Michaelis S
Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Semin Cell Biol. 1993 Feb;4(1):17-27. doi: 10.1006/scel.1993.1003.
In eukaryotic cells, most extracellular proteins exit the cell via the classical secretory pathway (ER-->Golgi-->secretory vesicles). A notable exception to this pattern is the Saccharomyces cerevisiae mating pheromone alpha-factor, an isoprenylated, methylated, oligopeptide signaling molecule which uses a distinctly non-classical mechanism for secretion. Export of alpha-factor from the yeast cell is mediated by STE6, a member of the ABC protein superfamily. STE6 is one of the few eukaryotic ABC proteins for which a true physiological substrate is known. The ability to carry out molecular manipulations with ease in yeast, together with the possibility of probing substrate-transporter interactions via genetic analysis, affords an excellent opportunity to rigorously dissect the workings of this ABC family member.
在真核细胞中,大多数细胞外蛋白质通过经典分泌途径(内质网→高尔基体→分泌囊泡)排出细胞。这种模式的一个显著例外是酿酒酵母交配信息素α因子,它是一种异戊二烯化、甲基化的寡肽信号分子,采用一种明显非经典的分泌机制。α因子从酵母细胞的输出由ABC蛋白超家族成员STE6介导。STE6是少数已知真正生理底物的真核ABC蛋白之一。在酵母中能够轻松进行分子操作,以及通过遗传分析探究底物-转运蛋白相互作用的可能性,为严格剖析这个ABC家族成员的作用机制提供了绝佳机会。