Rho GDI constitutes a family with three mammalian members: Rho-GDI alpha, the ubiquitously expressed archetypal member of the family; Ly/D4-GDI or Rho-GDI beta, which has hematopoietic tissue-specific expression, particularly in B- and T-lymphocytes; and Rho-GDI-3 or -gamma, which is membrane-anchored through an amphipathic helix and is preferentially expressed in the brain, pancreas, lung, kidney and testis (1). RhoGDI’s function by extracting Rho family GTPases including RhoA, Rac1, and Cdc42 from membranes and solubilizing them in the cytosol. Moreover, they interact only with prenylated Rho proteins both in vitro and in vivo. They also inhibit nucleotide exchange and GTP hydrolyzing activities on Rho proteins by interacting with their switch regions and probably restricting accessibility to GEFs and GAPs (2). The N-terminal domain of RhoGDI alpha binds to the switch region of the GTPases, affecting GDP-GTP cycling, whereas the C-terminal domain accommodates the isoprenyl moiety of the GTPases in its hydrophobic pocket, regulating cytosol/membrane partitioning (3). Rho-GDI alpha can be phosphorylated on two sites, serine 101 and serine 174, by PAK (P21-activated kinase) (4).
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