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首页> 外文期刊>Molecular biology of the cell >Oligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesicles
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Oligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesicles

机译：货物受体的寡聚化将蛋白质分选到COPII涂层的运输小泡中

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Secretory proteins are transported from the endoplasmic reticulum (ER) to the Golgi complex in vesicles coated with coat protein complex II (COPII). The incorporation of certain transport molecules (cargo) into the COPII vesicles is thought to be mediated by cargo receptors. Here we show that Emp47p, a type-I membrane protein, is specifically required for the transport of an integral membrane protein, Emp46p, from the ER. Exit of Emp46p from the ER was saturable and dependent on the expression level of Emp47p. Emp46p binding to Emp47p occurs in the ER through the coiled-coil region in the luminal domains of both Emp47p and Emp46p, and dissociation occurs in the Golgi. Further, this coiled-coil region is also required for Emp47p to form an oligomeric complex of itself in the ER, which is essential for exit of Emp47p from the ER. Our results suggest that Emp47p is a receptor protein for Emp46p that allows for the selective transport of this protein, and this event involves receptor oligomerization. [References: 30]
机译：分泌蛋白从内质网（ER）转运到被膜蛋白复合物II（COPII）包被的囊泡中的高尔基复合体。某些转运分子（货物）掺入COPII囊泡中被认为是由货物受体介导的。在这里，我们显示Emp47p（一种I型膜蛋白）是从ER转运完整膜蛋白Emp46p所特有的。 Emp46p从ER退出是可饱和的，并取决于Emp47p的表达水平。 Emp46p与Emp47p的结合在ER中通过Emp47p和Emp46p的腔结构域中的螺旋线圈区域发生，而解离发生在高尔基体中。此外，Emp47p在ER中形成其自身的寡聚复合物也需要该螺旋线圈区域，这对于Emp47p从ER退出至关重要。我们的结果表明Emp47p是Emp46p的受体蛋白，允许该蛋白的选择性转运，并且此事件涉及受体寡聚。 [参考：30]

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