The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor.

@article{Kazlauskas2001TheHC,
  title={The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor.},
  author={Arūnas Kazlauskas and Sara Sundstr{\"o}m and Lorenz Poellinger and Ingemar Pongratz},
  journal={Molecular and cellular biology},
  year={2001},
  volume={21 7},
  pages={
          2594-607
        }
}
The molecular chaperone complex hsp90-p23 interacts with the dioxin receptor, a ligand-dependent basic helix-loop-helix (bHLH)/Per-Arnt-Sim domain transcription factor. Whereas biochemical and genetic evidence indicates that hsp90 is important for maintenance of a high-affinity ligand binding conformation of the dioxin receptor, the role of hsp90-associated proteins in regulation of the dioxin receptor function remains unclear. Here we demonstrate that the integrity of the hsp90 complex… CONTINUE READING
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