p47(phox) PX domain of NADPH oxidase targets cell membrane via moesin-mediated association with the actin cytoskeleton

UMMS Affiliation

Department of Pediatrics

Publication Date


Document Type



Actins; Animals; COS Cells; Cell Membrane; Cricetinae; Cytoskeleton; Humans; K562 Cells; Microfilament Proteins; NADPH Oxidase; Phospholipids; Phosphoproteins; Protein Transport


Hematology | Oncology | Pediatrics


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(phox) PX domain and moesin.

DOI of Published Version



J Cell Biochem. 2004 Jul 1;92(4):795-809. doi: 10.1002/jcb.20084

Journal/Book/Conference Title

Journal of cellular biochemistry

Related Resources

Link to article in PubMed

PubMed ID