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

REVIEWS

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).

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Novel p47phox-Related Organizers Regulate Localized NADPH Oxidase 1 (Nox1) Activity.
D. Gianni, B. Diaz, N. Taulet, B. Fowler, S. A. Courtneidge, and G. M. Bokoch (2009)
Science Signaling 2, ra54
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Subcellular localization of Nox4 and regulation in diabetes.
K. Block, Y. Gorin, and H. E. Abboud (2009)
PNAS 106, 14385-14390
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NADPH Oxidase 1 Controls the Persistence of Directed Cell Migration by a Rho-Dependent Switch of {alpha}2/{alpha}3 Integrins.
A. Sadok, A. Pierres, L. Dahan, C. Prevot, M. Lehmann, and H. Kovacic (2009)
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Depleting Rac1 in mouse rod photoreceptors protects them from photo-oxidative stress without affecting their structure or function.
M. Haruta, R. A. Bush, S. Kjellstrom, C. Vijayasarathy, Y. Zeng, Y.-Z. Le, and P. A. Sieving (2009)
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Evidence for a Superoxide Permeability Pathway in Endosomal Membranes.
D. R. Mumbengegwi, Q. Li, C. Li, C. E. Bear, and J. F. Engelhardt (2008)
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G Protein-Coupled Receptor Ca2+-Linked Mitochondrial Reactive Oxygen Species Are Essential for Endothelial/Leukocyte Adherence.
B. J. Hawkins, L. A. Solt, I. Chowdhury, A. S. Kazi, M. R. Abid, W. C. Aird, M. J. May, J. K. Foskett, and M. Madesh (2007)
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