S-glutathionylation regulates GTP-binding of Rac2.
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 Cys(157) 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.
School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University, Taegu 702701, Republic of Korea.
In Sup
IS
Kil
Seoung Woo
SW
Shin
Jeen-Woo
JW
Park
D000818:Animals; D003545:Cysteine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004229:Dithiothreitol / Q000737:chemistry; D004789:Enzyme Activation; D005978:Glutathione / Q000737:chemistry / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D009249:NADP / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D020744:rac GTP-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000097766:RAC2 GTP-Binding Protein
D003545:Cysteine; D004229:Dithiothreitol; D005978:Glutathione; D006160:Guanosine Triphosphate; D009249:NADP; D011994:Recombinant Proteins; D020744:rac GTP-Binding Proteins; D000097766:RAC2 GTP-Binding Protein