Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells

被引：179

作者：

Hay, JC

Chao, DS

Kuo, CS

Scheller, RH

机构：

[1] Howard Hughes Medical Institute, Dept. of Molec. and Cell. Physiology, Stanford Univ. School of Medicine, Stanford

来源：

CELL | 1997年 / 89卷 / 01期

关键词：

D O I：

10.1016/S0092-8674(00)80191-9

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 proposed cis-Golgi vesicle receptor syntaxin 5 was found in a complex with Golgi-associated SNARE of 28 kDa (GOS-28), rbet1, rsly1, and two novel proteins characterized herein: rat sec22b and membrin, both cytoplasmically oriented integral membrane proteins. The complex appears to recapitulate vesicle docking interactions of proteins originating from distinct compartments, since syntaxin 5, rbet1, and GOS-28 localize to Golgi membranes, whereas mouse sec22b and membrin accumulate in the endoplasmic reticulum. Protein interactions in the complex are dramatically rearranged by N-ethylmaleimide-sensitive factor. The complex consists of two or more subcomplexes with some members (rat sec22b and syntaxin 5) in common and others (rbet1 and GOS-28) mutually exclusively associated. We propose that these protein interactions determine vesicle docking/fusion fidelity between the endoplasmic reticulum and Golgi.

引用

页码：149 / 158

页数：10

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