Phosphorylation of a conserved serine in the deoxyribonucleic acid binding domain of nuclear receptors alters intracellular localization.

@article{Sun2007PhosphorylationOA,
  title={Phosphorylation of a conserved serine in the deoxyribonucleic acid binding domain of nuclear receptors alters intracellular localization.},
  author={Kai Sun and Vedrana Montana and Karthikeyani Chellappa and Yann Brelivet and Dino Moras and Yutaka Maeda and Vladimir Parpura and Bryce M. Paschal and Frances M. Sladek},
  journal={Molecular endocrinology},
  year={2007},
  volume={21 6},
  pages={1297-311}
}
Nuclear receptors (NRs) are a superfamily of transcription factors whose genomic functions are known to be activated by lipophilic ligands, but little is known about how to deactivate them or how to turn on their nongenomic functions. One obvious mechanism is to alter the nuclear localization of the receptors. Here, we show that protein kinase C (PKC) phosphorylates a highly conserved serine (Ser) between the two zinc fingers of the DNA binding domain of orphan receptor hepatocyte nuclear… CONTINUE READING
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