Title : Redox regulation of Rac1 by thiol oxidation.

Pub. Date : 2015 Feb

PMID : 25289457






6 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Our results suggest that Rac1 oxidation at Cys(18) is a novel posttranslational modification that upregulates Rac1 activity. Cysteine Rac family small GTPase 1 Homo sapiens
2 Herein, we show that Rac1 contains a redox-sensitive cysteine (Cys(18)) that can be selectively oxidized at physiological pH because of its lowered pKa. Cysteine Rac family small GTPase 1 Homo sapiens
3 Herein, we show that Rac1 contains a redox-sensitive cysteine (Cys(18)) that can be selectively oxidized at physiological pH because of its lowered pKa. Cysteine Rac family small GTPase 1 Homo sapiens
4 Oxidation of Cys(18) by glutathione greatly perturbs Rac1 guanine nucleotide binding and promotes nucleotide exchange. Cysteine Rac family small GTPase 1 Homo sapiens
5 As aspartate substitutions have been previously used to mimic cysteine oxidation, we characterized the biochemical properties of Rac1(C18D). Cysteine Rac family small GTPase 1 Homo sapiens
6 Our results suggest that Rac1 oxidation at Cys(18) is a novel posttranslational modification that upregulates Rac1 activity. Cysteine Rac family small GTPase 1 Homo sapiens