| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1929625 | Biochemical and Biophysical Research Communications | 2012 | 5 Pages |
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.
