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RelB, a New Partner of Aryl Hydrocarbon Receptor-Mediated Transcription

Department of Environmental Toxicology (C.F.A.V., E.S., W.L., P.W., F.M.), University of California, Davis, Davis, California 95616; and Institut National de la Santé et de la Recherche Médicale Unité 844 (G.L.), Molecular and Cellular Endocrinology of Cancers, Montpellier F-34295, France

Address all correspondence and requests for reprints to: Christoph F. A. Vogel, Department of Environmental Toxicology, University of California, Davis, One Shields Avenue, Davis, California 95616. E-mail: cfvogel{at}ucdavis.edu.

The nuclear factor-B (NF-B) transcription factor family has a crucial role in rapid responses to stress and pathogens. We show that the NF-B subunit RelB is functionally associated with the aryl hydrocarbon receptor (AhR) and mediates transcription of chemokines such as IL-8 via activation of AhR and protein kinase A. RelB physically interacts with AhR and binds to an unrecognized RelB/AhR responsive element of the IL-8 promoter linking two signaling pathways to activate gene transcription. We found a time-dependent recruitment of AhR to the RelB/AhR responsive element site of IL-8 mediated by the AhR ligand 2,3,7,8-tetrachlorodibenzo-p-dioxin (dioxin) and via activation of protein kinase A. Furthermore, NF-B-binding sites that are preferentially recognized by RelB/p52 are a target for RelB/AhR complexes without addition of any stimuli, implicating the endogenous function of the AhR. RelB/AhR complexes are also found to bind on xenobiotic responsive element, and RelB drastically increases the 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced xenobiotic responsive element reporter activity. The interaction of RelB with AhR signaling, and AhR with NF-B RelB signaling pathways represent a new mechanism of cross talk between the two transcription factors.

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