand-activated transcription factor

Kazuhiro Sogawa, Yoshiaki Fujii-Kuriyama

Research output: Contribution to journalReview articlepeer-review

180 Citations (Scopus)

Abstract

The aryl hydrocarbon receptor (AhR) is widely distributed in vertebrates and is known to be involved in metabolism of xenobiotics including man-made chemicals, most of which act as a ligand for the receptor, although no endogenous ligand has yet been known. Upon binding a ligand, the receptor is activated to translocate to the nuclei, and during the nuclear translocation process, it is dissociated from the 90 kDa heat shock protein (Hsp90) to form a heterodimer with Arnt (Ah receptor nuclear translocator). The heterodimer complex binds a DNA response element termed xenobiotic responsive element (XRE) localized upstream of the target genes of many drug-metabolizing enzymes including cytochrome P4501A1 and glutathione S-transferase to activate their transcription. Recent cDNA cloning has revealed that the AhR, like Arnt, possesses characteristic structural motifs of basic helix-loop-helix and PAS domains responsible for DNA recognition, heterodimerization, and ligand binding, and functions as a novel receptor-type transcription factor.

Original languageEnglish
Pages (from-to)1075-1079
Number of pages5
JournalJournal of biochemistry
Volume122
Issue number6
DOIs
Publication statusPublished - 1997 Dec
Externally publishedYes

Keywords

  • Carcinogenesis
  • PAS domain
  • Transcription factor
  • Xenobiotics
  • bHLH domain

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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