| http://purl.uniprot.org/citations/18347018 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18347018 | http://www.w3.org/2000/01/rdf-schema#comment | "The NADPH oxidases (Noxs) are a family of superoxide-generating enzymes implicated in a variety of biological processes. Full activity of Nox1, -2, and -3 requires the action of a Rac GTPase. A direct regulatory interaction of Rac with Nox2 has been proposed as part of a two-step mechanism for regulating electron transfer during superoxide formation. Using truncation analysis of Rac binding to the cytoplasmic tail of Nox2, along with peptides derived from this region in cell-free assays, we identify a Rac interaction site within amino acids 419-430 of Nox2. This region is required for binding Rac2 but not p47(phox) or p67(phox) cytosolic regulatory factors. A cell-permeant version of the peptide encompassing amino acids 419-430 specifically inhibits NADPH oxidase activation in intact human neutrophils. Mutational analysis of the putative Rac-binding site revealed specific residues, particularly Lys-421, Tyr-425, and Lys-426, individually required for Rac-dependent NADPH oxidase activity that are conserved in the Rac-regulated Nox1, Nox2, and Nox3 enzymes but not in Nox4 or Nox5. Mutation of the conserved residues in the Rac-binding site of Nox1 also result in the loss of Rac-dependent activity. Our data identify a functional Rac interaction site conserved in Rac-dependent Noxs and support a direct regulatory interaction of Rac GTPases to promote activation of these NADPH oxidases."xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m801010200"xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://purl.uniprot.org/core/author | "Bokoch G.M."xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://purl.uniprot.org/core/author | "Taylor R.M."xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://purl.uniprot.org/core/author | "Gianni D."xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://purl.uniprot.org/core/author | "Kao Y.Y."xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://purl.uniprot.org/core/author | "Bohl B."xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18347018 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://purl.uniprot.org/core/pages | "12736-12746"xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://purl.uniprot.org/core/title | "Identification of a conserved Rac-binding site on NADPH oxidases supports a direct GTPase regulatory mechanism."xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://purl.uniprot.org/core/volume | "283"xsd:string |
| http://purl.uniprot.org/citations/18347018 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18347018 |
| http://purl.uniprot.org/citations/18347018 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18347018 |
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