Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles
Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles
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DOI：
10.1126/science.1065224
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发表时间：
2001-11-16
期刊：
影响因子：
56.9
通讯作者：
Barlowe, C
中科院分区：
文献类型：
--
作者：
Belden, WJ;Barlowe, C
蛋白质从内质网（ER）转运到由外壳蛋白复合物II（COPII）形成的囊泡中。可溶性分泌蛋白被认为是通过“整体流动”或通过假设的穿梭受体的识别而离开这些囊泡中的ER。我们发现，Erv 29 p，一个保守的跨膜蛋白，直接需要包装糖基化前α因子（gp α f）到COPII囊泡在酿酒酵母。此外，从ER衍生的转运囊泡中分离Erv 29 p-gp α f复合物。在体内，gpaf从ER的输出是饱和的，并且依赖于Erv 29 p的表达水平。这些结果表明，膜受体可以连接可溶性货物蛋白的COPII涂层。
Proteins are transported from the endoplasmic reticulum (ER) in vesicles formed by coat protein complex II (COPII). Soluble secretory proteins are thought to leave the ER in these vesicles by "bulk flow" or through recognition by hypothetical shuttling receptors. We found that Erv29p, a conserved transmembrane protein, was directly required for packaging glycosylated pro-alpha -factor (gp alphaf) into COPII vesicles in Saccharomyces cerevisiae. Further, an Erv29p-gp alphaf complex was isolated from ER-derived transport vesicles. In vivo, export of gpaf from the ER was saturable and depended on the expression level of Erv29p. These results indicate that membrane receptors can link soluble cargo proteins to the COPII coat.