类似的过程介导了哺乳动物细胞和酿酒酵母中糖肽从内质网的输出。
Similar processes mediate glycopeptide export from the endoplasmic reticulum in mammalian cells and Saccharomyces cerevisiae.
作者信息
Römisch K, Ali B R
机构信息
Medical Research Council Laboratory for Molecular Cell Biology and Department of Biochemistry, University College London, Gower Street, London WC1E 6BT, United Kingdom.
出版信息
Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6730-4. doi: 10.1073/pnas.94.13.6730.
Abstract
Glycopeptides are transported from the lumen of the yeast endoplasmic reticulum (ER) to the cytosol and in contrast to secretory proteins do not enter ER-to-Golgi transport vesicles. In a cell-free system, this process is ATP- and cytosol-dependent. While yeast cytosol promotes the export of glycopeptides from mammalian ER in vitro, glycopeptide release cannot be detected in the presence of mammalian cytosol. We demonstrate that this is due to an N-glycanase activity in mammalian cytosol rather than lack of glycopeptide transport activity in mammalian microsomes. Monitoring the amount of glycopeptide enclosed in ER membranes we show the cytosol- and ATP-dependent release of glycopeptide from mammalian microsomes. The fact that glycopeptide export can be achieved with ER and cytosol derived from heterologous sources indicates that glycopeptide export from the ER is an important process conserved during evolution.
摘要
糖肽从酵母内质网（ER）腔转运至细胞质溶胶，与分泌蛋白不同，它们不会进入内质网到高尔基体的运输小泡。在无细胞体系中，此过程依赖于ATP和细胞质溶胶。虽然酵母细胞质溶胶在体外能促进糖肽从哺乳动物内质网中输出，但在存在哺乳动物细胞质溶胶的情况下却检测不到糖肽的释放。我们证明这是由于哺乳动物细胞质溶胶中的N - 聚糖酶活性，而非哺乳动物微粒体中缺乏糖肽转运活性。通过监测内质网膜中封闭的糖肽量，我们显示了糖肽从哺乳动物微粒体中依赖于细胞质溶胶和ATP的释放。糖肽输出可通过来自异源的内质网和细胞质溶胶实现，这一事实表明从内质网输出糖肽是进化过程中保守的重要过程。
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Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6730-4. doi: 10.1073/pnas.94.13.6730.
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