STRUCTURAL STUDIES FOR THE EXOCYST COMPLEX

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 在真核生物中，细胞的极性是通过将囊泡定向输送到细胞膜上的不同位置来维持的，并要求囊泡识别它将与之融合的靶膜。这种识别是由大的蛋白质复合体介导的。这种复合体存在于细胞内的不同隔室，包括高尔基体、液泡和内小体，以及质膜上。在萌芽酵母中，一种称为胞囊的多蛋白复合体将分泌囊泡连接到质膜上。该实验室对胞囊的组装和功能很感兴趣。由于我们还不能准备足够数量的组装外囊用于结晶，我们已经开始了对单个亚基的结构研究。目前，我们已经结晶了Exo70亚单位，这是最早定位于胞吐作用部位的胞囊成分之一，整个多聚体复合体将围绕着它组装。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Cell polarity in eukaryotes is maintained through the targeted delivery of vesicles to distinct locations on the cell membrane and requires that the vesicle recognize the target membrane with which it will fuse. This recognition is mediated by large protein complexes. Such complexes have been identified in various compartments within the cell, including the Golgi apparatus, vacuoles, and endosomes, as well as on the plasma membrane. In the budding yeast Saccharomyces cerevisiae, a multiprotein complex called the exocyst tethers secretory vesicles to the plasma membrane. The lab is interested in exocyst assembly and function. Since we cannot yet prepare sufficient quantities of assembled exocyst for crystallization, we have started structural studies on individual subunits. Currently, we have crystallized the exo70 subunit, one of the first exocyst components to localize to the site of exocytosis, around which the entire multimeric complex will assemble.