Charting the secretory pathway in a simple eukaryote.
Charting the secretory pathway in a simple eukaryote.
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DOI：
10.1091/mbc.e10-05-0416
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发表时间：
2010-11-15
影响因子：
3.3
通讯作者：
Schekman R
中科院分区：
文献类型：
--
作者：
Schekman R
细胞生物学和美国细胞生物学学会 (ASCB) 的创始人 George Palade 建立了超微结构框架，用于分析真核细胞中蛋白质的分泌和细胞膜的组装方式。他的愿景激励了一代研究人员探索蛋白质运输的分子机制。我的实验室通过互补的遗传和生化方法剖析了这些途径。 Peter Novick，我的第一批研究生之一，分离了酿酒酵母的分泌突变体，并通过单突变体和双突变体的细胞学分析以及相应 SEC 基因的分子克隆，我们确定酵母细胞使用在所有真核生物中基本保守的分泌途径。使用概括分泌途径前半部分的生化反应来表征 Sec 蛋白，该蛋白包含内质网 (ER) 膜 (Sec61) 中的多肽易位通道和将货物蛋白捕获到从 ER 出芽的转运囊泡中的细胞质外壳蛋白复合物 (COPII)。
George Palade, a founding father of cell biology and of the American Society for Cell Biology (ASCB), established the ultrastructural framework for an analysis of how proteins are secreted and membranes are assembled in eukaryotic cells. His vision inspired a generation of investigators to probe the molecular mechanisms of protein transport. My laboratory has dissected these pathways with complementary genetic and biochemical approaches. Peter Novick, one of my first graduate students, isolated secretion mutants of Saccharomyces cerevisiae, and through cytological analysis of single and double mutants and molecular cloning of the corresponding SEC genes, we established that yeast cells use a secretory pathway fundamentally conserved in all eukaryotes. A biochemical reaction that recapitulates the first half of the secretory pathway was used to characterize Sec proteins that comprise the polypeptide translocation channel in the endoplasmic reticulum (ER) membrane (Sec61) and the cytoplasmic coat protein complex (COPII) that captures cargo proteins into transport vesicles that bud from the ER.