MOLECULAR AGGREGATION OF UPAR

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目及 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。 在作为尿激酶纤溶酶原激活物受体（uPAR）的相互作用候选物的蛋白质中，玻连蛋白（Vn）被认为特异性地决定细胞膜上的uPAR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募集用于细胞粘附。或者，不结合uPAR的Fn包被不应诱导细胞粘附位点处受体的二聚化。 将使用HEK 293细胞中与uPAR-mRFP 1共转染的uPAR-GFP的TCSPC衰变的新相量-FLIM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