Raft trafficking of AB5 subunit bacterial toxins

被引：90

作者：

Lencer, WI

Saslowsky, D

机构：

[1] Childrens Hosp, Boston, MA 02115 USA

[2] Harvard Digest Dis Ctr, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Dept Pediat, Boston, MA 02115 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2005年 / 1746卷 / 03期

关键词：

AB(5) toxin; GM1; lipid raft; retrograde transport; ceramide; ganglioside; sphingomyclin; cholesterol; cholera toxin; Shiga toxin;

D O I：

10.1016/j.bbamcr.2005.07.007

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：

Cholera and the related AB(5)-subunit toxins co-opt plasma membrane (PM) glycolipids to move retrograde into the endoplasmic reticulum (ER) of the host cell where a portion of the toxin is retro-translocated to the cylosol to induce disease. Only glycolipids that associate strongly with detergent insoluble membrane microdomains can sort the toxins backwards from PM to ER. The way certain lipids and proteins are clustered in the plane of the membrane to form lipid rafts likely explains how the glycolipids can function as sorting motifs for the toxins. (c) 2005 Elsevier B.V. All rights reserved.

引用

页码：314 / 321

页数：8

共 72 条

[71] Uncoupling of the cholera toxin-GM1 ganglioside receptor complex from endocytosis, retrograde Golgi trafficking, and downstream signal transduction by depletion of membrane cholesterol [J].