This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor 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
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