p47phox PX domain of NADPH oxidase targets cell membrane via moesin-mediated association with the actin cytoskeleton
✍ Scribed by Yong Zhan; Dandan He; Peter E. Newburger; G. Wayne Zhou
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 737 KB
- Volume
- 92
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
Abstract
Activation of phagocytic NADPH oxidase requires association of its cytosolic subunits with the membrane‐bound flavocytochrome. Extensive phosphorylation of the p47^phox^ subunit of NADPH oxidase marks the initiation of this activation process. The p47^phox^ subunit then translocates to the plasma membrane, bringing the p67^phox^ subunit to cytochrome b558 to form the active NADPH oxidase complex. However, the detailed mechanism for targeting the p47^phox^ subunit to the cell membrane during activation still remains unclear. Here, we show that the p47^phox^ PX domain is responsible for translocating the p47^phox^ subunit to the plasma membrane for subsequent activation of NADPH oxidase. We also demonstrate that translocation of the p47^phox^ PX domain to the plasma membrane is not due to interactions with phospholipids but rather to association with the actin cytoskeleton. This association is mediated by direct interaction between the p47^__pho__x^ PX domain and moesin. © 2004 Wiley‐Liss, Inc.