Interaction of Rac with p67 phox and Regulation pf Phagocytic NADPH Oxidase Activity
- 22 July 1994
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 265 (5171) , 531-533
- https://doi.org/10.1126/science.8036496
Abstract
Rho and Rac, two members of the Ras superfamily of guanosine triphosphate (GTP)-binding proteins, regulate a variety of signal transduction pathways in eukaryotic cells. Upon stimulation of phagocytic cells, Rac enhances the activity of the enzyme nicotinamide adenine dinucleotide phosphate (reduced) (NADPH) oxidase, resulting in the production of superoxide radicals. Activation of the NADPH oxidase requires the assembly of a multimolecular complex at the plasma membrane consisting of two integral membrane proteins, gp91phox and p21phox, and two cytosolic proteins, p67phox and p47phox. Rac1 interacted directly with p67phox in a GTP-dependent manner. Modified forms of Rac with mutations in the effector site did not stimulate oxidase activity or bind to p67phox. Thus, p67phox appears to be the Rac effector protein in the NADPH oxidase complex.Keywords
This publication has 31 references indexed in Scilit:
- A brain serine/threonine protein kinase activated by Cdc42 and Rac1Nature, 1994
- Immunoaffinity Purification of an Oxidase-Activating Cytosolic Complex from Bovine NeutrophilsBiochemical and Biophysical Research Communications, 1993
- Direct interaction of Ras and the amino-terminal region of Raf-1 in vitroNature, 1993
- Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1Nature, 1993
- Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho.The Journal of cell biology, 1993
- The biochemical basis of the NADPH oxidase of phagocytesTrends in Biochemical Sciences, 1993
- The small GTP-binding protein rac regulates growth factor-induced membrane rufflingCell, 1992
- The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factorsCell, 1992
- Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly. Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558.Journal of Clinical Investigation, 1991
- Regulators And Effectors Of Ras ProteinsAnnual Review of Cell and Developmental Biology, 1991