Palmitylation of cone opsins
| Autor: | Daniel R. Knapp, Rosalie K. Crouch, Zsolt Ablonczy, Masahiro Kono |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Rhodopsin
Opsin genetic structures G-protein-coupled receptor Molecular Sequence Data Palmitic Acid Urodela Retinal Cone Photoreceptor Cells Article Mice 03 medical and health sciences Optics Chlorocebus aethiops Animals Cone Opsin Base sequence 030304 developmental biology G protein-coupled receptor 0303 health sciences Base Sequence biology Mass spectrometry business.industry Chemistry Spectrum Analysis 030302 biochemistry & molecular biology Rod Opsins Lizards Sequence Analysis DNA Chromatography Ion Exchange Mass spectrometric Recombinant Proteins eye diseases Sensory Systems Ophthalmology COS Cells biology.protein Biophysics Cattle Palmitylation sense organs Spectrum analysis business Sequence Alignment Cone |
| Zdroj: | Vision Research. 46(27):4493-4501 |
| ISSN: | 0042-6989 |
| DOI: | 10.1016/j.visres.2006.08.003 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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