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Papers In Press, published online ahead of print March 14, 2002
J. Biol. Chem, 10.1074/jbc.M200061200
Submitted on January 3, 2002
Revised on March 6, 2002
Accepted on March 13, 2002

Rac activation induces NADPH oxidase activity in transgenic COSphox cells and level of superoxide production is exchange factor-dependent

Marianne O. Price, Simon J. Atkinson, Ulla G. Knaus, and Mary C. Dinauer

Pediatrics (Hematology/Oncology) and Medical and Molecular Genetics, James Whitcomb Riley Hospital for Children, Indianapolis, IN 46202-5225

Corresponding Author: mdinauer{at}iupui.edu

Transient expression of constitutively active Rac1 derivatives, (G12V) or (Q61L), was sufficient to induce phagocyte NAPDH oxidase activity in a COS-7 cell model in which human cDNAs for essential oxidase components, gp91phox, p22phox, p47phox and p67phox, were expressed as stable transgenes. Expression of constitutively active Rac1 in “COSphox” cells induced translocation of p47phox and p67phox to the membrane. Furthermore, translocation of p47phox was induced in the absence of p67phox expression, even though Rac does not directly bind p47phox. Rac effector domain point substitutions (A27K, G30S, D38A, Y40C), which can selectively eliminate interaction with different effector proteins, impaired Rac1V12-induced superoxide production. Activation of endogenous Rac1 by expression of constitutively active Rac-GEF derivatives was sufficient to induce high-level NADPH oxidase activity in COSphox cells. The constitutively active form of the hematopoietic-specific GEF, Vav1, was the most effective at activating superoxide production, despite detection of higher levels of Rac1-GTP upon expression of constitutively active Vav2 or Tiam1 derivatives. These data suggest that Rac can play a dual role in NADPH oxidase activation, both by directly participating in the oxidase complex and by activating signaling events leading to oxidase assembly, and that Vav1 may be the physiologically relevant GEF responsible for activating this Rac-regulated complex.


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