在静息细胞中，NADPH氧化酶成分NCF1 (p47phox)、NCF2 (p67phox)和NCF4 (p40phox)位于胞质中，它们通过特定结构域以1:1:1的化学计量比结合在三聚体复合物中(Groemping Y & Rittinger K 2005;El-Benna J et al. 2005;Park JW et al. 1994;Lapouge K et al. 2002;El-Benna J et al. 2016)。然而，NCF1也可能与三聚体分开存在(El-Benna J et al. 2016)。在静息状态下，NCF1的两个SH3结构域(p47phox)结合自抑制区(AIR;氨基酸292‐340)保持NCF1处于封闭的自抑制状态，防止其与p22phox结合，从而阻止NOX2的激活(Groemping Y et al. 2003;Yuzawa S et al. 2004;El-Benna J et al. 2016)。 Priming of neutrophils by several agents such as GM‐CSF, TNFα, PAF, LPS and CL097, a TLR7/8 agonist, induces partial phosphorylation of NCF1 (Makni-Maalej K et al. 2015; Dang PM et al. 1999; Dewas C et al. 2003; DeLeo FR et al. 1998). Mass spectrometry analysis of NCF1 identified Ser345 as the phosphorylated site in neutrophils primed by TNFα and GM‐CSF, and site‐directed mutagenesis of Ser345 and use of a competitive inhibitory peptide containing the Ser345 sequence have demonstrated that this step is critical for the priming of ROS production in human neutrophils (Dang PMC et al. 2006). Further, inhibitors of the MAPK1 and MAPK3 (ERK1/2) pathway abrogated GM-CSF-induced phosphorylation of Ser345 (Dang PMC et al. 2006).