SH3 domain-mediated interactions involving the phox components of the NADPH oxidase (original) (raw)

Abstract.

Objective and Design: To derive a model describing the SH3 domain-mediated assembly of the activated NADPH oxidase.¶Materials: Recombinant SH3 domain and Pro-rich fusion proteins were used to investigate potential co-associations.¶Methods: Interactions were assessed using biotinylated overlay assays and the yeast two hybrid system. Association with p47phox from cell lysates was examined by immunoblot analysis.¶Results: The association between p47- and p22phox involves the SH3 domains of p47phox functioning in tandem. The Pro-rich motif in p47phox interacts with both p40phox and the COOH-terminal SH3 domain of p67phox.¶Conclusions: In the resting cell, the Pro-rich motif of p47phox interacts with the SH3 domain of p40phox, which in turn associates with p67phox. Upon activation, the p47-p40phox regulatory complex dissociates, permitting the association of p47phox with the COOH-terminal SH3 domain of p67phox. This complex translocates to the plasma membrane and associates with cytochrome b558, via interaction of the tandem SH3 domains of p47phox with the p22phox Pro-rich motif.

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Authors and Affiliations

  1. Yamanouchi Research Institute, Littlemore Park, Oxford OX4 4SX, UK, Fax +44 1865 748974, GB
    L. Wilson, C. Butcher & S. Kellie
  2. Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, Lincoln's Inn Fields, P.O. Box 123, London WC2A 3PX, UK, GB
    P. Finan

Authors

  1. L. Wilson
  2. C. Butcher
  3. P. Finan
  4. S. Kellie

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Received 20 January 1997; returned for revision 27 March 1997; accepted by M. Seed 23 April 1997

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Wilson, L., Butcher, C., Finan, P. et al. SH3 domain-mediated interactions involving the phox components of the NADPH oxidase.Inflamm. res. 46, 265–271 (1997). https://doi.org/10.1007/s000110050185

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