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J Cell Biol 2000 Dec 25;1517:1369-80. doi: 10.1083/jcb.151.7.1369.
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Identification of an outer segment targeting signal in the COOH terminus of rhodopsin using transgenic Xenopus laevis.

Tam BM , Moritz OL , Hurd LB , Papermaster DS .

Mislocalization of the photopigment rhodopsin may be involved in the pathology of certain inherited retinal degenerative diseases. Here, we have elucidated rhodopsin's targeting signal which is responsible for its polarized distribution to the rod outer segment (ROS). Various green fluorescent protein (GFP)/rhodopsin COOH-terminal fusion proteins were expressed specifically in the major red rod photoreceptors of transgenic Xenopus laevis under the control of the Xenopus opsin promoter. The fusion proteins were targeted to membranes via lipid modifications (palmitoylation and myristoylation) as opposed to membrane spanning domains. Membrane association was found to be necessary but not sufficient for efficient ROS localization. A GFP fusion protein containing only the cytoplasmic COOH-terminal 44 amino acids of Xenopus rhodopsin localized exclusively to ROS membranes. Chimeras between rhodopsin and alpha adrenergic receptor COOH-terminal sequences further refined rhodopsin's ROS localization signal to its distal eight amino acids. Mutations/deletions of this region resulted in partial delocalization of the fusion proteins to rod inner segment (RIS) membranes. The targeting and transport of endogenous wild-type rhodopsin was unaffected by the presence of mislocalized GFP fusion proteins.

PubMed ID: 11134067
PMC ID: PMC2150681
Article link: J Cell Biol
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: brdt rasl12 rho rnd1

Article Images: [+] show captions
References [+] :
Alfalah, O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts. 1999, Pubmed