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J Biol Chem, Vol. 274, Issue 19, 13198-13204, May 7, 1999
From the Departments of Immunology and Cell Biology, The Scripps
Research Institute, La Jolla, California 92037
A major function of Rac2 in neutrophils is the
regulation of oxidant production important in bacterial killing. Rac
and the related GTPase Cdc42 also regulate the dynamics of the actin
cytoskeleton, necessary for leukocyte chemotaxis and phagocytosis of
microorganisms. Although these GTPases appear to be critical downstream
components of chemoattractant receptor signaling in human neutrophils,
the pathways involved in direct control of Rac/Cdc42 activation remain to be determined. We describe an assay that measures the formation of
Rac-GTP and Cdc42-GTP based on their specific binding to the p21-binding domain of p21-activated kinase 1. A p21-binding domain glutathione S-transferase fusion protein specifically binds
Rac and Cdc42 in their GTP-bound forms both in vitro and in
cell samples. Binding is selective for Rac and Cdc42 versus
RhoA. Using this assay, we investigated Rac and Cdc42 activation in
neutrophils and differentiated HL-60 cells. The chemoattractant
fMet-Leu-Phe and the phorbol ester phorbol myristate acetate stimulate
formation of Rac-GTP and Cdc42-GTP with distinct time courses that
parallel cell activation. We also show that the signaling pathways
leading to Rac and Cdc42 activation in HL-60 cells involve G proteins sensitive to pertussis toxin, as well as tyrosine kinase and
phosphatidylinositol 3-kinase activities.
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