Ligand binding alters dimerization and sequestering of urokinase receptors in raft-mimicking lipid mixtures.

ABSTRACT: Lipid heterogeneities, such as lipid rafts, are widely considered to be important for the sequestering of membrane proteins in plasma membranes, thereby influencing membrane protein functionality. However, the underlying mechanisms of such sequestration processes remain elusive, in part, due to the small size and often transient nature of these functional membrane heterogeneities in cellular membranes. To overcome these challenges, here we report the sequestration behavior of urokinase receptor (uPAR), a glycosylphosphatidylinositol-anchored protein, in a planar model membrane platform with raft-mimicking lipid mixtures of well-defined compositions using a powerful optical imaging platform consisting of confocal spectroscopy XY-scans, photon counting histogram, and fluorescence correlation

SUBMITTER: Ge Y 

PROVIDER: S-EPMC4223190 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature