ArticleThe Biochemical journal2001
Phosphorylation of the leucocyte NADPH oxidase subunit p47(phox) by casein kinase 2: conformation-dependent phosphorylation and modulation of oxidase activity.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 49 citations in OpenAlex.
- Review
- The Emerging Roles of Nicotinamide Adenine Dinucleotide Phosphate Oxidase 2 in Skeletal Muscle Redox Signaling and Metabolism.Antioxidants & redox signaling · 2019Review
- Inhibition of Casein Kinase 2 Disrupts Differentiation of Myeloid Cells in Cancer and Enhances the Efficacy of Immunotherapy in Mice.Cancer research · 2018Article
- Markers and Biomarkers of Endothelium: When Something Is Rotten in the State.Oxidative medicine and cellular longevity · 2017Review
- 5d, a novel analogue of 3-n-butylphthalide, decreases NADPH oxidase activity through the positive regulation of CK2 after ischemia/reperfusion injury.Oncotarget · 2016Article
- S-Nitrosylation of p47(phox) enhances phosphorylation by casein kinase 2.Redox report : communications in free radical research · 2015Article
- Regulation of cytoskeletal dynamics by redox signaling and oxidative stress: implications for neuronal development and trafficking.Frontiers in cellular neuroscience · 2015Review
- Nitroarachidonic acid prevents NADPH oxidase assembly and superoxide radical production in activated macrophages.Free radical biology & medicine · 2013Article
- Targeting microglia-mediated neurotoxicity: the potential of NOX2 inhibitors.Cellular and molecular life sciences : CMLS · 2012Review
- Cell signaling through protein kinase C oxidation and activation.International journal of molecular sciences · 2012Review
- Endothelial dysfunction in diabetes: multiple targets for treatment.Pflugers Archiv : European journal of physiology · 2010Review
- CK2 is a novel negative regulator of NADPH oxidase and a neuroprotectant in mice after cerebral ischemia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- p47phox, the phagocyte NADPH oxidase/NOX2 organizer: structure, phosphorylation and implication in diseases.Experimental & molecular medicine · 2009Review
- Small interfering peptide (siP) for in vivo examination of the developing lung interactonome.Developmental dynamics : an official publication of the American Association of Anatomists · 2009Article
- Casein kinase 2 regulates the active uptake of the organic osmolyte taurine in NIH3T3 mouse fibroblasts.Pflugers Archiv : European journal of physiology · 2008Article
- Hemoglobin neurotoxicity is attenuated by inhibitors of the protein kinase CK2 independent of heme oxygenase activity.Current neurovascular research · 2008Article
- Perturbation of actin dynamics induces NF-kappaB activation in myelomonocytic cells through an NADPH oxidase-dependent pathway.The Biochemical journal · 2005Article
- Activation and assembly of the NADPH oxidase: a structural perspective.The Biochemical journal · 2005Review
- The NADPH oxidase of professional phagocytes--prototype of the NOX electron transport chain systems.Biochimica et biophysica acta · 2004Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 eukaryotic organisms. The leucocyte NADPH oxidase subunit p47(phox) has several putative CK2 phosphorylation sites. In the present study, we report that CK2 is able to catalyse the phosphorylation of p47(phox) in vitro. Phosphoamino acid analysis of phosphorylated p47(phox) by CK2 indicated that the phosphorylation occurs on serine residues. CNBr mapping and phosphorylation of peptides containing the putative site of CK2 indicated that the main phosphorylated residues are Ser-208 and Ser-283 in the Src homology 3 (SH3) domains, and Ser-348 in the C-terminal domain of p47(phox). Dependence of phosphorylation on the conformation of p47(phox) is supported by the finding that p47(phox) undergoes better phosphorylation by CK2 in the presence of arachidonic acid, a known activator of NADPH oxidase which induces conformational changes in p47(phox). In addition, 5,6-dichloro-1-beta-o-ribofuranosyl benzimidazole, a CK2 inhibitor, potentiates formyl-Met-Leu-Phe-induced NADPH oxidase activity in DMSO-differentiated HL-60 cells. Taken together, we propose that CK2 is the p47(phox) kinase, and that phosphorylation of p47(phox) by CK2 regulates the deactivation of NADPH oxidase.
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