Phosphorylation of human vitamin D receptor serine-182 by PKA suppresses 1,25(OH)2D3-dependent transactivation.

@article{Hsieh2004PhosphorylationOH,
  title={Phosphorylation of human vitamin D receptor serine-182 by PKA suppresses 1,25(OH)2D3-dependent transactivation.},
  author={Jui-Cheng Hsieh and Hope T L Dang and Michael A. Galligan and Grahame Whitfield and Carol A. Haussler and Peter W Jurutka and Mark R. Haussler},
  journal={Biochemical and biophysical research communications},
  year={2004},
  volume={324 2},
  pages={801-9}
}
The human vitamin D receptor (hVDR), which is a substrate for several protein kinases, mediates the actions of its 1,25-dihydroxyvitamin D3 (1,25(OH)2D3) ligand to regulate gene expression. To determine the site, and functional impact, of cAMP-dependent protein kinase (PKA)-catalyzed phosphorylation of hVDR, we generated a series of C-terminally truncated… CONTINUE READING