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Originally published In Press as doi:10.1074/jbc.M202413200 on September 4, 2002

J. Biol. Chem., Vol. 277, Issue 46, 44028-44034, November 15, 2002
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Interaction with Nedd8, a Ubiquitin-like Protein, Enhances the Transcriptional Activity of the Aryl Hydrocarbon Receptor*

Monica AntenosDagger §, Robert F. CasperDagger §||, and Theodore J. BrownDagger §||**

From the Dagger  Division of Reproductive Sciences, Samuel Lunenfeld Research Institute, Mount Sinai Hospital and Departments of  Zoology, || Physiology, and § Obstetrics and Gynecology, University of Toronto, Toronto, Ontario M5G 1X5, Canada

The aryl hydrocarbon receptor (AhR) is a ligand-activated member of the basic helix-loop-helix period aryl hydrocarbon nuclear translocator single-minded (PAS) transcription factor family. This receptor has been shown to be important in various aspects of growth and development as demonstrated by AhR-null mice. A yeast two-hybrid screen of a mouse embryonic day 11 library for AhR-interacting proteins revealed Nedd8 as a candidate. The interaction was confirmed in a cell-free system and in mammalian cells by co-immunoprecipitation; however, in vitro neddylation assays showed that Nedd8 does not covalently modify AhR. Transfection of Nedd8 into a cell line stably transfected with a dioxin response element linked to a chloramphenicol acetyltransferase reporter gene demonstrated that Nedd8 amplified ligand-induced transcription. Deletion of the Gly-76 residue in the carboxyl terminus of Nedd8 abolished this effect and prevented AhR-Nedd8 interaction. Nedd8 overexpression also resulted in accumulation of AhR protein in the nucleus, independent of exogenous ligand. These studies demonstrate that the AhR interacts with Nedd8 and suggest that this interaction enhances the transcriptional activity of the receptor, perhaps involving increased nuclear accumulation or retention. Immunohistochemistry performed on embryonic day 11.5 mouse sections indicated Nedd8 and AhR localize to overlapping areas in the heart and spinal ganglia, raising the possibility that this interaction may play a role in organogenesis.

* This work was supported by the Canadian Institutes of Health Research. A portion of this manuscript was presented at the Endocrine Society Conference 2001.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** To whom correspondence should be addressed: Division of Reproductive Sciences, Depts. of Obstetrics and Gynecology, Physiology, and Zoology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Ave. Rm. 876, Toronto, Ontario M5G 1X5, Canada. Tel.: 416-586-4800 (ext. 2451); Fax: 416-586-8588; E-mail: brown@mshri.on.ca.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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