Protein sorting upon exit from the endoplasmic reticulum
Protein sorting upon exit from the endoplasmic reticulum
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DOI：
10.1016/s0092-8674(01)00215-x
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发表时间：
2001-01-26
期刊：
影响因子：
64.5
通讯作者：
Riezman, H
中科院分区：
文献类型：
--
作者：
Muñiz, M;Morsomme, P;Riezman, H
目前认为，所有的分泌蛋白都一起进入高尔基体，在那里它们被分类到不同的目的地。然而，酵母中gpi锚定蛋白从内质网运输到高尔基体的特殊要求可以解释为蛋白质分选发生在该途径的早期。通过体外实验重建内质网单轮出芽，我们发现gpi锚定蛋白和其他分泌蛋白以不同的囊泡形式离开内质网。因此，gpi锚定蛋白在分泌途径的早期阶段就与其他蛋白，特别是其他质膜蛋白进行了分类。这些结果对蛋白质退出内质网的机制具有广泛的意义。
It is currently thought that all secretory proteins travel together to the Golgi apparatus where they are sorted to different destinations. However, the specific requirements for transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in yeast could be explained if protein sorting occurs earlier in the pathway. Using an in vitro assay that reconstitutes a single round of budding from the endoplasmic reticulum, we found that GPI-anchored proteins and other secretory proteins exit the endoplasmic reticulum in distinct vesicles. Therefore, GPI-anchored proteins are sorted from other proteins, in particular other plasma membrane proteins, at an early stage of the secretory pathway. These results have wide implications for the mechanism of protein exit from the endoplasmic reticulum.