Rac1 and cdc42 are members of the Rho-GTPase family. They play key roles in cytoskeletal reorganization, membrane trafficking, transcriptional regulation, cell growth and development. It has been established that GTP binding stimulates the activity of Rac1/cdc42. A putative Akt phosphorylation site at Ser71 of Rac1/cdc42 has been identified and confirmed by in vitro kinase assay (1). Phosphorylation at this site may inhibit GTP binding of Rac1, attenuating the signal transduction pathway downstream of Rac1 (1).
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