Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1)

Asataro Yamamoto, Keiichiro Kami, Ryu Takeya, Hideki Sumimoto

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)

Abstract

NADPH oxidase organizer 1 (Noxo1), harboring a PX domain, two SH3 domains, and a proline-rich region (PRR), participates in activation of superoxide-producing Nox-family NADPH oxidases. Here, we show that Noxo1 supports superoxide production in a cell-free system for gp91phox/Nox2 activation by arachidonic acid. This lipid enhances an SH3-mediated binding of Noxo1 to p22phox, a protein complexed with Nox oxidases; the binding is known to be required for Nox activation. We also demonstrate that the bis-SH3 domain directly interacts with the Noxo1 PRR. The interaction appears to prevent the bis-SH3 domain and PRR from binding to their target proteins; disruption of the intramolecular interaction facilitates Noxo1 binding to p22phox and also allows the PRR to associate with the Nox activator Noxa1, which association is crucial for Nox activation as well. These findings suggest that Nox activation involves a conformational change leading to disruption of the bis-SH3-PRR interaction in Noxo1.

Original languageEnglish
Pages (from-to)560-565
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume352
Issue number2
DOIs
Publication statusPublished - Jan 12 2007

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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