Palmitylation of cone opsins

descriptionPublicationkeyboard_double_arrow_right Article 01 Dec 2006 English Publisher:Elsevier BVJournal:Vision Research, volume 46, pages 4,493-4,501 (issn: 0042-6989,

Copyright policy )Funded by:NIH | STRUCTURE AND FUNCTION OF..., NIH | MUSC FACIL EXPANSION &REN..., NIH | Core Resources for Vision...

Authors: Ablonczy, Zsolt; Kono, Masahiro; Knapp, Daniel R.; Crouch, Rosalie K.;

doi: 10.1016/j.visres.2006.08.003

pmid: 16989884

pmc: PMC2025682

Palmitylation of cone opsins

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Abstract

Palmitylation is a widespread modification in G-protein-coupled receptors and often a dynamic process. In rhodopsins, palmitylation is static on C322/C323. Red/green (M/LWS) cone opsins have no cysteines at corresponding positions and no palmitylation. Blue (SWS2) cone opsins have a single corresponding cysteine and mass spectrometric analysis showed partial palmitylation of salamander SWS2 cone opsin. Ultraviolet (SWS1) cone opsins have one corresponding cysteine, but only unpalmitylated opsin was observed for mouse and salamander. The results show that the static palmitylation found on rhodopsin is not found on cone opsins and suggest the possibility of an unidentified role for opsin palmitylation in cones.

Related Organizations

MEDICAL UNIVERSITY OF SOUTH CAROLINA
Medical University of South Carolina
United States

Keywords

Rhodopsin, Caudata, G-protein-coupled receptor, Molecular Sequence Data, Palmitic Acid, Mice, Chlorocebus aethiops, Animals, Mass spectrometry, Base Sequence, Spectrum Analysis, Rod Opsins, Lizards, Sequence Analysis, DNA, Chromatography, Ion Exchange, Sensory Systems, Recombinant Proteins, Ophthalmology, Opsin, COS Cells, Retinal Cone Photoreceptor Cells, Palmitylation, Cattle, Sequence Alignment, Cone

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