Dual Role of Rac in the Assembly of NADPH Oxidase, Tethering to the Membrane and Activation of p67phox
- R. Sarfstein, Y. Gorzalczany, E. Pick
- Biology, ChemistryJournal of Biological Chemistry
- 16 April 2004
It is reported that a chimeric construct, consisting of residues 1–212 of p67phox and full-length Rac1, activates the oxidase in vitro in anamphiphile-dependent manner, and when prenylated, in the absence of amphiphile and p47phox, demonstrating that Rac has a dual role in the assembly of NADPH oxidase.
Assembly of the phagocyte NADPH oxidase complex: chimeric constructs derived from the cytosolic components as tools for exploring structure‐function relationships
- Ariel Mizrahi, Y. Berdichevsky, E. Pick
- BiologyJournal of Leukocyte Biology
- 1 May 2006
A “propagated wave” model of NADPH oxidase activation is proposed in which a conformational change initiated in Rac is propagated to p67phox and from p 67phox to gp91phox, as demonstrated by fluorescence resonance energy transfer, small angle X‐ray scattering, and gel filtration.
Activation of the Phagocyte NADPH Oxidase by Rac Guanine Nucleotide Exchange Factors in Conjunction with ATP and Nucleoside Diphosphate Kinase*
- Ariel Mizrahi, S. Molshanski-Mor, C. Weinbaum, Yi Zheng, M. Hirshberg, E. Pick
- BiologyJournal of Biological Chemistry
- 4 February 2005
It is shown that Trio and another Rac GEF (Tiam1) act by inducing GDP to GTP exchange on prenylated Rac1-GDP and that earlier assertion that activation is GTP-independent is explained by contamination of p67phox preparations with GTP and/or ATP.
Rational design of small molecule inhibitors targeting the Rac GTPase-p67(phox) signaling axis in inflammation.
- E. Bosco, Sachin Kumar, Yi Zheng
- Biology, ChemistryChemistry and Biology
- 24 February 2012
A Prenylated p47phox-p67phox-Rac1 Chimera Is a Quintessential NADPH Oxidase Activator
- Ariel Mizrahi, Y. Berdichevsky, P. Casey, E. Pick
- Biology, ChemistryJournal of Biological Chemistry
- 7 June 2010
Prenylation of the GFP-trimera supersedes completely the dependence of oxidase activation on the p47phox phox homology domain and, partially, on the Rac1 polybasic domain, but the requirement for Trp193 in p 47phox persists.
Tripartite Chimeras Comprising Functional Domains Derived from the Cytosolic NADPH Oxidase Components p47phox, p67phox, and Rac1 Elicit Activator-independent Superoxide Production by Phagocyte…
- Y. Berdichevsky, Ariel Mizrahi, Yelena Ugolev, S. Molshanski-Mor, E. Pick
- BiologyJournal of Biological Chemistry
- 27 July 2007
The trimera had a higher affinity for and formed a more stable complex with cytochrome b559 compared with the combined individual components, full-length or truncated, and was capable of oxidase activation in vitro in the presence of an anionic amphiphile.
Cell-free assays: the reductionist approach to the study of NADPH oxidase assembly, or "all you wanted to know about cell-free assays but did not dare to ask".
- S. Molshanski-Mor, Ariel Mizrahi, Yelena Ugolev, I. Dahan, Y. Berdichevsky, E. Pick
- BiologyMethods in molecular biology
- 2007
Cell-free assays played a paramount role in the identification of the components of the NADPH oxidase complex, the diagnosis of various forms of chronic granulomatous disease (CGD), and, more recently, the analysis of the domains present on the components in protein-protein interactions leading to the assembly of the active complex.