Phosphorylation of the human retinoid X receptor alpha at serine 260 impairs coactivator(s) recruitment and induces hormone resistance to multiple ligands.

@article{Macoritto2008PhosphorylationOT,
  title={Phosphorylation of the human retinoid X receptor alpha at serine 260 impairs coactivator(s) recruitment and induces hormone resistance to multiple ligands.},
  author={Michael Macoritto and Loan Nguyen-Yamamoto and Dao Huang and Sara M. Samuel and Xian Fang Yang and Tian Tian Wang and John H. White and Richard Kremer},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 8},
  pages={4943-56}
}
The retinoid X receptor alpha (RXRalpha) is a member of the nuclear receptor superfamily that regulates transcription of target genes through heterodimerization with several partners, including peroxisome proliferator-activated receptor, retinoic acid receptor, thyroid receptor, and vitamin D receptor (VDR). We have shown previously that signaling through VDR.RXRalpha heterodimers was attenuated in ras-transformed keratinocytes due to phosphorylation of serine 260 of the RXRalpha via the… CONTINUE READING

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