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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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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DOI: https://doi.org/10.1007/s000110050185