INVIVO FARNESYLATION OF RAT RHODOPSIN KINASE

被引：32

作者：

ANANT, JS

FUNG, BKK

机构：

[1] Jules Stein Eye Institute University of California, Los Angeles

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 183卷 / 02期

关键词：

D O I：

10.1016/0006-291X(92)90505-F

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have shown by intravitreal injection of [3H]mevalonolactone that a 65 kDa protein in rat photoreceptors is posttranslationally modified by farnesylation. We further identified this 65 kDa prenylated protein as rhodopsin kinase based on its affinity for photolyzed rhodopsin and its ability to autophosphorylate in the presence of [γ-32P]ATP. The farnesylation of rhodopsin kinase may be important for correctly targeting this enzyme to the photoreceptor outer segments, allowing it to phosphorylate photolyzed rhodopsin efficiently. © 1992.

引用

页码：468 / 473

页数：6

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