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J. Biol. Chem., Vol. 276, Issue 46, 43231-43238, November 16, 2001
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From the Department of Cell and Molecular Biology, Karolinska
Institutet, Stockholm S-171 77, Sweden
The dioxin receptor belongs to the basic
helix-loop helix/Per-Arnt-Sim (bHLH)/PAS family of proteins and
functions as a ligand-dependent transcription factor to
activate target genes. The function of the PAS domain of the dioxin
receptor is only partially understood. Whereas the C-terminal half of
the PAS domain has been shown to harbor ligand binding activity and to
function as an accessory dimerization interface, the precise functional
role of the N-terminal half of the PAS domain remains unclear. We have
previously shown that this domain confers dimerization specificity to
the dioxin receptor. Here we report the identification and
characterization of a novel nuclear export sequence (NES) motif,
located in the N-terminal portion of the PAS domain, in addition to the
previously identified NES in the bHLH domain. By point mutagenesis, we
have generated a dominant positive form of the PAS domain NES motif that inhibits accumulation of the dioxin receptor in the nuclear compartment of the cell. This mutant form of the receptor was furthermore unable to sustain reporter gene activation. Importantly, we
demonstrate that the ligand-free and ligand-occupied forms of the
dioxin receptor differentially employ the two NES motifs. In the
absence of ligand, nuclear export is sustained via the PAS domain NES,
whereas following ligand-dependent activation nuclear
export of the receptor is mediated by the NES in the bHLH domain.
Differential Usage of Nuclear Export Sequences
Regulates Intracellular Localization of the Dioxin (Aryl Hydrocarbon)
Receptor*
*
This work was supported by the Swedish Cancer Society.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.
Supported by the Swedish Medical Research Council. To whom
correspondence should be addressed. Tel.: 46-8-728-7336; Fax:
46-8-34-8819; E-mail: Ingemar.Pongratz@cmb.ki.se.
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