Phosphorylation of the leucocyte NADPH oxidase subunit p47(phox) by casein kinase 2: conformation-dependent phosphorylation and modulation of oxidase activity.

@article{Park2001PhosphorylationOT,
  title={Phosphorylation of the leucocyte NADPH oxidase subunit p47(phox) by casein kinase 2: conformation-dependent phosphorylation and modulation of oxidase activity.},
  author={H S Park and Sun min Lee and Jung Hyun Lee and Yu Sam Kim and Young Suk Bae and Junguk Park},
  journal={The Biochemical journal},
  year={2001},
  volume={358 Pt 3},
  pages={783-90}
}
The leucocyte NADPH oxidase of neutrophils is a membrane-bound enzyme that catalyses the reduction of oxygen to O(-)(2) at the expense of NADPH. The enzyme is dormant in resting neutrophils but becomes active when the cells are exposed to the appropriate stimuli. During oxidase activation, the highly basic cytosolic oxidase component p47(phox) becomes phosphorylated on several serines and migrates to the plasma membrane. Protein kinase CK2 is an essential serine/threonine kinase present in all… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 17 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 61 references

Characterization of protein interaction among subunits of protein kinase CKII in vivo and in vitro

  • Kim, M.-S, +5 authors Y. S. Bae
  • Mol. Cells
  • 1998

Kinase - dependentactivation of the leukocyte NADPH oxidase in a cell - free system . Phosphorylation of membranes and p 47 phox during oxidase activation

  • J.-W. Park, C. R. Hoyal, J. El Benna, B. M. Babior
  • J . Biol . Chem .
  • 1997

Similar Papers

Loading similar papers…