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The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain

F B Wientjes1, E P Reeves, V Soskic

  • 1Centre for Molecular Medicine, University College London, 5 University Street, London WC1E 6JJ, United Kingdom. rmhafrw@ucl.ac.uk

Biochemical and Biophysical Research Communications
|November 22, 2001
PubMed

Insights

Moesin, an F-actin-binding protein, interacts with phagocyte NADPH oxidase components p47phox and p40phox. This interaction is phosphoinositide-dependent and involves moesin’s N-terminal region binding to the PX domain of p47phox and p40phox.

Area of Science:

  • Cell biology
  • Molecular biology
  • Immunology

Background:

  • The NADPH oxidase enzyme complex in phagocytes is crucial for generating reactive oxygen species.
  • Cytosolic proteins, including p47phox, p67phox, p40phox, and rac, regulate NADPH oxidase activity.
  • Previous studies indicated interactions between cytosolic phox proteins and the cytoskeleton, such as coronin.

Purpose of the Study:

  • To investigate the interaction between the cytoskeletal protein moesin and the phox proteins involved in NADPH oxidase.
  • To elucidate the binding mechanism and domains involved in the moesin-phox protein interaction.

Main Methods:

  • Co-immunoprecipitation assays to detect protein-protein interactions.
  • Analysis of protein binding in a phosphoinositide-dependent manner.
  • Mapping of binding sites using protein domains, specifically the PX domain.

Main Results:

  • Moesin interacts with p47phox and p40phox, two key cytosolic components of the NADPH oxidase complex.
  • The binding of moesin to p47phox and p40phox is dependent on phosphoinositides.
  • The N-terminal region of moesin directly binds to the PX (phox homology) domain of p47phox and p40phox.

Conclusions:

  • Moesin is a novel cytoskeletal interactor of the NADPH oxidase phox proteins.
  • The interaction is mediated by phosphoinositide binding and specific domain interactions (moesin N-terminus with PX domains).
  • This finding adds to the understanding of NADPH oxidase regulation and its association with the cytoskeleton.

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