GDI proteins RhoGTPase:GDP Inactivated RhoGTPase:GDP:GDI complex Dissociation of Rho GTP:GDP from GDI complex Authored: Van Aelst, L, 2007-04-28 21:26:24 Edited: Gopinathrao, G, 2007-04-02 21:35:36 GDIs sequester the inactive GTPases, preventing the dissociation of GDP and interactions with regulatory and effector molecules. They maintain Rho GTPases as soluble cytosolic proteins by forming high affinity complexes. In these complexes, the geranylgeranyl membrane targeting moiety present at the C terminus of the Rho GTPases is shielded from the solvent by its insertion into the hydrophobic pocket formed by the immunoglobulin like beta sandwich of the GDI (DerMardirossian and Bokoch, 2005).<p>Rho proteins, when released from the sequestering cytosolic GDIs, insert into the lipid bilayer of the plasma membrane with their isoprenylated C termini. The membrane bound GEFs activate these free RhoGTPases and thereby trigger the downstream signaling events via respective effector proteins on the membrane (Robbe et al., 2003). Detailed annotation of the activities of farnesyltransferase / geranylgeranyltransferases on prenylation of Rho GTPases thereby enabling their subsequent localization to plasma membrane will be available in future releases. Pubmed10655614 Pubmed10676816 Pubmed12471028 Pubmed15921909 Pubmed9194563 Reactome Database ID Release 43195146 Reactome, http://www.reactome.org ReactomeREACT_10051 Reviewed: Bernards, A, 2007-04-28 21:27:12