Mechanism for interaction between Nox2/gp91^<phox>and p22^<phox>: two membrane proteins of the phagocyte NADPH oxidase

在静止细胞中处于休眠状态的吞噬细胞NADPH氧化酶在吞噬过程中被激活，产生超氧化物，这是杀微生物氧化剂的前体。吞噬细胞氧化酶的催化核心是Nox2/gp91^<phox>，这是一种跨膜蛋白，与p22^<phox>形成稳定的异源二聚体。在这项研究中，我发现n端和c端区域在Nox与p22^<phox>的结合中起着至关重要的作用。此外，我发现在Nox2中加入特定区域的非吞噬性Nox （Nox5）会导致Nox2蛋白的大量表达。

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/gp91^<phox>, a membrane-spaning protein that forms a stable heterodimer with p22^<phox>. In this study, I found thatboth N-and C-terminal regions play a crucial role in Nox binding to p22^<phox>.Furthermore, I found that the addition of a specific region of nonphagocytic Nox (Nox5) to Nox2 leads to a large amount of Nox2 protein expression.