VESICULAR STOMATITIS-VIRUS GLYCOPROTEIN IS SORTED AND CONCENTRATED DURING EXPORT FROM THE ENDOPLASMIC-RETICULUM
VESICULAR STOMATITIS-VIRUS GLYCOPROTEIN IS SORTED AND CONCENTRATED DURING EXPORT FROM THE ENDOPLASMIC-RETICULUM
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DOI：
10.1016/0092-8674(94)90359-x
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发表时间：
1994-03-11
期刊：
影响因子：
64.5
通讯作者：
FARQUHAR, MG
中科院分区：
文献类型：
--
作者：
BALCH, WE;MCCAFFERY, JM;FARQUHAR, MG
新合成的蛋白质被认为是通过大量流动从内质网（ER）移动到高尔基体，并且分选被认为只发生在高尔基体网络（TGN）中。使用定量免疫电子显微镜，我们表明，水泡性口炎病毒糖蛋白（VSV-G）从居民ER蛋白和浓缩5- 10倍，在40-80 nm的囊泡出芽从ER囊泡。VSV-G在前高尔基体囊泡载体中的积累是其运输到TGN的唯一可检测的浓度步骤。从这些结果中，很明显，从ER的输出并不完全由整体流动介导。雌激素受体发挥一种意想不到的控制水平，以确保成熟蛋白质选择性和有效地进入分泌途径。
Newly synthesized proteins are believed to move from the endoplasmic reticulum (ER) to the Golgi by bulk flow, and sorting is assumed to occur exclusively in the trans-Golgi network (TGN). Using quantitative immunoelectron microscopy, we demonstrate that vesicular stomatitis virus glycoprotein (VSV-G) is sorted from resident ER proteins and concentrated 5- to 10-fold in 40-80 nm vesicles during vesicle budding from the ER. Accumulation of VSV-G in pre-Golgi vesicular carriers is the only detectable concentration step in its transport to the TGN. From these results, it is apparent that export from the ER is not exclusively mediated by bulk flow. The ER exerts an unanticipated level of control to insure selective and efficient entry of mature protein into the secretory pathway.