Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation.

@article{Ago2003PhosphorylationOP,
  title={Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation.},
  author={Tetsuro Ago and Futoshi Kuribayashi and Hidekazu Hiroaki and Ryu Takeya and Takashi Ito and Daisuke Kohda and Hideki Sumimoto},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 8},
  pages={4474-9}
}
Protein-phosphoinositide interaction participates in targeting proteins to membranes where they function correctly and is often modulated by phosphorylation of lipids. Here we show that protein phosphorylation of p47(phox), a cytoplasmic activator of the microbicidal phagocyte oxidase (phox), elicits interaction of p47(phox) with phosphoinositides. Although the isolated phox homology (PX) domain of p47(phox) can interact directly with phosphoinositides, the lipid-binding activity of this… CONTINUE READING
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Membrane Proteins: Structure, Function and Expression Control, eds

  • H. Sumimoto, T. Ito, +6 authors K. Takeshige
  • 1997

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