The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor.

@article{Kazlauskas2000TheIP,
  title={The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor.},
  author={Arūnas Kazlauskas and Lorenz Poellinger and Ingemar Pongratz},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 52},
  pages={
          41317-24
        }
}
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… CONTINUE READING

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