Biochemical and Biophysical Research Communications
Regular ArticleThe NADPH Oxidase Components p47phox and p40phox Bind to Moesin through Their PX Domain☆
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2018, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Interestingly, knockdown of moesin had no noticable effect on phagosomal ROS production. This was surprising since a previous study identified moesin as a binding partner of p47phox, a cytosolic component of NOX2 [31]. This interaction was shown to involve the PX domain of p47phox, which also mediates interaction with phosphoinositides.
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2014, Cellular SignallingCitation Excerpt :p40phox was the last NADPH oxidase subunit to be discovered, and although there is evidence of its both positive and negative effects on oxidase function, its exact role remains poorly defined. This protein was reported by Wientjes et al. [1] as a 40-kDa protein which co-purified in a 250 kDa complex with p67phox and p47phox, and whose primary association appeared to be with p67phox. Furthermore, the amount of this protein is reduced in patients with CGD (chronic granulomatous disease), who lack p67phox.
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Abbreviations used: CGD, chronic granulomatous disease; ERM, ezrin-radixin-moesin; PMA, phorbol myristate acetate; GST, glutathione S-transferase; PIPs, phosphatidylinositol phosphates; MALDI-TOF, matrix associated laser desorption ionisation–time of flight; His-tag, a tag consisting of 6 His residues.
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