Rab9 effector protein with kelch motifs (RABEPK)

Rab9 effector protein with kelch motifs (RABEPK) is a monomeric cytosolic and membrane-associated protein characterized by six kelch repeats which form a β-propeller structure that mediates protein-protein interactions[1][3]. RABEPK binds to the active, GTP-bound form of Rab9 GTPase with high specificity and facilitates the transport and docking of vesicles carrying mannose 6-phosphate receptors from endosomes to the trans-Golgi network, a process essential for proper lysosomal enzyme trafficking and cellular logistics[1][2][4][5][6][8]. This protein does not interact with closely related Rabs such as Rab7, and appears to inhibit the GTPase activity of Rab9[1]. While crucial for intracellular membrane trafficking, RABEPK is not currently considered a direct pharmacological target, nor does it have established roles as a biomarker or safety concern in clinical settings[5][8].

Other names

Rab9 effector protein with kelch motifsRABEPKRab9 effector p40p4040 kDa Rab9 effector proteinRAB9P40bA65N13.1