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

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。可溶性蛋白质进入内质网的分泌途径，然后进入高尔基复合体。如果它们没有特定的分类信息，它们就会离开高尔基体，分泌到细胞外部。因此，从这种大量流动中分离出来，既需要可溶性蛋白质携带信号，也需要完整的膜受体蛋白质识别信号，并将可溶性蛋白质拉入囊泡，将其带到不同的目的地。不知何故，在植物高尔基体中，一个受体(BP80)识别一种类型的信号，并将一种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，将另一种不同的可溶性蛋白质拉入蛋白质储存液泡途径。类似的过程也发生在哺乳动物高尔基复合体中，除了裂解途径的受体是甘露糖-6-磷酸受体和山梨素。为了了解这种复杂但决定性的分选机制，我们决定解决受体分子的晶体结构。

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.