Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
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DOI：
10.1016/s0092-8674(00)80191-9
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发表时间：
1997-04-04
期刊：
影响因子：
64.5
通讯作者：
Scheller, RH
中科院分区：
文献类型：
--
作者：
Hay, JC;Chao, DS;Scheller, RH
所提出的顺式高尔基体囊泡受体突触蛋白 5 被发现与 28 kDa 的高尔基体相关 SNARE (GOS-28)、rbet1、rsly1 和本文表征的两种新蛋白形成复合物：大鼠 sec22b 和 membrin，这两种蛋白都是细胞质定向的整合膜蛋白。该复合物似乎重现了源自不同区室的蛋白质的囊泡对接相互作用，因为突触蛋白 5、rbet1 和 GOS-28 定位于高尔基体膜，而小鼠 sec22b 和膜蛋白在内质网中积累。 N-乙基马来酰亚胺敏感因子可显着重新排列复合物中的蛋白质相互作用。该复合体由两个或多个子复合体组成，其中一些成员（大鼠 sec22b 和 Syntaxin 5）是共同的，而其他成员（rbet1 和 GOS-28）则相互排斥相关。我们认为这些蛋白质相互作用决定了内质网和高尔基体之间的囊泡对接/融合保真度。
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.