p47(phox) PX domain of NADPH oxidase targets cell membrane via moesin-mediated association with the actin cytoskeleton
UMass Chan Affiliations
Department of PediatricsDocument Type
Journal ArticlePublication Date
2004-07-01Keywords
ActinsAnimals
COS Cells
Cell Membrane
Cricetinae
Cytoskeleton
Humans
K562 Cells
Microfilament Proteins
NADPH Oxidase
Phospholipids
Phosphoproteins
Protein Transport
Hematology
Oncology
Pediatrics
Metadata
Show full item recordAbstract
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.Source
J Cell Biochem. 2004 Jul 1;92(4):795-809. doi: 10.1002/jcb.20084DOI
10.1002/jcb.20084Permanent Link to this Item
http://hdl.handle.net/20.500.14038/43389PubMed ID
15211576Related Resources
Link to article in PubMedae974a485f413a2113503eed53cd6c53
10.1002/jcb.20084