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J. Biol. Chem., Vol. 269, Issue 49, 30749-30752, 12, 1994
PG Heyworth, BP Bohl, GM Bokoch and JT Curnutte
When the neutrophil NADPH oxidase is activated to generate superoxide, the
cytosolic components, p47phox, p67phox, and the GTP-binding protein Rac,
become stably associated with the plasma membrane. The translocation of
p47phox and p67phox is dependent on the presence in the membrane of the
flavocytochrome b558, itself composed of two subunits, gp91phox and
p22phox. In this study we have quantitated Rac1 and Rac2 in human
neutrophils and show that > 96% of the Rac protein is Rac2 and that
chronic granulomatous disease (CGD) neutrophils contain normal levels of
the protein. We used a cell-free translocation system as well as intact
normal and CGD neutrophils to determine whether the translocation of Rac2
is dependent upon the presence of the other oxidase components. When
cell-free reactions contained any combination of normal, p47phox-deficient
or p67phox-deficient cytosol and normal or flavocytochrome b558-deficient
membranes, the GTP gamma S (guanosine 5'- 3-O-(thio)triphosphate)-dependent
association of Rac2 with the re- isolated membranes was not significantly
different from the control mixture of normal membranes and cytosol. In
intact CGD neutrophils lacking p47phox or p67phox and stimulated with
phorbol myristate acetate the translocation of Rac2 was also normal, and we
conclude that Rac translocation can occur independently of the cytosolic
NADPH oxidase components. In contrast, in the absence of flavocytochrome
b558 from intact X-chromosome linked CGD neutrophils, Rac2 translocation
was reduced to only 25% of the control value. On the basis of these
observations we propose that while Rac2 can bind to a site distinct from
either gp91phox or p22phox, it depends upon an interaction with the
flavocytochrome b558 for maximal stability in the membrane.
Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox. Evidence for its interaction with flavocytochrome b558
Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, California 92037.
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