Acetylation-Dependent Signal Transduction for Type I Interferon Receptor

@article{Tang2007AcetylationDependentST,
  title={Acetylation-Dependent Signal Transduction for Type I Interferon Receptor},
  author={Xiaoli Tang and Jin-song Gao and Ying-Jie Guan and Katya E. McLane and Zheng-long Yuan and Bharat Ramratnam and Y Eugene Chin},
  journal={Cell},
  year={2007},
  volume={131},
  pages={93-105}
}
Cytokine-activated receptors initiate intracellular signaling by recruiting protein kinases that phosphorylate the receptors on tyrosine residues, thus enabling docking of SH2 domain-bearing activating factors. Here we report that in response to type 1 interferon (IFNalpha), IFNalpha receptors recruit cytoplasmic CREB-binding protein (CBP). By binding to IFNalphaR2 within the region where two adjacent proline boxes bear phospho-Ser364 and phospho-Ser384, CBP acetylates IFNalphaR2 on Lys399… CONTINUE READING

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