STRUCTURAL STUDY OF LIGAND BINDING DOMAIN OF A PLANT VACUOLAR SORTING RECEPTOR

植物液泡分选受体配体结合域的结构研究

• 批准号: 7721878
• 负责人: CHULHEE KANG
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721878
• 关键词: Cells; Complex; Computer Retrieval of Information on Scientific Projects Database; Destinations; Funding; Golgi Apparatus; Grant; IGF Type 2 Receptor; Institution; Ligand Binding Domain; Lytic; Membrane; Pathway interactions; Plants; Process; Proteins; Research; Research Personnel; Resources; Reticulum; Signal Transduction; Sorting - Cell Movement; Source; Structure; United States National Institutes of Health; Vacuole; Vesicle; receptor; sortilin

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. Soluble proteins enter the secretory pathway in the endoplasminc reticulum and then move to the Golgi complex. If they have no specific sorting information on them, they exit the Golgi and are secreted to the cell exterior. Therefore, sorting away from this ?bulk flow? requires both that the soluble protein carries a signal, and that an integral membrane receptor protein recognizes the signal and pulls the soluble protein into a vesicle that will carry it to a different destination. Somehow, within the plant Golgi apparatus, one receptor (BP80) recognizes one type of signal and pulls a soluble protein into the lytic vacuole pathway, while a different receptor (RMR) recognizes a different signal and pulls a different soluble protein into the protein storage vacuole pathway. A similar process occurs in the mammalian Golgi complex, except the lytic pathway receptors are the mannose-6-phosphate receptor and sortilin. In order to understand this complex but decisive sorting mechanism, we have decided to solve the crystal structure of the receptor molecules.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 中心，不一定是研究者的机构。 可溶性蛋白质进入内质网的分泌途径，然后移动到高尔基复合体。如果它们没有特定的分类信息，它们就会离开高尔基体并分泌到细胞外部。因此，要远离这种“大流量”？需要可溶性蛋白携带信号，并且整合膜受体蛋白识别信号并将可溶性蛋白拉入囊泡，将其携带到不同的目的地。不知何故，在植物高尔基体中，一种受体 (BP80) 识别一种类型的信号并将可溶性蛋白质拉入裂解液泡途径，而另一种受体 (RMR) 识别不同的信号并将不同的可溶性蛋白质拉入蛋白质储存液泡途径。类似的过程发生在哺乳动物高尔基复合体中，不同之处在于裂解途径受体是甘露糖-6-磷酸受体和分拣蛋白。为了理解这种复杂但决定性的分选机制，我们决定解析受体分子的晶体结构。