YEAST TWO-HYBRID INTERACTIONS WITH EXOCYST SUBUNIT DOMAINS

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。在质膜上特定位置的极化胞吐需要一种保守的，叫做胞囊的八个亚基蛋白复合物。在SNARE介导的膜融合之前，分泌部位的囊泡组装对于将囊泡系在质膜上至关重要。我们的目标是单个和组合酵母胞囊亚基的分子特征，以阐明胞囊复合物的功能。为此，我们对几个囊胞亚基的生物化学和结构域进行了表征。我们将使用这些单独的结构域来测试新的相互作用使用酵母双杂交试验。

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. Polarized exocytosis at specific sites on the plasma membrane requires a conserved, eight-subunit protein complex called the exocyst. Exocyst assembly at sites of secretion is essential for tethering the vesicle to the plasma membrane, prior to SNARE¿¿mediated membrane fusion. Our goal is the molecular characterization of the yeast exocyst subunits individually and in combination in order to elucidate the function of the exocyst complex. Towards this end, we have biochemically and structurally characterized domains of several of the exocyst subunits. We will use these individual domains to test for novel interactions using the yeast two-hybrid assay.