ROCK2 interacts with p22phox to phosphorylate p47phox and to control NADPH oxidase activation in human monocytes - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2023

ROCK2 interacts with p22phox to phosphorylate p47phox and to control NADPH oxidase activation in human monocytes

Résumé

Significance Monocytes play a key role in innate immunity and inflammation by producing reactive oxygen species (ROS). The enzyme responsible for ROS production is the phagocyte NADPH oxidase, which is composed of two membrane proteins (p22phox and gp91phox/NOX2) and four cytosolic proteins (p47phox, p67phox, p40phox, and Rac1/2). Here, we show that p22phox associates with Rho-associated coiled-coil kinase 2 (ROCK2) in human monocytes. Interestingly, ROCK2 does not phosphorylate p22phox, p40phox, p67phox or gp91phox in vitro but highly phosphorylates p47phox. Furthermore, selective inhibition of ROCK2 activity and expression, inhibited both ROS production and p47phox phosphorylation in human monocytes. These data identify a key role of ROCK2 in the regulation of ROS production by monocytes. The ROCK2-p22phox interaction could be used to target monocyte ROS production.

Domaines

Immunité innée
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Dates et versions

hal-04255125 , version 1 (23-10-2023)

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Asma Tlili, Coralie Pintard, Margarita Hurtado-Nedelec, Dan Liu, Viviana Marzaioli, et al.. ROCK2 interacts with p22phox to phosphorylate p47phox and to control NADPH oxidase activation in human monocytes. Proceedings of the National Academy of Sciences of the United States of America, 2023, 120 (3), pp.e2209184120. ⟨10.1073/pnas.2209184120⟩. ⟨hal-04255125⟩

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