Rab protein (Rab)

Rab protein is the canonical name for a large family of small GTPases belonging to the Ras superfamily, with over 60 distinct members in humans. Rab proteins function as molecular switches, cycling between active (GTP-bound) and inactive (GDP-bound) forms, to regulate all major steps of intracellular vesicle trafficking—including vesicle budding, cargo selection, motility, docking, and fusion with target membranes. They achieve their specificity and localization through unique C-terminal hypervariable domains and interactions with Rab-specific effector proteins. Different Rab isoforms associate with particular organelles or vesicle populations, defining organelle identity and mediating transport between compartments such as the ER, Golgi, endosomes, and plasma membrane. Dysfunction or misregulation of Rab proteins has been implicated in a variety of diseases, including neurodegenerative conditions, cancer, and infectious processes, although they have proven difficult to target therapeutically due to their essential roles and high homology across the family[1][2][3][6].

Other names

Rab GTPaseRas-related in brain proteinRab family protein

Drugs targeting Rab or their regulators can modulate membrane trafficking processes (e.g., interfere with GTPase cycle, disrupt Rab-effector interactions, or modulate prenylation/localization)[1][3]. Targeting Rab-cycle regulators (like GEFs, GAPs, or prenyltransferases) may indirectly affect Rab function[1][2].