ArticleMolecular biology of the cell1993
Requirement for posttranslational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase.
Article in Molecular biology of the cell, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 126 citations in OpenAlex.
- The small GTPase Rap1A expedites the NOX2 oxidative burst by facilitating Rac and NOX2 autoactivations.The FEBS journal · 2025Article
- The role of magnesium in different inflammatory diseases.Inflammopharmacology · 2019Review
- Carcinogenesis and Reactive Oxygen Species Signaling: Interaction of the NADPH Oxidase NOX1-5 and Superoxide Dismutase 1-3 Signal Transduction Pathways.Antioxidants & redox signaling · 2019Review
- Intracellular cAMP Sensor EPAC: Physiology, Pathophysiology, and Therapeutics Development.Physiological reviews · 2018Review
- Review
- Role of the Rho GTPase Rac in the activation of the phagocyte NADPH oxidase: outsourcing a key task.Small GTPases · 2014Review
- Matrix compliance regulates Rac1b localization, NADPH oxidase assembly, and epithelial-mesenchymal transition.Molecular biology of the cell · 2012Article
- Selective Rac1 inhibition protects renal tubular epithelial cells from oxalate-induced NADPH oxidase-mediated oxidative cell injury.Urological research · 2012Article
- Modulation of RhoGTPases improves the behavioral phenotype and reverses astrocytic deficits in a mouse model of Rett syndrome.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2012Article
- A prenylated p47phox-p67phox-Rac1 chimera is a Quintessential NADPH oxidase activator: membrane association and functional capacity.The Journal of biological chemistry · 2010Article
- Identification of a conserved Rac-binding site on NADPH oxidases supports a direct GTPase regulatory mechanism.The Journal of biological chemistry · 2008Article
- Capturing proteins that bind polyunsaturated fatty acids: demonstration using arachidonic acid and eicosanoids.Lipids · 2008Article
- Mechanisms of degranulation in neutrophils.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2006Article
- The molecular basis for adhesion-mediated suppression of reactive oxygen species generation by human neutrophils.The Journal of clinical investigation · 2003Article
- Assembly of the neutrophil respiratory burst oxidase: a direct interaction between p67PHOX and cytochrome b558.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex.The Journal of cell biology · 2000Article
- Profilin enhances Cdc42-induced nucleation of actin polymerization.The Journal of cell biology · 2000Article
- Rho GTPase signaling in inflammation and transformation.Immunologic research · 2000Review
- Pseudomonas aeruginosa hemolytic phospholipase C suppresses neutrophil respiratory burst activity.Infection and immunity · 1999Article
- RacF1, a novel member of the Rho protein family in Dictyostelium discoideum, associates transiently with cell contact areas, macropinosomes, and phagosomes.Molecular biology of the cell · 1999Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Rac1 and Rac2 are closely related, low molecular weight GTP-binding proteins that have both been implicated in regulation of phagocyte NADPH oxidase. This enzyme system is composed of multiple membrane-bound and cytosolic subunits and when activated catalyzes the one-electron reduction of oxygen to superoxide. Superoxide and its highly reactive derivatives are essential for killing microorganisms. Rac proteins undergo posttranslational processing, primarily the addition of an isoprenyl group to a carboxyl-terminal cysteine residue. We directly compared recombinant Rac1 and Rac2 in a human neutrophil cell-free NADPH oxidase system in which cytosol was replaced by purified recombinant cytosolic components (p47-phox and p67-phox). Processed Rac1 and Rac2 were both highly active in this system and supported comparable rates of superoxide production. Under different cell-free conditions, however, in which suboptimal amounts of cytosol were present in the assay mixture, processed Rac2 worked much better than Rac1 at all but the lowest concentrations. This suggests that a factor in the cytosol may suppress the activity of Rac1 but not of Rac2. Unprocessed Rac proteins were only weakly able to support superoxide generation in either system, but preloading of Rac1 or Rac2 with guanosine 5'-O-(3-thio-triphosphate) (GTP gamma S) restored activity. These results indicate that processing is required for nucleotide exchange but not for interaction with oxidase components.
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