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Papers In Press, published online ahead of print September 26, 2002
Regeneration Medicine, Institute of Molecular Embryology and Genetics, Kumamoto, Kumamoto 860-0811
Corresponding Author: mnakao{at}gpo.kumamoto-u.ac.jp
The aryl hydrocarbon receptor nuclear transporter (ARNT) is a member of the basic helix-loop-helix Per-ARNT-Sim (bHLH-PAS) transcriptional factors, which are important for cell regulation in response to environmental conditions. ARNT is an indispensable partner to the aryl hydrocarbon receptor (AHR) or hypoxia-inducible factor 1a (HIF1a). 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 lysine 245 within the PAS domain of this protein, both in vivo and in vitro. Substitution of the target lysine to alanine enhances the transcriptional potential of ARNT per se. Furthermore, the green fluorescent protein-fused ARNT tends to form nuclear foci in about 20 % of the transfected cells, and the foci partly colocalize with PML-nuclear bodies. PML, one of the well-known substrates for sumoylation, is found to augment the transcriptional activities of ARNT. ARNT binds AHR or PML, meanwhile the sumoylated form of ARNT associates with AHR but not with PML, resulting in a reduced effect of PML on the 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.
J. Biol. Chem, 10.1074/jbc.M205987200
Submitted on June 17, 2002
Revised on September 26, 2002
Accepted on September 26, 2002
The Aryl hydrocarbon receptor nuclear transporter is modulated by the SUMO-1 conjugating system
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