{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kuihon SVNP"],"funding":["American Heart Association Inc","National Institutes of Health"],"pagination":["107130"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10979099"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["300(4)"],"pubmed_abstract":["The actin cytoskeleton and reactive oxygen species (ROS) both play crucial roles in various cellular processes. Previous research indicated a direct interaction between two key components of these systems: the WAVE1 subunit of the WAVE regulatory complex (WRC), which promotes actin polymerization and the p47<sup>phox</sup> subunit of the NADPH oxidase 2 complex (NOX2), which produces ROS. Here, using carefully characterized recombinant proteins, we find that activated p47<sup>phox</sup> uses its dual Src homology 3 domains to bind to multiple regions within the WAVE1 and Abi2 subunits of the WRC, without altering WRC's activity in promoting Arp2/3-mediated actin polymerization. Notably, contrary to previous findings, p47<sup>phox</sup> uses the same binding pocket to interact with both the WRC and the p22<sup>phox</sup> subunit of NOX2, albeit in a mutually exclusive manner. This observation suggests that when activated, p47<sup>phox</sup> may separately participate in two distinct processes: assembling into NOX2 to promote ROS production and engaging with WRC to regulate the actin cytoskeleton."],"journal":["The Journal of biological chemistry"],"pubmed_title":["The NADPH oxidase 2 subunit p47<sup>phox</sup> binds to the WAVE regulatory complex and p22<sup>phox</sup> in a mutually exclusive manner."],"pmcid":["PMC10979099"],"funding_grant_id":["19IPLOI34660134","R35 GM128786"],"pubmed_authors":["Kuihon SVNP","Bayless KJ","Abbey CA","Chen B","Sevart BJ"],"additional_accession":[]},"is_claimable":false,"name":"The NADPH oxidase 2 subunit p47<sup>phox</sup> binds to the WAVE regulatory complex and p22<sup>phox</sup> in a mutually exclusive manner.","description":"The actin cytoskeleton and reactive oxygen species (ROS) both play crucial roles in various cellular processes. Previous research indicated a direct interaction between two key components of these systems: the WAVE1 subunit of the WAVE regulatory complex (WRC), which promotes actin polymerization and the p47<sup>phox</sup> subunit of the NADPH oxidase 2 complex (NOX2), which produces ROS. Here, using carefully characterized recombinant proteins, we find that activated p47<sup>phox</sup> uses its dual Src homology 3 domains to bind to multiple regions within the WAVE1 and Abi2 subunits of the WRC, without altering WRC's activity in promoting Arp2/3-mediated actin polymerization. Notably, contrary to previous findings, p47<sup>phox</sup> uses the same binding pocket to interact with both the WRC and the p22<sup>phox</sup> subunit of NOX2, albeit in a mutually exclusive manner. This observation suggests that when activated, p47<sup>phox</sup> may separately participate in two distinct processes: assembling into NOX2 to promote ROS production and engaging with WRC to regulate the actin cytoskeleton.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2025-04-26T11:27:42.358Z","creation":"2025-04-06T13:39:20.45Z"},"accession":"S-EPMC10979099","cross_references":{"pubmed":["38432630"],"doi":["10.1016/j.jbc.2024.107130"]}}