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New methods to directly visualize Rho GTPases reveal how a protein called RhoGDI regulates the activity of these 'molecular switches' at the plasma membrane.
Figure 1. The Rho GTPase cycle.Rho GTPases cycle between active (Rho-GTP; green) and inactive (Rho-GDP; orange) forms: the inactive form is activated (blue arrow) by proteins called GEFs (not shown), and the active form can go on to activate (grey arrow) various downstream effector proteins (grey). Other proteins called GDIs (purple) can bind inactive Rho GTPases and extract them from the membrane (black arrow). Now Golding et al. have shown that GDIs can also bind to active Rho GTPases and extract them from the membrane (purple arrow). Proteins called GAPs (not shown) help convert these active GDI-Rho-GTP complexes into inactive GDI-Rho-GDP complexes (red arrow): this can happen at the membrane or in the cytoplasm. Further research is needed to address a number of questions: can Rho-GTP escape from the GDI-Rho-GTP complex (green arrow)? And how can GEFs activate the Rho-GDP in GDI-Rho-GDP complexes (dashed black arrow)? GEF: guanine nucleotide exchange factor; GDI: Guanine nucleotide dissociation inhibitor; GDP: guanosine diphosphate; GTP: guanosine triphosphate; GAP: GTPase-activating proteins.
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