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J. Biol. Chem., Vol. 275, Issue 52, 41317-41324, December 29, 2000
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From the Department of Cell and Molecular Biology, Karolinska
Institute, S-171 77 Stockholm, Sweden
The dioxin (aryl hydrocarbon) receptor is a
ligand-dependent transcription factor that induces
expression of a number of genes encoding drug metabolizing enzymes. The
nonactivated form of the dioxin receptor is associated with heat shock
protein (hsp) 90, the co-chaperone p23, and the immunophilin-like
protein XAP2. Whereas hsp90 has a role in maintenance of the
high-affinity ligand binding conformation of the dioxin receptor
complex, and p23 stabilizes receptor-hsp90 interaction, the exact role
of XAP2 is largely unknown. Here we show that XAP2 protected the
ligand-free form of receptor against ubiquitination, resulting in
increased dioxin receptor protein levels. Upon exposure to ligand,
nuclear translocation of the dioxin receptor was markedly delayed by
XAP2, indicating an additional role of XAP2 in regulation of the
subcellular localization of the receptor by a mechanism of cytoplasmic
retention. In order to mediate these effects, XAP2 required stable
association with the hsp90-p23 molecular chaperone complex. The
association of XAP2 as well as p23 with the dioxin receptor was
determined by the functional state of hsp90. These data indicate a
novel mode of regulation of dioxin receptor signaling by the
hsp90-dependent molecular chaperone machinery.
The Immunophilin-like Protein XAP2 Regulates Ubiquitination and
Subcellular Localization of the Dioxin Receptor*
, and
*
This work was supported in part by the Swedish Cancer
Society and the Swedish Society for Medical Research.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: Dept. of Cell and
Molecular Biology, Karolinska Institute, S-171-77 Stockholm, Sweden.
Tel.: 46-8-728-7330; Fax: 46-8-34-88-19; E-mail:
lorenz.poellinger@cmb.ki.se.
§
Supported by the Swedish Medical Research Council.
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