S-glutathionylation regulates GTP-binding of Rac2

descriptionPublicationkeyboard_double_arrow_right Article 01 Sep 2012 English Publisher:Elsevier BVJournal:Biochemical and Biophysical Research Communications, volume 425, pages 892-896 (issn: 0006-291X,

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Authors: In Sup, Kil; Seoung Woo, Shin; Jeen-Woo, Park;

doi: 10.1016/j.bbrc.2012.07.169

pmid: 22902632

S-glutathionylation regulates GTP-binding of Rac2

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Abstract

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.

Related Organizations

UPRRP College of Natural Sciences
Puerto Rico
Kyungpook National University
Korea (Republic of)

Keywords

Enzyme Activation, Dithiothreitol, RAC2 GTP-Binding Protein, Animals, Cysteine, Guanosine Triphosphate, Glutathione, NADP, Recombinant Proteins, rac GTP-Binding Proteins

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