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Details on Person In resting cells, the NADPH oxidase components, NCF1 (p47pho...

Class:Id	Summation:9626757
_displayName	In resting cells, the NADPH oxidase components, NCF1 (p47pho...
_timestamp	2018-11-06 21:33:45
created	[InstanceEdit:9626781] Shamovsky, Veronica, 2018-10-29
literatureReference	[LiteratureReference:9626812] Architecture of the p40-p47-p67phox complex in the resting state of the NADPH oxidase. A central role for p67phox [LiteratureReference:9626779] Isolation of a complex of respiratory burst oxidase components from resting neutrophil cytosol [LiteratureReference:9626790] Activation and assembly of the NADPH oxidase: a structural perspective [LiteratureReference:9626811] Molecular basis of phosphorylation-induced activation of the NADPH oxidase [LiteratureReference:9626856] Phagocyte NADPH oxidase: a multicomponent enzyme essential for host defenses [LiteratureReference:9626766] Priming of the neutrophil respiratory burst: role in host defense and inflammation [LiteratureReference:9626794] Neutrophils exposed to bacterial lipopolysaccharide upregulate NADPH oxidase assembly [LiteratureReference:9626801] Priming of human neutrophil respiratory burst by granulocyte/macrophage colony-stimulating factor (GM-CSF) involves partial phosphorylation of p47(phox) [LiteratureReference:9626864] TLR8, but not TLR7, induces the priming of the NADPH oxidase activation in human neutrophils [LiteratureReference:9626795] TNF-alpha induces phosphorylation of p47(phox) in human neutrophils: partial phosphorylation of p47phox is a common event of priming of human neutrophils by TNF-alpha and granulocyte-macrophage colony-stimulating factor [LiteratureReference:9626828] A specific p47phox -serine phosphorylated by convergent MAPKs mediates neutrophil NADPH oxidase priming at inflammatory sites [LiteratureReference:9626853] A molecular mechanism for autoinhibition of the tandem SH3 domains of p47phox, the regulatory subunit of the phagocyte NADPH oxidase
modified	[InstanceEdit:9628185] Shamovsky, Veronica, 2018-11-06
text	In resting cells, the NADPH oxidase components, NCF1 (p47phox), NCF2 (p67phox), and NCF4 (p40phox) are located in the cytosol where they associate in a trimer complex with a 1:1:1 stoichiometry through specific domains (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). However, NCF1 may also exist separately from the trimer (El-Benna J et al. 2016). In the resting state, two SH3 domains of NCF1 (p47phox) bind the auto‐inhibitory region (AIR; amino acids 292‐340) to keep NCF1 in a closed auto‐inhibited state, preventing its binding to p22phox and therefore NOX2 activation (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).
(summation)	[Reaction:9626832] MAPK1 or MAPK3 phosphorylates NCF1 at Ser345 [Homo sapiens]
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