Department of Molecular and Cell Biology and Howard Hughes Medical Institute, University of California-Berkeley, Berkeley, CA 94720, USA.
Mol Biol Cell. 2010 Nov 15;21(22):3781-4. doi: 10.1091/mbc.E10-05-0416.
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.
乔治·帕拉德（George Palade）是细胞生物学和美国细胞生物学会（ASCB）的奠基人之一，他为分析真核细胞中蛋白质的分泌和膜的组装建立了超微结构框架。他的远见激发了一代研究人员探究蛋白质运输的分子机制。我的实验室采用互补的遗传和生化方法来剖析这些途径。我的第一批研究生之一彼得·诺维克（Peter Novick）分离出了酿酒酵母的分泌突变体，通过对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，我们证实酵母细胞使用了一种在所有真核生物中都保守的分泌途径。我们利用一种能够重现分泌途径前半部分的生化反应，来鉴定构成内质网（ER）膜多肽易位通道的 Sec 蛋白（Sec61）和捕获货物蛋白并将其装入从 ER 出芽的运输小泡的细胞质衣被蛋白复合物（COPII）。
