A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic

被引：189

作者：

Short, B

Preisinger, C

Körner, R

Kopajtich, R

Byron, O

Barr, FA

机构：

[1] Max Planck Inst Biochem, Dept Cell Biol, D-85152 Martinsried, Germany

[2] Max Planck Inst Biochem, Dept Cell Biol, D-82152 Martinsried, Germany

[3] Univ Glasgow, Fac Biomed & Life Sci, Div Infect & Immun, Glasgow, Lanark, Scotland

来源：

JOURNAL OF CELL BIOLOGY | 2001年 / 155卷 / 06期

基金：

英国惠康基金;

关键词：

Golgi apparatus; protein transport; rab GTPases; rab2; Golgi stacks;

D O I：

10.1083/jcb.200108079

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Membrane traffic between the encloplasmic reticulum (ER) and Golgi apparatus and through the Golgi apparatus is a highly regulated process controlled by members of the rab GTPase family. The GTP form of rab1 regulates ER to Golgi transport by interaction with the vesicle tethering factor p115 and the cis-Golgi matrix protein GM130, also part of a complex with GRASP65 important for the organization of cis-Golgi cisternae. Here, we find that a novel coiled-coil protein golgin-45 interacts with the medial-Golgi matrix protein GRASP55 and the GTP form of rab2 but not other Golgi rab proteins. Depletion of golgin-45 disrupts the Golgi apparatus and causes a block in secretory protein transport. These results demonstrate that GRASP55 and golgin-45 form a rab2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure.

引用

页码：877 / 883

页数：7