Assembly of the neutrophil respiratory burst oxidase: A direct interaction between p67PHOX and cytochrome b558 II
AUTOR(ES)
Dang, Pham My-Chan
FONTE
The National Academy of Sciences
RESUMO
Activation of the phagocyte NADPH oxidase complex requires assembly of the cytosolic factors p47PHOX, p67PHOX, p40PHOX, and Rac with the membrane-bound cytochrome b558. We recently established a direct interaction between p67PHOX and cytochrome b558. In the present study, we show that removal of the C-terminal domain of p67PHOX increased its binding to cytochrome b558. Whereas phosphorylated p40PHOX alone did not bind to cytochrome b558, phosphorylated p47PHOX did, and, moreover, it allowed the binding of p40PHOX to the cytochrome. Furthermore, both increased the binding of p67PHOX to the cytochrome. Phosphorylated p47PHOX thus appears to increase the binding of p67PHOX to cytochrome b558 by serving as an adapter, bringing p67PHOX into proximity with cytochrome b558, whereas phosphorylated p40PHOX may increase the binding by inducing a conformational change that allows p67PHOX to interact fully with cytochrome b558.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=123636Documentos Relacionados
- Assembly of the neutrophil respiratory burst oxidase: A direct interaction between p67PHOX and cytochrome b558
- Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly. Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558.
- A point mutation in gp91-phox of cytochrome b558 of the human NADPH oxidase leading to defective translocation of the cytosolic proteins p47-phox and p67-phox.
- Inhibitory effect of porcine surfactant on the respiratory burst oxidase in human neutrophils. Attenuation of p47phox and p67phox membrane translocation as the mechanism.
- Reactive oxygen species and neutrophil respiratory burst cytochrome b558 are produced by kidney glomerular cells in passive Heymann nephritis.