Abstract
Rac1 is a member of the family of small Rho GTPases that are molecular switches governing a variety of fundamental cellular processes, such as cell growth and motility. Its subcellular location and activity are regulated by several posttranslational modifications. S-glutathionylation, the adduction of glutathione to cysteine residues in Rac1, is a redox-dependent thiol modification and is generally associated with oxidative/nitrosative stress, representing a novel mechanism of GTPase regulation. Here, we describe the use of biotin-labeled glutathione to monitor intracellular glutathionylated Rac1 in response to exogenous stimuli.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
