Mechanism for interaction between Nox2 and p22phox: two membrane integrated proteins of the phagocytic oxidase

2015 Fiscal Year Final Research Report

• Project/Area Number: 25460372
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: General medical chemistry
• Research Institution: Kyushu University
• Principal Investigator: Miyano Kei 九州大学, 医学(系)研究科(研究院), 助教 (60444783)
• Project Period (FY): 2013-04-01 – 2016-03-31
• Keywords: NADPHオキシダーゼ / 活性酸素 / Nox2 / 膜タンパク質 / レドックスシグナル

Outline of Final Research Achievements

The phagocyte NADPH oxidase, dormant in resting cells, is activated during phagocytosis to produce superoxide, a precursor of microbicidal oxidants. The catalytic core of the phagocyte oxidase is Nox2, a membrane-spaning protein that forms a stable heterodimer with p22phox. In this study, I found that both N- and C-terminal regions play a crucial role in Nox binding to p22phox. Furthermore, I showed that the C-terminal part of Nox1, Nox2 and Nox4 play a role in activation of activator proteins-dependent or -independent activation of Nox family. I also found that the posttranslational modification plays a crucial role for the protein maturation of Nox.

Free Research Field

医歯薬学