Localizing NADPH Oxidase–Derived ROS

See allHide authors and affiliations

Science's STKE  22 Aug 2006:
Vol. 2006, Issue 349, pp. re8
DOI: 10.1126/stke.3492006re8

You are currently viewing the gloss.

View Full Text


This STKE Review, with 3 figures and 55 citations, describes evidence for localized production of reactive oxygen species in targeted or polarized cell movement. Targeting of NADPH (nicotinamide adenine dinucleotide phosphate) oxidase to the focal complexes in lamellipodia and membrane ruffles of cells provides a mechanism for achieving localized ROS production. This targeting is achieved by the interaction of the p47phox subunit of the NADPH oxidase with various scaffold proteins such as TRAF4 and WAVE1. ROS are believed to inactivate protein tyrosine phosphatases, thereby establishing a positive feedback system that promotes directed cell migration. Additionally, ROS production may be localized through interactions of NADPH oxidase with signaling platforms associated with lipid rafts and caveolae, as well as with endosomes and the nucleus. These mechanisms may explain how localized ROS activate discrete signaling pathways.