A POLYBASIC DOMAIN OR PALMITOYLATION IS REQUIRED IN ADDITION TO THE CAAX MOTIF TO LOCALIZE P21RAS TO THE PLASMA-MEMBRANE

被引：929

作者：

HANCOCK, JF ^{[1
]}

PATERSON, H ^{[1
]}

MARSHALL, CJ ^{[1
]}

机构：

[1] CHESTER BEATTY LABS,CELL & MOLEC BIOL SECT,LONDON SW3,ENGLAND

来源：

CELL | 1990年 / 63卷 / 01期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/0092-8674(90)90294-O

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：

The C-terminal CAAX motif of ras proteins undergoes a triplet of posttranslational modifications that are required for membrane association. The CAAX motif lies immediately C-terminal to the hypervariable domain, a region of 20 amino acids that distinguishes the ras proteins from each other. The hypervariable domains of p21H-ras, p21N-ras, and p21K-ras(A) contain sites for palmitoylation, which we now show must combine with the CAAX motif to target specific plasma membrane localization. Within the hypervariable domain of p21K-ras(B), which is not paimitoylated, we have identified a novel plasma membrane targeting signal consisting of a polybasic domain that also acts in combination with the CAAX motif. One function of the hypervariable domains of p21ras is therefore to provide different signals for plasma membrane localization. © 1990.

引用

页码：133 / 139

页数：7

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