Rabphilin-3A (RPH3A)

Rabphilin-3A is a synaptic vesicle-associated effector protein with multiple functional domains. It was originally identified as a binding partner of the small GTPases Rab3A and Rab27A, which localize to secretory vesicles in neurons and neuroendocrine cells. Rabphilin-3A interacts with GTP-bound Rab proteins via its N-terminal Rab-binding domain and links vesicles to the actin cytoskeleton through α-actinin binding. Its C-terminal C2 domains bind calcium, phospholipids, and SNAP-25. Rabphilin-3A's main biological role is to regulate both exocytosis and endocytosis of vesicles, especially facilitating SNARE complex assembly for neurotransmitter release. It acts at distinct stages in the vesicular trafficking pathway, influencing vesicle docking, fusion, and membrane retrieval, but does not function as a receptor, enzyme, transporter, or transcription factor[1][2].

Other names

Rabphilin-3ARPH3AKIAA0985Exophilin-1RabphilinRabphilin 3A homolog

Not applicable; drugs do not directly target this molecule. Its mechanism involves regulation of vesicle docking and fusion through protein-protein interactions.