Priming agents such as tumor necrosis factor-α (TNFα) and toll like receptor 7 (TLR7)/TLR8 agonists induced the activation of the peptidyl-prolyl cis/trans isomerase PIN1 in human neutrophils (Boussetta T et al. 2010; Makni-Maalej K et al. 2015). PIN1 is an enzyme that binds to phosphorylated Ser‐Pro or Thr‐Pro sequences, and subsequently catalyzes their conformational changes (Liou YC et al. 2011). In intact neutrophils, PIN1 was found to bind to the neutrophil cytosol factor 1 (NCF1 or p47phox) via the phosphorylated residue of Ser345 (Boussetta T et al. 2010). PIN1 then catalyzed a conformational change of NCF1 that facilitated subsequent phosphorylation of the protein on other sites by protein kinase C (PKC) (Boussetta T et al. 2010; El-Benna J et al. 2016). Extensive phosphorylation of the subunit NCF1 (p47phox) occurs during the activation of the NADPH oxidase (NOX2) in intact cells.
Bartegi, A, Malter, JS, El-Benna, J, Arabi Derkawi, R, Hayem, G, Boussetta, T, Raad, H, Zhou, XZ, Bournier, O, Gougerot-Pocidalo, MA, Dang, PM, Lu, PK, Ciappelloni, S, Kroviarski, Y
peptidyl-prolyl cis-trans isomerase activity of PIN1 [cytosol]
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