کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1929625 | 1050469 | 2012 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: S-glutathionylation regulates GTP-binding of Rac2 S-glutathionylation regulates GTP-binding of Rac2](/preview/png/1929625.png)
Phagocyte NADPH oxidase catalyzes the reduction of molecular oxygen to superoxide and is essential for defense against microbes. Rac2 is a low molecular weight GTP-binding protein that has been implicated in the regulation of phagocyte NADPH oxidase. Here we report that Cys157 of Rac2 is a target of S-glutathionylation and that this modification is reversed by dithiothreitol as well as enzymatically by thioltransferase in the presence of GSH. S-glutathionylated Rac2 enhanced the binding of GTP, presumably due to structural alterations. These results elucidate the redox regulation of cysteine in Rac2 and a possible mechanism for regulating NADPH oxidase activation.
► Cys157 of Rac2 is a target of S-glutathionylation.
► S-glutathionylated Rac2 enhanced the binding of GTP.
► S-glutathionylation induces structural alterations.
Journal: Biochemical and Biophysical Research Communications - Volume 425, Issue 4, 7 September 2012, Pages 892–896