Hyperphosphorylation of the retinoid X receptor α by activated c-Jun NH2-terminal kinases
S Adam-Stitah, L Penna, P Chambon… - Journal of Biological …, 1999 - ASBMB
The nuclear receptor mouse retinoid X receptor α (mRXRα) was shown to be constitutively
phosphorylated in its NH 2-terminal A/B region, which contains potential phosphorylation
sites for proline-directed Ser/Thr kinases. Mutants for each putative site were generated and
overexpressed in transfected COS-1 cells. Constitutively phosphorylated residues identified
by tryptic phosphopeptide mapping included serine 22 located in the A1 region that is
specific to the RXRα1 isoform. Overexpression and UV activation of the stress-activated …
phosphorylated in its NH 2-terminal A/B region, which contains potential phosphorylation
sites for proline-directed Ser/Thr kinases. Mutants for each putative site were generated and
overexpressed in transfected COS-1 cells. Constitutively phosphorylated residues identified
by tryptic phosphopeptide mapping included serine 22 located in the A1 region that is
specific to the RXRα1 isoform. Overexpression and UV activation of the stress-activated …
