Transcriptional activation by peroxisome proliferator-activated receptor gamma is inhibited by phosphorylation at a consensus mitogen-activated protein kinase site.

@article{Adams1997TranscriptionalAB,
  title={Transcriptional activation by peroxisome proliferator-activated receptor gamma is inhibited by phosphorylation at a consensus mitogen-activated protein kinase site.},
  author={Maria D. Adams and Mauricio J Reginato and Deng Shao and Mitchell A Lazar and V. Krishna K. Chatterjee},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 8},
  pages={
          5128-32
        }
}
The nuclear receptor peroxisome proliferator-activated receptor gamma (PPARgamma) regulates transcription in response to prostanoid and thiazolidinedione ligands and promotes adipocyte differentiation. The amino-terminal A/B domain of this receptor contains a consensus mitogen-activated protein kinase site in a region common to PPARgamma1 and -gamma2 isoforms. The A/B domain of human PPARgamma1 was phosphorylated in vivo, and this was abolished either by mutation of serine 84 to alanine (S84A… CONTINUE READING

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