Roles for proline-rich regions of p47phox and p67phox in the phagocyte NADPH oxidase activation in vitro

Kenichiro Hata, Koichiro Takeshige, Hideki Sumimoto

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

The cytosolic proteins p47phox and p67phox, each containing two SH3 domains, are required for activation of the superoxide-producing phagocyte NADPH oxidase in a cell-free system with human neutrophil membrane and the small GTPase Rac. Here we focus on roles of proline-rich regions (PRRs) that reside in p47phox and p67phox. Deletion of the p47phox PRR, to which the C-terminal SH3 domain of p67phox binds, results in three-fold decreased activation of the enzyme in the cell-free system with the full-length p67phox, suggesting a modulatory role of the p47phox PRR. The modulation is likely mediated via the C-terminal region of p67phox, since the p47phox mutant protein fully activates the oxidase in combination with the N-terminus of p67phox. Neither deletion of the p67phox PRR nor substitutions for prolines in the region affects the ability to support superoxide production under the cell-free conditions, indicating that the PRR of p67phox has no primary function in the oxidase activation.

Original languageEnglish
Pages (from-to)226-231
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume241
Issue number2
DOIs
Publication statusPublished - Dec 18 1997
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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