STRUCTURAL STUDY OF THE OUTER SHELL OF THE COPII VESICLE COAT

COPII囊泡外壳的结构研究

• 批准号: 7726251
• 负责人: JONATHAN D GOLDBERG
• 金额: $ 0.76万
• 依托单位: BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-09-18 至 2009-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7726251
• 关键词: Cells; Clathrin; Coated vesicle; Complex; Computer Retrieval of Information on Scientific Projects Database; Endoplasmic Reticulum; Funding; Golgi Apparatus; Grant; Image; Institution; Membrane; Object Attachment; Paper; Proteins; Publishing; Research; Research Personnel; Resources; SNAP receptor; Series; Source; Structure; Transport Vesicles; United States National Institutes of Health; Yeasts; interest

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. This is the third in a series of proposals that aims at obtaining structural information on the yeast COPII vesicalar coat. COPII is a 420 kDa pentameric complex responsible for budding transport vesicles from the endoplasmic reticulum (ER) and delivering the specific cargo contents to the Golgi complex. In the first proposal we focused on the inner shell of the COPII coat, the Sec23/24-Sar1 complex. We were able to determine the structures of three complexes of Sec24 bond to cargo and SNARE sequences (paper published in Cell). In the current proposal we focus on the outer shell of COPII , comprising of the Sec13/31 complex. Sec 13/31 is functionally, but not structurally, homolosous to clathrin--it polymerizes the COPII inner shell on the ER membrane and causes membrane deformation. Since, like clathrin, Sec13/31 is a long, flexible structure capable of oligomerizing (as seen in EM images) it is unlikely that the intact complex can be crystallized. There fore, we have dessected the protein into waht we believe are the tow functionally interesting fragments, and these constitue the two projects that we propose in this application.

这个子项目是许多利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 这是一系列旨在获得酵母COPII囊泡外壳结构信息的建议中的第三个。 COPII是一个420 kDa的五聚体复合物，负责从内质网（ER）出芽运输囊泡，并将特定的货物内容物递送到高尔基复合体。 在第一个提案中，我们专注于COPII涂层的内壳，Sec 23/24-Sar 1复合物。 我们能够确定Sec 24键与货物和SNARE序列的三种复合物的结构（发表在Cell上的论文）。 在目前的提案中，我们侧重于COPII的外壳，包括Sec 13/31复合体。 Sec 13/31在功能上而不是结构上与网格蛋白同源-它使ER膜上的COPII内壳聚合并引起膜变形。 因为，像网格蛋白，Sec 13/31是一个长的，灵活的结构，能够寡聚化（如EM图像所示），它是不可能的，完整的复合物可以结晶。 因此，我们将蛋白质切割成我们认为是两个功能上有趣的片段，这两个片段构成了我们在本申请中提出的两个项目。