The hsp90 Co-chaperone XAP2 alters importin beta recognition of the bipartite nuclear localization signal of the Ah receptor and represses transcriptional activity.

@article{Petrulis2003TheHC,
  title={The hsp90 Co-chaperone XAP2 alters importin beta recognition of the bipartite nuclear localization signal of the Ah receptor and represses transcriptional activity.},
  author={John R. Petrulis and Ann Kusnadi and Preeti Ramadoss and Brett D. Hollingshead and Gary H Perdew},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 4},
  pages={
          2677-85
        }
}
The mouse aryl hydrocarbon receptor (mAhR) is a ligand-activated transcription factor that exists in a tetrameric, core complex with a dimer of the 90-kDa heat shock protein, and the hepatitis B virus X-associated protein 2 (XAP2). Transiently expressed mAhR-YFP (yellow fluorescent protein fused with the mAhR) localizes throughout cells, with a majority occupying nuclei. Co-expression of XAP2 with mAhR-YFP results in a distinct redistribution to the cytoplasm. We have utilized several… CONTINUE READING

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