Computational Model Explains High Activity and Rapid Cycling of Rho GTPases within Protein Complexes
Figure 1
Reaction Scheme of the Small GTPase Cycle
The three forms of the GTPase (RD, RT, and nucleotide-free R) (middle layer) form complexes with a GEF (E) (bottom layer) and a GAP (A) (top layer). Solid arrows indicate the main reaction fluxes. All reactions except GTP hydrolyses (2 → 1, 6 → 8, 5 → 3) are reversible. Numbering of the species is consistent with the reaction rate constants listed in Table 3. Free GTP (T), GDP (D), GEF, and GAP are not shown for simplicity.