p47 phox Molecular Activation for Assembly of the Neutrophil NADPH Oxidase Complex - Groupe Membrane et pathogènes / Membrane and Pathogens Group (IBS-MP) Accéder directement au contenu
Article Dans Une Revue Journal of Biological Chemistry Année : 2010

p47 phox Molecular Activation for Assembly of the Neutrophil NADPH Oxidase Complex

Résumé

The p47phox cytosolic factor from neutrophilic NADPH oxidase has always been resistant to crystallogenesis trials due to its modular organization leading to relative flexibility. Hydrogen/deuterium exchange coupled to mass spectrometry was used to obtain structural information on the conformational mechanism that underlies p47phox activation. We confirmed a relative opening of the protein with exposure of the SH3 Src loops that are known to bind p22phox upon activation. A new surface was shown to be unmasked after activation, representing a potential autoinhibitory surface that may block the interaction of the PX domain with the membrane in the resting state. Within this surface, we identified 2 residues involved in the interaction with the PX domain. The double mutant R162A/D166A showed a higher affinity for specific phospholipids but none for the C-terminal part of p22phox, reflecting an intermediate conformation between the autoinhibited and activated forms.
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Dates et versions

hal-02335575 , version 1 (19-03-2021)

Identifiants

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Julien Marcoux, Petr Man, Isabelle Petit-Härtlein, Corinne Vivès, Eric Forest, et al.. p47 phox Molecular Activation for Assembly of the Neutrophil NADPH Oxidase Complex. Journal of Biological Chemistry, 2010, 285 (37), pp.28980-28990. ⟨10.1074/jbc.M110.139824⟩. ⟨hal-02335575⟩
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