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Sci. STKE, 22 August 2006
Vol. 2006, Issue 349, p. re8
[DOI: 10.1126/stke.3492006re8]

Localizing NADPH Oxidase–Derived ROS

Masuko Ushio-Fukai*

Department of Pharmacology and Center for Lung and Vascular Biology, University of Illinois College of Medicine, Chicago, IL 60612, USA.

Gloss: 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.

*Corresponding author. E-mail: mfukai{at}uic.edu

Citation: M. Ushio-Fukai, Localizing NADPH Oxidase–Derived ROS. Sci. STKE 2006, re8 (2006).

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