| Autor: |
Ellson, Chris D., Gobert-Gosse, Stéphanie, Anderson, Karen E, Davidson, Keith, Erdjument-Bromage, Hediye, Tempst, Paul, Thuring, Jan W., Cooper, Matthew A., Lim, Ze-Yi, Holmes, Andrew B., Gaffney, Piers R. J., Coadwell, John, Chilvers, Edwin R., Hawkins, Phill T., Stephens, Len R. |
| Předmět: |
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| Zdroj: |
Nature Cell Biology; Jul2001, Vol. 3 Issue 7, p679, 4p |
| Abstrakt: |
The production of reactive oxygen species (ROS) by neutrophils has a vital role in defence against a range of infectious agents, and is driven by the assembly of a multi-protein complex containing a minimal core of five proteins: the two membrane-bound subunits of cytochrome b[sub 558] (gp91[sup phox] and p22[sup phox]) and three soluble factors (GTP-Rac, p47[sup phox] and p67[sup phox] (refs 1, 2). This minimal complex can reconstitute ROS formation in vitro in the presence of non-physiological amphiphiles such as SDS. p40[sup phox] has subsequently been discovered as a binding partner for p67[sup phox] (ref. 3), but its role in ROS formation is unclear. Phosphoinositide-3-OH kinases (PI(3)Ks) have been implicated in the intracellular signalling pathways coordinating ROS formation but through an unknown mechanism. We show that the addition of p40[sup phox] to the minimal core complex allows a lipid product of PI(3)Ks, phosphatidylinositol 3-phosphate (PtdIns(3)P), to stimulate specifically the formation of ROS. This effect was mediated by binding of PtdIns(3)P to the PX domain of p40[sup phox]. These results offer new insights into the roles for PI(3)Ks and p40[sup phox] in ROS formation and define a cellular ligand for the orphan PX domain. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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