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J.Health Sci., 50(3), 215-219, 2004
-Minireview-
Regulation of Nucleo-Cytoplasmic Transport of the Aryl Hydrocarbon Receptor
Kaname Kawajiri* and Togo Ikuta
Research Institute, Saitama Cancer Center, 818 Komuro, Ina-machi, Kitaadachi-gun, Saitama 362-0806, Japan
The aryl hydrocarbon receptor (AhR) is a ligand-activated transcription factor that plays a role as an
intracellular mediator of the xenobiotic signaling pathway. AhR is a nucleo-cytoplasmic shuttling protein mediated by nuclear
localization signals (NLS) and nuclear export signals (NES). Protein kinase C-mediated phosphorylation of NLS
inhibits the ligand-dependent nuclear import of AhR, suggesting a two-step mechanism of nuclear import. Cell
density regulates AhR intracellular localization, due to modulation of nuclear export activity. The p38
mitogen-activated protein kinase (MAPK)-mediated phosphorylation of NES and its dephosphorylation, regulated by
cell-cell contact signals, may have pivotal roles in the novel AhR relocalization.
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