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首页> 外文期刊>Molecular and Cellular Biology >Activation State-Dependent Interaction between Gαi and p67phox
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Activation State-Dependent Interaction between Gαi and p67phox

机译：Gαi和p67phox之间的激活状态相关相互作用

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The phagocyte NADPH oxidase consists of multiple protein subunits that interact with each other to form a functional superoxide-generating complex. Although the essential components for superoxide production have been well characterized, other proteins potentially involved in the regulation of NADPH oxidase activation remain to be identified. We report here that the Gαi subunit of heterotrimeric G proteins is a novel binding partner for p67phox in transfected HEK293T cells and peripheral blood polymorphonuclear leukocytes. p67phox preferably interacted with inactive Gαi. Expression of p67phox caused a dose-dependent decrease in intracellular cyclic AMP concentration, suggesting altered function of Gαi. We identified a fragment of p67phox, consisting of the PB1 domain and the C-terminal SH3 domain, to be critical for the interaction with Gαi. Because these domains are involved in the interaction with p47phox and p40phox, the relationship between the respective binding events was investigated. Wild-type Gαi, but not its QL mutant, could promote the interaction between p67phox and p47phox. However, the interaction between p67phox and p40phox was not affected by either Gαi form. These results provide the first evidence for an interaction between p67phox and an alpha subunit of heterotrimeric G proteins, suggesting a potential role for Gαi in the regulation or activation of NADPH oxidase.
机译：吞噬细胞NADPH氧化酶由彼此相互作用形成功能性超氧化物生成复合物的多个蛋白质亚基组成。尽管已经很好地表征了产生超氧化物的基本成分，但仍需要鉴定可能参与调节NADPH氧化酶活化的其他蛋白质。我们在这里报道，异源三聚体G蛋白的Gαi亚基是p67 phox 在转染的HEK293T细胞和外周血多形核白细胞中的新型结合伴侣。 p67 phox 优选与非活性Gαi相互作用。 p67 phox 的表达引起细胞内环AMP浓度的剂量依赖性降低，提示Gαi功能改变。我们确定了一个p67 phox 片段，该片段由PB1域和C末端SH3域组成，对于与Gαi的相互作用至关重要。由于这些域参与了与p47 phox 和p40 phox 的相互作用，因此研究了各个结合事件之间的关系。野生型Gαi，但不是其QL突变体，可以促进p67 phox 和p47 phox 之间的相互作用。但是，p67 phox 和p40 phox 之间的相互作用均不受Gαi形式的影响。这些结果为p67 phox 与异源三聚体G蛋白的α亚基之间的相互作用提供了第一个证据，表明Gαi在调节或激活NADPH氧化酶中的潜在作用。

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