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Originally published In Press as doi:10.1074/jbc.M205987200 on September 26, 2002

J. Biol. Chem., Vol. 277, Issue 48, 46576-46585, November 29, 2002
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The Aryl Hydrocarbon Receptor Nuclear Transporter Is Modulated by the SUMO-1 Conjugation System*

Masahide TojoDagger §, Kazuhito Matsuzaki§, Takeshi MinamiDagger , Yoshiomi Honda§, Hideyo Yasuda||, Tsutomu Chiba, Hideyuki Saya§, Yoshiaki Fujii-Kuriyama**, and Mitsuyoshi NakaoDagger Dagger Dagger

From the Dagger  Department of Regeneration Medicine, Institute of Molecular Embryology and Genetics, Kumamoto University, and the § Department of Tumor Genetics and Biology, Kumamoto University School of Medicine, 2-2-1 Honjo, Kumamoto 860-0811, the  Department of Gastroenterology and Hepatology, Graduate School of Medicine, Kyoto University, 54 Shogoinkawara-cho, Sakyo-ku, Kyoto 606-8507, the || Tokyo University of Pharmacy and Life Science, School of Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, and the ** Department of Chemistry, Graduate School of Science, Tohoku University, Aoba-ku, Sendai 980-8578, Japan

The aryl hydrocarbon receptor nuclear transporter (ARNT) is a member of the basic helix-loop-helix/PAS (Per-ARNT-Sim) family of transcription factors, which are important for cell regulation in response to environmental conditions. ARNT is an indispensable partner of the aryl hydrocarbon receptor (AHR) or hypoxia-inducible factor-1alpha . This protein is also able to form homodimers such as ARNT/ARNT. However, the molecular mechanism that regulates the transcriptional activity of ARNT remains to be elucidated. Here, we report that ARNT is modified by SUMO-1 chiefly at Lys245 within the PAS domain of this protein, both in vivo and in vitro. Substitution of the target lysine with alanine enhanced the transcriptional potential of ARNT per se. Furthermore, green fluorescent protein-fused ARNT tended to form nuclear foci in ~20% of the transfected cells, and the foci partly colocalized with PML nuclear bodies. PML, one of the well known substrates for sumoylation, was found to augment the transcriptional activities of ARNT. ARNT bound AHR or PML, whereas the sumoylated form of ARNT associated with AHR, but not with PML, resulting in a reduced effect of PML on transactivation by ARNT. Our data suggest that the sumoylation of ARNT modulates its transcriptional role through affecting the ability of ARNT to interact with cooperative molecules such as PML. This exemplifies a crucial role of protein sumoylation in modulating protein-protein interactions.

* This work was supported by a grant-in-aid for scientific research on priority areas from the Ministry of Education, Science, Sports, and Culture of Japan (to M. N.).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.

Dagger Dagger To whom correspondence should be addressed. Tel.: 81-96-373-6800; Fax: 81-96-373-6804; E-mail: mnakao@gpo.kumamoto-u.ac.jp.

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