A role for rhodopsin in a signal transduction cascade that regulates membrane trafficking and photoreceptor polarity.

This review summarizes the most recent progress in the understanding of the role of rhodopsin C-terminal domain in the regulation of intracellular trafficking and photoreceptor morphogenesis. A proposed cascade of molecular interactions, initiated by the rhodopsin C-terminal sequence VXPX-COOH during trafficking from the Golgi/TGN in retinal photoreceptors, is relayed by the small GTPase ARF4 to the downstream effectors. One of the candidates for an ARF4 effector is the ARF-GAP ASAP1, which may function as a subunit of, or form a novel protein coat involved in trafficking from the TGN and in cytoskeletal remodeling, whose assembly is regulated by the binding of ARF4 to rhodopsin, and whose function is essential for the polarized trafficking toward the ROS.