Linked Life Data

16297854

Source:http://linkedlifedata.com/resource/pubmed/id/16297854

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pubmed-article:16297854pubmed:abstractTextActivation of the phagocyte NADPH oxidase requires the regulatory proteins p47(phox) and p67(phox), each harboring two SH3 domains. p67(phox) interacts with p47(phox) via simultaneous binding of the p67(phox) C-terminal SH3 domain to both the proline-rich region (PRR) of amino acid residues 360-369 and its C-terminally flanking region of p47(phox); the role of the interaction in oxidase regulation has not been fully understood. Here we show that the p47(phox)-p67(phox) interaction is disrupted not only by deletion of the PRR but also by substitution for basic residues in the extra-PRR (K383E/K385E). The substitution impaired oxidase activation partially in vitro and much more profoundly in vivo, indicating the significance of the p47(phox) extra-PRR. Replacement of Ser-379 in the extra-PRR, a residue known to undergo phosphorylation in stimulated cells, by aspartate attenuates the interaction and thus results in a defective superoxide production, suggesting that phosphorylation of Ser-379 is involved in oxidase regulation.lld:pubmed
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pubmed-article:16297854pubmed:authorpubmed-author:SumimotoHidek...lld:pubmed
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pubmed-article:16297854pubmed:pagination185-94lld:pubmed
pubmed-article:16297854pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:16297854pubmed:year2005lld:pubmed
pubmed-article:16297854pubmed:articleTitleA region C-terminal to the proline-rich core of p47phox regulates activation of the phagocyte NADPH oxidase by interacting with the C-terminal SH3 domain of p67phox.lld:pubmed
pubmed-article:16297854pubmed:affiliationMedical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.lld:pubmed
pubmed-article:16297854pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16297854pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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