Rab GDI (GDP dissociation inhibitor) Inibidores

GDP Dissociation Inhibitors (GDI1 and GDI2) are crucial regulators of the Rab family of small GTPases, which play key roles in vesicular transport and membrane trafficking. GDIs function by binding to Rab proteins in their inactive GDP-bound form, the dissociation of GDP and thus maintaining the GTPases in an inactive state. This interaction also helps in the sequestration of Rab proteins in the cytosol, their association with membranes where they would otherwise exert their action. GDIs are essential for the recycling of Rab proteins, facilitating their transport back to donor membranes for another round of vesicle formation and trafficking. The GDI-mediated regulation of Rab GTPases is vital for cellular homeostasis, influencing processes like endocytosis, exocytosis, and the maintenance of organelle identity.

Targeting GDP Dissociation Inhibitors (GDI1 and GDI2) for disruption or inhibition represents a strategy to modulate the activity of Rab GTPases, key regulators of intracellular vesicle trafficking. Inhibiting GDIs could potentially enhance the membrane association and activation of Rab proteins, thereby influencing vesicular transport processes.