| Literature DB >> 16989884 |
Zsolt Ablonczy1, Masahiro Kono, Daniel R Knapp, Rosalie K Crouch.
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.Entities:
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Year: 2006 PMID： 16989884 PMCID： PMC2025682 DOI： 10.1016/j.visres.2006.08.003
Source DB: PubMed Journal: Vision Res ISSN： 0042-6989 Impact factor: 1.886