MOLECULAR AGGREGATION OF UPAR

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。 在与尿激酶型纤溶酶原激活剂受体(UPAR)相互作用的候选蛋白中，Vitronectin(VN)被认为特异性地决定了uPAR在细胞膜上的单体-二聚体交换和动力学。 当表达uPAR的细胞接种在VN包被的平板上时，uPAR的二聚体应该形成并被招募用于细胞黏附。或者，FN的涂层不结合uPAR，不应该在细胞的黏附位置诱导受体的二聚化。 在HEK293细胞中，将使用与uPAR-mRFP1共转染的uPAR-GFP的TCSPC衰变的新相量分析来检测二聚体

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. Among the proteins that are interacting candidates of the Urokinase Plasminogen Activator Receptor (uPAR), vitronectin (Vn) is thought to specifically dictate the uPAR monomer-dimer exchange and dynamics at the cell membrane. When cells expressing uPAR are seeded on Vn coated plates, dimers of uPAR should form and be recruited for cell adhesion. Alternatively, coating of Fn, which does not bind uPAR, should not induce the dimerization of the receptor at the adhesion sites of the cell. Dimers will be detected using the new phasor-FLIM analysis of TCSPC decays of uPAR-GFP co-transfected with uPAR-mRFP1 in HEK293 cells