Post-Golgi trafficking of rhodopsin in retinal photoreceptors.
Rod outer segment renewal in retinal rod photoreceptors is mediated by polarised sorting of rhodopsin, and its associated proteins and lipids, on post-Golgi vesicles that bud from the trans-Golgi network and fuse with the specialised domain of the plasma membrane in the rod inner segment. This domain surrounds the cilium that connects the inner segment and the rod outer segment to which mature rhodopsin is delivered. The intracellular sorting machinery that regulates budding, targeting and fusion of rhodopsin carrier vesicles has been studied using multiple means including a newly developed cell-free assay that reconstitutes vesicle budding. These studies have revealed an essential role for small GTP-binding protein rab6, as well as the carboxyl-terminal domain of rhodopsin, in the formation of post-Golgi vesicles. In this report their role in post-Golgi trafficking of rhodopsin and the maintenance of photoreceptor cell polarity and health is discussed.
Department of Ophthalmology, University of Michigan, Ann Arbor 48105, USA. dereticd@umich.edu
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D000818:Animals; D002352:Carrier Proteins / Q000502:physiology; D002474:Cell-Free System / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism*; D017948:Retinal Rod Photoreceptor Cells / Q000378:metabolism*; D012243:Rhodopsin / Q000378:metabolism*; D020691:rab GTP-Binding Proteins; D018631:ras Proteins / Q000502:physiology
D002352:Carrier Proteins; C094135:Rab6 protein; D012243:Rhodopsin; D020691:rab GTP-Binding Proteins; D018631:ras Proteins