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GTPases regulate a wide range of cellular processes, such as intracellularvesicular transport, signal transduction, and protein translation. Thesehydrolase enzymes operate as biochemical switches by toggling between an activeguanosine triphosphate (GTP)-bound state and an inactive guanosine diphosphate(GDP)-bound state. We compare two network motifs, a single-species switch andan interlinked cascade that consists of two species coupled through positiveand negative feedback loops. We find that interlinked cascades are closer tothe ideal all-or-none switch and are more robust against fluctuating signals.While the single-species switch can only achieve bistability, interlinkedcascades can be converted into oscillators by tuning the cofactorconcentrations, which catalyse the activity of the cascade. These regimes canonly be achieved with sufficient chemical driving provided by GTP hydrolysis.In this study, we present a thermodynamically consistent model that can achievebistability and oscillations with the same feedback motif.

Interlinked GTPase cascades provide a motif for both robust switches and oscillators