Rac-dependent feedforward autoactivation of NOX2 leads to oxidative burst

• Published in: The Journal of biological chemistry Vol. 297; no. 2; p. 100982
• Main Authors: Hoang, Hanh My, Johnson, Hope Elizabeth, Heo, Jongyun
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.08.2021; American Society for Biochemistry and Molecular Biology
• Subjects: allostery; autoactivation; Cell Line; Cell Line, Tumor; Enzyme Activation; Humans; NADPH Oxidase 2 - immunology; NADPH Oxidase 2 - metabolism; NOX1; NOX2; Oxidation-Reduction; Rac; rac GTP-Binding Proteins - metabolism; Reactive Oxygen Species - metabolism; redox; Signal Transduction; superoxide; Superoxides - metabolism; dHL60; ClC-3; PMA; GEF; SOD; H2O2; redox; SITS; DIDS; Rac; GAP; autoactivation; superoxide; MAP; NOX1; allostery; NOX2

NADPH oxidase 2 (NOX2) produces the superoxide anion radical (O2−), which has functions in both cell signaling and immune defense. NOX2 is a multimeric-protein complex consisting of several protein subunits including the GTPase Rac. NOX2 uniquely facilitates an oxidative burst, which is described by...