Palmitylation of cone opsins

被引：14

作者：

Ablonczy, Zsolt

Kono, Masahiro

Knapp, Daniel R.

Crouch, Rosalie K.

机构：

[1] Med Univ S Carolina, Dept Ophthalmol, Charleston, SC 29425 USA

[2] Med Univ S Carolina, Dept Pharmacol & Expt Therapeut, Charleston, SC 29425 USA

来源：

VISION RESEARCH | 2006年 / 46卷 / 27期

关键词：

cone; opsin; palmitylation; mass spectrometry; G-protein-coupled receptor;

D O I：

10.1016/j.visres.2006.08.003

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

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. (c) 2006 Elsevier Ltd. All rights reserved.

引用

页码：4493 / 4501

页数：9

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[1] Mass spectrometric analysis of integral membrane proteins at the subpicomolar level: Application to rhodopsin [J].