STRUCTURAL STUDIES OF 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。 我们将确定Rab GTPase Sec4与其鸟嘌呤交换因子Sec2之间的络合物的结构。该结构有望对Rab家族的GTP酶如何催化鸟嘌呤交换产生第一个机械性的见解。目前有一种已知的结构作用于Rab GTPase(Rabex5的Vps9结构域)，还没有与Rab GTPase形成复合体的结构。我们的机械论洞察力将通过突变来检验。Sec4 GTP酶在胞囊连接复合体的组装过程中起着关键作用，在胞吐作用中起着关键作用。

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. We will determine the structure of the complex between the Rab GTPase Sec4 and its guanine exchange factor Sec2. The structure is expected to yield the first mechanistic insights as to how guanine exchange is catalysed for the Rab family of GTPases. There is at present one known structure for a GEF that acts on a Rab GTPase (Vps9 domain of Rabex5) and no structure of a GEF in complex with a Rab GTPase. Our mechanistic insights will be tested by mutagenesis. The Sec4 GTPase is pivotal in the assembly of the exocyst tethering complex, which plays a key role in exocytosis.