The carboxyl-terminal domain is essential for rhodopsin transport in rod photoreceptors

被引：60

作者：

Concepcion, F

Mendez, A

Chen, J

机构：

[1] Univ So Calif, Doheny Eye Inst, Beckman Macular Res Ctr, Mary D Allen Lab Vis Res, Los Angeles, CA 90089 USA

[2] Univ So Calif, Dept Ophthalmol, Los Angeles, CA 90089 USA

[3] Univ So Calif, Keck Sch Med, Dept Cell & Neurobiol, Los Angeles, CA 90089 USA

来源：

VISION RESEARCH | 2002年 / 42卷 / 04期

关键词：

rhodopsin transport; photoreceptors; transgenic mice; retinal degeneration;

D O I：

10.1016/S0042-6989(01)00195-X

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

The role of the carboxyl-terminal domain in rhodopsin transport was investigated using transgenic mice expressing a rhodopsin truncation mutant lacking the terminal 15 amino acids (S334ter). It was previously shown that S334ter translocates to the outer segment in the presence of endogenous rhodopsin. We now show that in the absence of endogenous rhodopsin S334ter mis-localizes to the plasma membrane and fails to reconstitute outer segment structures. Surprisingly, this mis-localization does not affect photoreceptor cell survival. These results provide further evidence on the important role of the COOH-terminal domain in rhodopsin trafficking and demonstrate an absolute requirement of this domain for correct vectorial transport of rhodopsin in rod photoreceptors. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：417 / 426

页数：10

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